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1
Wang, Hongliang, Fabio Squina, Fernando Segato, et al. "High-Temperature Enzymatic Breakdown of Cellulose." Applied and Environmental Microbiology 77, no. 15 (2011): 5199–206. http://dx.doi.org/10.1128/aem.00199-11.
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ABSTRACTCellulose is an abundant and renewable biopolymer that can be used for biofuel generation; however, structural entrapment with other cell wall components hinders enzyme-substrate interactions, a key bottleneck for ethanol production. Biomass is routinely subjected to treatments that facilitate cellulase-cellulose contacts. Cellulases and glucosidases act by hydrolyzing glycosidic bonds of linear glucose β-1,4-linked polymers, producing glucose. Here we describe eight high-temperature-operating cellulases (TCel enzymes) identified from a survey of thermobacterial and archaeal genomes. Three TCel enzymes preferentially hydrolyzed soluble cellulose, while two preferred insoluble cellulose such as cotton linters and filter paper. TCel enzymes had temperature optima ranging from 85°C to 102°C. TCel enzymes were stable, retaining 80% of initial activity after 120 h at 85°C. Two modes of cellulose breakdown, i.e., with endo- and exo-acting glucanases, were detected, and with two-enzyme combinations at 85°C, synergistic cellulase activity was observed for some enzyme combinations.
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Brumm, Phillip, Phillip Brumm, Dan Xie, et al. "Hydrolysis of Cellulose by Soluble Clostridium Thermocellum and Acidothermus Cellulolyticus Cellulases." Journal of Enzymes 1, no. 1 (2018): 5–19. http://dx.doi.org/10.14302/issn.2690-4829.jen-18-2025.
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The goal of this work was to clone, express, characterize and assemble a set of soluble thermostablecellulases capable of significantly degrading cellulose. We successfully cloned, expressed, and purified eleven Clostridium thermocellum (Cthe) cellulases and eight Acidothermuscellulolyticus(Acel) cellulases. The performance of the nineteen enzymes was evaluated on crystalline (filter paper) and amorphous (PASC) cellulose. Hydrolysis products generated from these two substrates were converted to glucose using beta-glucosidase and the glucose formed was determined enzymatically. Ten of the eleven Cthe enzymes were highly active on amorphous cellulose. The individual enzymes all produced <10% reducing sugar equivalents from filter paper. Combinations of Cthe cellulases gave higher conversions, with the combination of CelE, CelI, CelG, and CelK converting 34% of the crystalline cellulose. All eight Acel cellulases showed endo-cellulase activity and were highly active on PASC. Only Acel_0615 produced more than 10% reducing sugar equivalents from filter paper, and a combination of six Acel cellulases produced 32% conversion. Acel_0617, a GH48 exo-cellulase, and Acel_0619, a GH12 endo-cellulase, synergistically stimulated cellulose degradation by the combination of Cthe cellulases to almost 80%. Addition of both Acel enzymes to the Cthe enzyme mix did not further stimulate hydrolysis. Cthe CelG and CelI stimulated cellulose degradation by the combination of Acel cellulases to 66%.
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Mingardon, Florence, Ang�lique Chanal, Ana M. L�pez-Contreras, Cyril Dray, Edward A. Bayer, and Henri-Pierre Fierobe. "Incorporation of Fungal Cellulases in Bacterial Minicellulosomes Yields Viable, Synergistically Acting Cellulolytic Complexes." Applied and Environmental Microbiology 73, no. 12 (2007): 3822–32. http://dx.doi.org/10.1128/aem.00398-07.
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ABSTRACT Artificial designer minicellulosomes comprise a chimeric scaffoldin that displays an optional cellulose-binding module (CBM) and bacterial cohesins from divergent species which bind strongly to enzymes engineered to bear complementary dockerins. Incorporation of cellulosomal cellulases from Clostridium cellulolyticum into minicellulosomes leads to artificial complexes with enhanced activity on crystalline cellulose, due to enzyme proximity and substrate targeting induced by the scaffoldin-borne CBM. In the present study, a bacterial dockerin was appended to the family 6 fungal cellulase Cel6A, produced by Neocallimastix patriciarum, for subsequent incorporation into minicellulosomes in combination with various cellulosomal cellulases from C. cellulolyticum. The binding of the fungal Cel6A with a bacterial family 5 endoglucanase onto chimeric miniscaffoldins had no impact on their activity toward crystalline cellulose. Replacement of the bacterial family 5 enzyme with homologous endoglucanase Cel5D from N. patriciarum bearing a clostridial dockerin gave similar results. In contrast, enzyme pairs comprising the fungal Cel6A and bacterial family 9 endoglucanases were substantially stimulated (up to 2.6-fold) by complexation on chimeric scaffoldins, compared to the free-enzyme system. Incorporation of enzyme pairs including Cel6A and a processive bacterial cellulase generally induced lower stimulation levels. Enhanced activity on crystalline cellulose appeared to result from either proximity or CBM effects alone but never from both simultaneously, unlike minicellulosomes composed exclusively of bacterial cellulases. The present study is the first demonstration that viable designer minicellulosomes can be produced that include (i) free (noncellulosomal) enzymes, (ii) fungal enzymes combined with bacterial enzymes, and (iii) a type (family 6) of cellulase never known to occur in natural cellulosomes.
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Rohrmann, S., and H. P. Molitoris. "Screening for wood-degrading enzymes in marine fungi." Canadian Journal of Botany 70, no. 10 (1992): 2116–23. http://dx.doi.org/10.1139/b92-263.
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Forty marine and 15 terrestrial fungi in the Ascomycetes, Basidiomycetes, and Deuteromycetes were screened for presence and relative amount of enzymes involved in wood degradation (cellulases and redox enzymes) using seawater and deionized water media. Distribution of cellulases, laccase, tyrosinase, and peroxidase among marine and terrestrial groups of fungi was investigated. β-Glucosidase (C4) and endoglucanase (C3) were the most frequent enzymes (80 – 100% of the strains) of cellulose metabolism. Acid-swollen cellulose (C1) was generally more easily degraded than microcrystalline-dyed Avicel® (C2).All groups of strains showed relatively high percentages of cellulases C1, C3, C4, whereas production of cellulase C2 was lower. In comparison with Sporotrichum pulverulentum, a strongly cellulolytic terrestrial Deuteromycete, about 25% of the marine fungi tested showed the same high cellulase activity. Peroxidase was formed by nearly all strains tested at least on seawater medium; tyrosinase was the least frequent enzyme (20 – 35%). The presence of laccase was different among the various fungal systematic groups, reaching its highest percentages in the marine and terrestrial Basidiomycetes and the marine Ascomycetes, which mostly belong to the ecological groups of white-rot and soft-rot fungi, respectively. Enzymes involved in wood degradation were demonstrated in large number and sometimes considerable amounts in wood-inhabiting marine fungi. Key words: marine fungi, wood degradation, cellulase, phenoloxidases, screening, ecology.
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Metreveli, Eka, Tamar Khardziani, and Vladimir Elisashvili. "The Carbon Source Controls the Secretion and Yield of Polysaccharide-Hydrolyzing Enzymes of Basidiomycetes." Biomolecules 11, no. 9 (2021): 1341. http://dx.doi.org/10.3390/biom11091341.
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In the present study, the polysaccharide-hydrolyzing secretomes of Irpex lacteus (Fr.) Fr. (1828) BCC104, Pycnoporus coccineus (Fr.) Bondartsev and Singer (1941) BCC310, and Schizophyllum commune Fr. (1815) BCC632 were analyzed in submerged fermentation conditions to elucidate the effect of chemically and structurally different carbon sources on the expression of cellulases and xylanase. Among polymeric substrates, crystalline cellulose appeared to be the best carbon source providing the highest endoglucanase, total cellulase, and xylanase activities. Mandarin pomace as a growth substrate for S. commune allowed to achieve comparatively high volumetric activities of all target enzymes while wheat straw induced a significant secretion of cellulase and xylanase activities of I. lacteus and P. coccineus. An additive effect on the secretion of cellulases and xylanases by the tested fungi was observed when crystalline cellulose was combined with mandarin pomace. In I. lacteus the cellulase and xylanase production is inducible in the presence of cellulose-rich substrates but is suppressed in the presence of an excess of easily metabolizable carbon source. These enzymes are expressed in a coordinated manner under all conditions studied. It was shown that the substitution of glucose in the inoculum medium with Avicel provides accelerated enzyme production by I. lacteus and higher cellulase and xylanase activities of the fungus. These results add new knowledge to the physiology of basidiomycetes to improve cellulase production.
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Sher, Hassan, Muhammad Faheem, Abdul Ghani, Rashid Mehmood, Hamza Rehman, and Syed A. I. Bokhari. "OPTIMIZATION OF CELLULASE ENZYME PRODUCTION FROM Aspergillus oryzae FOR INDUSTRIAL APPLICATIONS." World Journal of Biology and Biotechnology 2, no. 2 (2017): 155. http://dx.doi.org/10.33865/wjb.002.02.0088.
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Cellulases are the hydrolytic group of enzymes, responsible for release of sugars in the bioconversion of the cellulosic biomass into a variety of value added industrial products. Fungal isolated cellulases are well studied and playing a significant role in various industrial processes. Enzymatic depolymerisation of cellulosic material has been done by the various fungal isolated enzymes. In the present study, the cultivation conditions for cellulase production from Aspergillus species were optimized. Optimization of scarification conditions such as time course, inoculum size, carbon source and concentration, nitrogen source, various pH levels were performed for the production of extracellular carboxymethyl cellulase and endoglucanase enzyme. The result exhibited, 15 % inoculums size, corncobs 2 % concentration, Urea and medium pH 7 at 30oC supported high yield of carboxymethyl cellulase (38.80 U/ml/min) and exoglucanase enzyme (10.94 U/ml/min) through a submerged fermentation (SmF). In future biotechnological applications in cellulase enzyme production attain a vital role to obtain high degradable yield.
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DAS, ARPAN, TANMAY PAUL, SUMAN KUMAR HALDER, et al. "Study on Regulation of Growth and Biosynthesis of Cellulolytic Enzymes from Newly Isolated Aspergillus fumigatus ABK9." Polish Journal of Microbiology 62, no. 1 (2013): 31–43. http://dx.doi.org/10.33073/pjm-2013-004.
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This study was aimed to evaluate the pattern of cellulase biosynthesis from Aspergillusfumigatus ABK9 under submerged fermentation. Production was increased concomitantly with fungal growth up to 72 h and reached maximum (Xmax -6.72 g/l) with specific growth rate (mu max) of 0.126/h. Highest specific rate of enzyme production (q ) was found at initial medium pH of 5.0 and incubation temperature of 30 degrees C. At the same time, in the presence of 2-deoxy-D-glucose concentration of 0.5 mg/ml, the production of cellulolytic enzymes, viz, carboxymethyl cellulase activity (CMCase), filter paper degrading activity (FPase) and P-glucosidase activity reached maximum of 132.2, 21.3 and 28.9 U/ml, respectively. Cellulase biosynthesis was induced in respect to higher volumetric production rate (Qp), specific rate of enzymes production (qp, U/g biomass/h) and enzyme/biomass yield (YE/X) when grown in carboxymethyl cellulose in comparison to other saccharides as sole carbon source. Induction ratios (IR) of cellulases were between 12.3 and 24.4 in the presence of 1.5% (w/v) CMC in the culture media. The strain was quite resistant to catabolic repression by glucose up to 0.4% (w/v). Cellulases production was greatly influenced in the presence of yeast extract and potassium dihydrogen phosphate (KH2POA) as nitrogen and phosphate sources in the culture media. C/N ratio of 10.0 and C/P ratio of 4.0 proved to be the best for the production of enzyme cocktail. Along with the high production yield, the crude enzymes showed a promising cellulose hydrolyzing efficiency of rice straw, indicating the enzyme could be beneficial for its large scale industrial exploitation.
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Igarashi, Kiyohiko, Takayuki Uchihashi, Anu Koivula, et al. "Traffic Jams Reduce Hydrolytic Efficiency of Cellulase on Cellulose Surface." Science 333, no. 6047 (2011): 1279–82. http://dx.doi.org/10.1126/science.1208386.
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A deeper mechanistic understanding of the saccharification of cellulosic biomass could enhance the efficiency of biofuels development. We report here the real-time visualization of crystalline cellulose degradation by individual cellulase enzymes through use of an advanced version of high-speed atomic force microscopy. Trichoderma reesei cellobiohydrolase I (TrCel7A) molecules were observed to slide unidirectionally along the crystalline cellulose surface but at one point exhibited collective halting analogous to a traffic jam. Changing the crystalline polymorphic form of cellulose by means of an ammonia treatment increased the apparent number of accessible lanes on the crystalline surface and consequently the number of moving cellulase molecules. Treatment of this bulky crystalline cellulose simultaneously or separately with T. reesei cellobiohydrolase II (TrCel6A) resulted in a remarkable increase in the proportion of mobile enzyme molecules on the surface. Cellulose was completely degraded by the synergistic action between the two enzymes.
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Poomai, Nutt, Wilailak Siripornadulsil, and Surasak Siripornadulsil. "Cellulase Enzyme Production from Agricultural Waste by Acinetobacter sp. KKU44." Advanced Materials Research 931-932 (May 2014): 1106–10. http://dx.doi.org/10.4028/www.scientific.net/amr.931-932.1106.
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Due to a high ethanol demand, the approach for effective ethanol production is important and has been developed rapidly worldwide. Several agricultural wastes are highly abundant in celluloses and the effective cellulase enzymes do exist widely among microorganisms. Accordingly, the cellulose degradation using microbial cellulase to produce a low-cost substrate for ethanol production has attracted more attention. In this study, the cellulase producing bacterial strain has been isolated from rich straw and identified by 16S rDNA sequence analysis as Acinetobacter sp. KKU44. This strain is able to grow and exhibit the cellulase activity. The optimal temperature for its growth and cellulase production is 37 °C. The optimal temperature of bacterial cellulase activity is 60 °C. The cellulase enzyme from Acinetobacter sp. KKU44 is heat-tolerant enzyme. The bacterial culture of 36 h. showed highest cellulase activity at 120 U/mL when grown in LB medium containing 2% (w/v). The capability of Acinetobacter sp. KKU44 to grow in cellulosic agricultural wastes as a sole carbon source and exhibiting the high cellulase activity at high temperature suggested that this strain could be potentially developed further as a cellulose degrading strain for a production of low-cost substrate used in ethanol production.
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Idiawati, Nora, Elliska Murni Harfinda, and Lucy Arianie. "Produksi Enzim Selulase olehAspergillus niger pada Ampas Sagu." Jurnal Natur Indonesia 16, no. 1 (2015): 1. http://dx.doi.org/10.31258/jnat.16.1.1-9.
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Production of cellulase by Aspergillus niger was carried out by growing the cultureson sago waste. Sago waste containscellulose that has not been used optimally. Cellulose is a polysaccharide consisting of glucose monomers linked by β-1,4-glycosides bonds. Glycoside bonds in cellulose can be enzymatically hydrolyzed into glucose with cellulase enzymes. Solid fermentation used to produce cellulase on sago waste as substrate was influenced by pH (3 to 6), moisture content(40% to 85%), and fermentation time (4 to 10 days). Products of the cellulase enzyme activity was measured by phenolsulfuricacid method. The results showed that the highest cellulase enzyme activity was 0.172 U/mL obtained at 85%moisture content, pH 5, and 8 days of fermentation time.
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Isheanesu Dzambi and Rumbidzai Mangoyi. "The effects of Psidium guajava leaf extract on the production of cellulases and glucose oxidases by Aspergillus niger." GSC Advanced Research and Reviews 5, no. 2 (2020): 118–22. http://dx.doi.org/10.30574/gscarr.2020.5.2.0109.
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Aspergillus niger, is a filamentous fungus and producer of industrial enzymes such as glucose oxidases and cellulases. These enzymes are naturally produced by the fungus in order to digest and absorb nutrients from its environment. However, the enzyme quantities that are naturally produced are low. Thus, the aim of this study was to determine the effects of Psidum guajava leaf extract on the production of cellulases and glucose oxidases from Aspergillus niger. The leaves of Psidium guajava were extracted using absolute methanol. Aspergillus niger was then grown in the presence and absence of the extract in order to investigate the effects of extract on enzyme production by the fungus. The enzymes secreted into the broth medium were isolated by centrifugation. The supernatant which contained the secreted enzymes was used for the determination of enzyme activity. Enzyme activity was determined using the specific substrate for the specific enzyme, such as 2 % cellulose for cellulase and standard glucose solution for glucose oxidase. The results showed that the Psidium guajava leaf extract had an effect on production and activity of cellulases and glucose oxidases. From this study, it was noted that the Psidium guajava leaf extract may be used to induce the production of enzymes by Aspergillus niger and these enzymes may be of industrial use.
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Lynd, Lee R., Paul J. Weimer, Willem H. van Zyl, and Isak S. Pretorius. "Microbial Cellulose Utilization: Fundamentals and Biotechnology." Microbiology and Molecular Biology Reviews 66, no. 3 (2002): 506–77. http://dx.doi.org/10.1128/mmbr.66.3.506-577.2002.
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SUMMARY Fundamental features of microbial cellulose utilization are examined at successively higher levels of aggregation encompassing the structure and composition of cellulosic biomass, taxonomic diversity, cellulase enzyme systems, molecular biology of cellulase enzymes, physiology of cellulolytic microorganisms, ecological aspects of cellulase-degrading communities, and rate-limiting factors in nature. The methodological basis for studying microbial cellulose utilization is considered relative to quantification of cells and enzymes in the presence of solid substrates as well as apparatus and analysis for cellulose-grown continuous cultures. Quantitative description of cellulose hydrolysis is addressed with respect to adsorption of cellulase enzymes, rates of enzymatic hydrolysis, bioenergetics of microbial cellulose utilization, kinetics of microbial cellulose utilization, and contrasting features compared to soluble substrate kinetics. A biological perspective on processing cellulosic biomass is presented, including features of pretreated substrates and alternative process configurations. Organism development is considered for “consolidated bioprocessing” (CBP), in which the production of cellulolytic enzymes, hydrolysis of biomass, and fermentation of resulting sugars to desired products occur in one step. Two organism development strategies for CBP are examined: (i) improve product yield and tolerance in microorganisms able to utilize cellulose, or (ii) express a heterologous system for cellulose hydrolysis and utilization in microorganisms that exhibit high product yield and tolerance. A concluding discussion identifies unresolved issues pertaining to microbial cellulose utilization, suggests approaches by which such issues might be resolved, and contrasts a microbially oriented cellulose hydrolysis paradigm to the more conventional enzymatically oriented paradigm in both fundamental and applied contexts.
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Shafique, Shazia, Rukhsana Bajwa, and Sobiya Shafique. "Mutagenesis and Genotypic Characterization of Aspergillus niger FCBP-02 for Improvement in Cellulolytic Potential." Natural Product Communications 4, no. 4 (2009): 1934578X0900400. http://dx.doi.org/10.1177/1934578x0900400423.
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Cellulase is a collective term that encompasses enzymes which catalyze reactions that participate in the degradation of insoluble cellulose to soluble carbohydrates. In the present study, production of extra cellular cellulases by a filamentous fungus, Aspergillus niger FCBP-02, was studied in solid-state fermentation (SSF) as well as in submerged fermentation (SmF). Trials were conducted to evaluate the effect of mutagenesis by UV irradiation (5–40 min) and ethyl methane sulfonate (EMS) treatment (50–300 μg mL−1) to obtain hyper active cellulase enzyme producers among the potential strains. The enzyme activity assays of parental and mutant strains clearly revealed significantly higher cellulase activity of mutant A-Ch-5.5 (96 Units mL−1), followed by A-UV-5.6 (71 Units mL−1) with respect to the wild strain of A. niger FCBP–02 (53.7 Units mL−1). The profile of genetic variability among wild and mutant derivatives was scrutinized through RAPD–PCR. The expression pattern of mutants exhibited that the mutants were isogenic variants of the wild type and the out performance of the mutants could be attributed to the change in genetic make up.
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Rahman, M. M., U. F. Shahjadee, F. Khanam, A. Z. Rupa та M. A. K. Azad. "Effect of chemical agents, metallic salts on the stability of α-amylase, protease and comparative analyses of enzyme activity of selected salad vegetables". Food Research 4, № 4 (2020): 1066–70. http://dx.doi.org/10.26656/fr.2017.4(4).259.
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The present investigation was conducted to analyze the activity of enzymes (protease, αamylase, cellulase and urease) of selected salad vegetables (white radish, red radish, beet, carrot, papaya, cucumber and tomato) as well as to determine the effect of chemical agents and metallic salts on the stability of enzymes. Salad vegetables are one of the cheap sources of adequate vitamins, minerals and enzymes. The protease, α-amylase and cellulase activity were highest in papaya (4.11±0.21 U/g, 1.68±0.21 U/g and 0.26±0.13 U/ g) whereas the urease activity was not detected in papaya, cucumber and tomato. The protease, α-amylase and cellulase activity of papaya were increased 24.83%, 42.26% and 57.69% than cucumber while the cellulase activity of carrot was increased 44.45% than tomato. The activity of protease and α-amylase of beet were decreased 52.44%, 33.63% while the cellulase activity of beet was increased 36.36% from radish. The toxicity indicating urease enzyme activity was not detected in papaya, tomato and cucumber but negligible in radish, beet and carrot which can be nullified. The activities of enzymes were increased in the presence of metallic salts such as Ca2+, Mg2+ and Mn2+ while Fe2+, Zn2+ and Cu2+ inhibited the enzyme's activity moderately. Results revealed that in the presence of higher concentrations of urea, EDTA and acetic acid, the activities of all the enzymes were completely inhibited.
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Legodi, L. M., D. La Grange, E. L. Jansen van Rensburg, and I. Ncube. "Isolation of Cellulose Degrading Fungi from Decaying Banana Pseudostem and Strelitzia alba." Enzyme Research 2019 (July 25, 2019): 1–10. http://dx.doi.org/10.1155/2019/1390890.
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Cellulases are a group of hydrolytic enzymes that break down cellulose to glucose units. These enzymes are used in the food, beverage, textile, pulp, and paper and the biofuel industries. The aim of this study was to isolate fungi from natural compost and produce cellulases in submerged fermentation (SmF). Initial selection was based on the ability of the fungi to grow on agar containing Avicel followed by cellulase activity determination in the form of endoglucanase and total cellulase activity. Ten fungal isolates obtained from the screening process showed good endoglucanase activity on carboxymethyl cellulose-Congo Red agar plates. Six of the fungal isolates were selected based on high total cellulase activity and identified as belonging to the genera Trichoderma and Aspergillus. In SmF of synthetic media with an initial pH of 6.5 at 30°C Trichoderma longibrachiatum LMLSAUL 14-1 produced total cellulase activity of 8 FPU/mL and endoglucanase activity of 23 U/mL whilst Trichoderma harzianum LMLBP07 13-5 produced 6 FPU/mL and endoglucanase activity of 16 U/mL. The produced levels of both cellulases and endoglucanase by Trichoderma species were higher than the levels for the Aspergillus fumigatus strains. Aspergillus fumigatus LMLPS 13-4 produced higher β-glucosidase 38 U/mL activity than Trichoderma species.
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Maryanty, Yanty, Fandi Lintang Wahyu Saputra, and Robby Prasetyo. "Pembuatan Asam Laktat dari Selulosa oleh Bakteri Lactobacillus delbrueckii dengan Selulase dari Bakteri Bacillus subtilis dan Bacillus circulans." Jurnal Teknik Kimia dan Lingkungan 4, no. 2 (2020): 153. http://dx.doi.org/10.33795/jtkl.v4i2.179.
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Bakteri asam laktat memanfaatkan gula sebagai sumber energi, pertumbuhan, dan menghasilkan metabolit berupa asam laktat selama proses fermentasi. Gula berupa monomer glukosa dapat diperoleh dari hidrolisis atau pemutusan ikatan pada selulosa. Penelitian ini bertujuan untuk memproduksi asam laktat dari media selulosa menggunakan metode Simultaneous Saccharification and Fermentation (SSF). SSF diharapkan bermanfaat untuk pengembangan produksi asam laktat yang efektif dari limbah lignoselulosa. Pada tahap pertama, selulosa digunakan oleh Bacillus subtilis dan Bacillus circulans untuk memproduksi enzim selulase. Tahap kedua, enzim selulase kemudian digunakan untuk sakarifikasi selulosa menghasilkan glukosa. Glukosa yang diperoleh difermentasi oleh Lactobacillus delbrueckii menghasilkan asam laktat. Proses pada tahap kedua ini terjadi secara simultan, setelah itu proses fermentasinya digunakan metode SSF, dengan variasi konsentrasi enzim selulase untuk proses sakarifikasi berasal dari Bacillus subtilis dan Bacillus circulans. Proses awal pembuatan enzim selulase menggunakan bakteri Bacillus subtilis dan Bacillus circulans sebagai variabel dan waktu inkubasi selama 84 jam. Enzim selulase selanjutnya digunakan untuk mendegradasi media selulosa dalam proses SSF menjadi glukosa yang selanjutnya akan difermentasi oleh Lactobacillus delbrueckii. Pada proses SSF dengan inokulum Bacillus circulans diperoleh asam laktat tertinggi pada kadar enzim selulase 10% yaitu 1,29% dan dengan inokulum Bacillus subtilis pada kadar enzim selulase 5% yaitu 1,24%.Lactic acid bacteria use sugar as an energy source, growth, and produce metabolites in the form of lactic acid during the fermentation process. This research aimed to make lactic acid from cellulose used Simultaneous Saccharification and Fermentation (SSF). Cellulose is composed of glucose monomers. This method is expected to be useful for the development of significant lactic acid production from lignocellulosic waste. In the first stage, cellulose was used by Bacillus subtilis and Bacillus circulans to produce cellulase enzymes. In the second stage, the cellulase enzyme is then used to saccharify cellulose to produce glucose. The glucose fermented by Lactobacillus delbrueckii to produce lactic acid. The fermentation process uses the SSF method with various concentrations of cellulase enzymes. The initial process by making cellulase enzymes first used the bacteria Bacillus subtilis and Bacillus circulans as variables, and the incubation time was 84 hours. The cellulase enzyme is then used to degrade cellulose media in the SSF process into glucose, which will then be fermented by Lactobacillus delbrueckii. In the SSF process with Bacillus circulans inoculum, the highest lactic acid was obtained at 10% cellulase enzyme levels, amounting to 1.29%, and with Bacillus subtilis inoculums at 5% cellulase enzyme levels, amounting to 1.24%.
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Contreras, Francisca, Subrata Pramanik, Aleksandra M. Rozhkova, et al. "Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails." International Journal of Molecular Sciences 21, no. 5 (2020): 1589. http://dx.doi.org/10.3390/ijms21051589.
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Lignocellulosic biomass is a most promising feedstock in the production of second-generation biofuels. Efficient degradation of lignocellulosic biomass requires a synergistic action of several cellulases and hemicellulases. Cellulases depolymerize cellulose, the main polymer of the lignocellulosic biomass, to its building blocks. The production of cellulase cocktails has been widely explored, however, there are still some main challenges that enzymes need to overcome in order to develop a sustainable production of bioethanol. The main challenges include low activity, product inhibition, and the need to perform fine-tuning of a cellulase cocktail for each type of biomass. Protein engineering and directed evolution are powerful technologies to improve enzyme properties such as increased activity, decreased product inhibition, increased thermal stability, improved performance in non-conventional media, and pH stability, which will lead to a production of more efficient cocktails. In this review, we focus on recent advances in cellulase cocktail production, its current challenges, protein engineering as an efficient strategy to engineer cellulases, and our view on future prospects in the generation of tailored cellulases for biofuel production.
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Purba, Nursatria, Ida Bagus Wayan Gunam, and I. Made Mahaputra Wijaya. "Produksi Enzim Selulase Kasar dari Isolat Bakteri B2S8 menggunakan Substrat Brangkasan Jagung dengan Perlakuan Konsentrasi Inokulum dan Komposisi Media yang berbeda." JURNAL REKAYASA DAN MANAJEMEN AGROINDUSTRI 8, no. 2 (2020): 267. http://dx.doi.org/10.24843/jrma.2020.v08.i02.p11.
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The purpose of this study was determined the media and concentration of cellulolytic bacterial isolates to produce high cellulase enzyme activity. Production of crude cellulase enzyme in media and concentration of different bacterial isolate used a factorial Randomized Block Design (RBD) which consist of two factors. The first factor was the media production of different cellulase enzyme consisting of 3 levels, namely media 1, 2 and 3. The second factor was the concentration of bacterial isolate consisting of 5 levels namely 1, 2, 3, 4 and 5%. This study used a B2S8 cellulolytic bacterial isolate that has the highest value of cellulase enzyme activity and the highest degradation rate of cellulose in previous studied and determined the ability of exoglucanase enzyme activity, endoglucanase enzyme and dissolved protein content produced from cellulolytic bacterial isolate. This study used Carboxymethyl Cellulose (CMC) for enzyme activity test and 1% corn stover as a substrate on the media to produce crude cellulase enzyme. The result showed that the highest cellulase enzyme activity in the third media and 5% cellulolytic bacterial inoculum concentration resulted in endoglucanase activity of 0.0332 IU/mL, exoglucanases enzyme activity of 0.0060 IU/mL, dissolved protein content in the amount of 0.5670 mg/mL, the specific endoglucanase activity of 0.0807 IU/mg and the specific activity of exoglucanase of 0.0123 IU/mg.
 Keywords: Cellulolytic bacteria, Cellulase enzymes, Enzyme activity, Corn stover
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Caspi, Jonathan, Yoav Barak, Rachel Haimovitz, et al. "Effect of Linker Length and Dockerin Position on Conversion of a Thermobifida fusca Endoglucanase to the Cellulosomal Mode." Applied and Environmental Microbiology 75, no. 23 (2009): 7335–42. http://dx.doi.org/10.1128/aem.01241-09.
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ABSTRACT We have been developing the cellulases of Thermobifida fusca as a model to explore the conversion from a free cellulase system to the cellulosomal mode. Three of the six T. fusca cellulases (endoglucanase Cel6A and exoglucanases Cel6B and Cel48A) have been converted in previous work by replacing their cellulose-binding modules (CBMs) with a dockerin, and the resultant recombinant “cellulosomized” enzymes were incorporated into chimeric scaffolding proteins that contained cohesin(s) together with a CBM. The activities of the resultant designer cellulosomes were compared with an equivalent mixture of wild-type enzymes. In the present work, a fourth T. fusca cellulase, Cel5A, was equipped with a dockerin and intervening linker segments of different lengths to assess their contribution to the overall activity of simple one- and two-enzyme designer cellulosome complexes. The results demonstrated that cellulose binding played a major role in the degradation of crystalline cellulosic substrates. The combination of the converted Cel5A endoglucanase with the converted Cel48A exoglucanase also exhibited a measurable proximity effect for the most recalcitrant cellulosic substrate (Avicel). The length of the linker between the catalytic module and the dockerin had little, if any, effect on the activity. However, positioning of the dockerin on the opposite (C-terminal) side of the enzyme, consistent with the usual position of dockerins on most cellulosomal enzymes, resulted in an enhanced synergistic response. These results promote the development of more complex multienzyme designer cellulosomes, which may eventually be applied for improved degradation of plant cell wall biomass.
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Nababan, Monalisa, Ida Bagus Wayan Gunam, and I. Made Mahaputra Wijaya. "PRODUKSI ENZIM SELULASE KASAR DARI BAKTERI SELULOLITIK." JURNAL REKAYASA DAN MANAJEMEN AGROINDUSTRI 7, no. 2 (2019): 190. http://dx.doi.org/10.24843/jrma.2019.v07.i02.p03.
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The purpose of this research was to elucidate the potentials of cellulolytic bacteria isolates in producing crude cellulose enzymes and to determine the ability of exoglucanase enzymes and endoglucanase enzymes produced from selected cellulolytic bacteria isolates. Ten potential isolates from previous research were confirmed using 1% Carboxymethyl Cellulose (CMC) media with the addition of Congo red and four potential isolates were obtained which then crude cellulose production and enzyme activity tests were carried out using cellulose substrates such as Carboxymethyl Cellulose (CMC), and Filter Paper (FP) Whattman number 1. The exoglucanase enzyme activity was obtained between 0.069 IU/mL to 0.072 IU/mL. The activity test of endoglucanase enzyme was obtained between 0.069 IU / mL to 0.074 IU/mL. Cellulose degradation was obtained between 3.32% to 11.37%. Isolate that have the highest enzymatic activity and cellulose degradation ability was B2S8.
 Keywords: Cellulolytic bacteria, Cellulase enzyme, Enzyme activity, Congo red.
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Liu, Hui Qin, Yue Feng, Jian Xin Jiang, and Li Wei Zhu. "Enzymatic Hydrolysis of Furfural Residues Using Crude Trichoderma cellulases." Advanced Materials Research 236-238 (May 2011): 452–55. http://dx.doi.org/10.4028/www.scientific.net/amr.236-238.452.
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The aim of this study was to compare the hydrolytic potential of the cellulase produced byTrichoderma pseudokoningiiand byTrichoderma koningiiin the enzymatic hydrolysis of furfural residues with different cellulose content. The results showed that the glucose yield was improved by increasing the cellulose of the substrates. The maximum glucose yield of 83.7% was obtained when the substrates with cellulose content of 94.92%, which was hydrolyzed by the enzymes produced byTrichoderma pseudokoningii.The cellulolytic enzyme fromTrichoderma pseudokoningiiwas found to have a high hydrolysis capability to the furfural residues and it possessed more efficient adsorption and desorption on the substrates. There was the nonproductive cellulase adsorption onto lignin in the enzymatic hydrolysis of the furfural residues by the cellulase preparations fromT.strains.
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Gea, Saharman, Noni Oktari, Andriayani Andriayani, Sri Rahayu, and Averroes F. Piliang. "Comparative Optimization of Cellulase and Laccase Enzymes in Deinking Process of Used Newspapers." Jurnal Kimia Sains dan Aplikasi 23, no. 10 (2020): 353–59. http://dx.doi.org/10.14710/jksa.23.10.353-359.
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The use of enzymes in the bio-deinking process of newspaper waste has promising potential. However, investigations on the concentration of enzyme combinations need to be carried out to obtain the optimum ratio of cellulase and laccase enzymes for the bio-deinking process of recycled newspapers. The mixture of the two enzymes at various ratios was used to remove the ink on paper pulp from used newspapers by mechanical disintegration method treatment and followed by the bio-deinking process in an incubator shaker. The characterization of functional groups, structures, and thermal properties of bio-deinked pulp paper was carried out by FTIR, XRD, DTG/TGA, and an analysis of the degree of brightness to the prepared paper. FTIR results confirmed three main components of papers, such as cellulose, hemicellulose, and lignin. The XRD results showed that the equal ratio of cellulase and laccase enzymes had an effect on a higher crystallinity index, which was 78.8% compared to those obtained from the conventional methods with a crystallinity index of 69.7%. Thermal analysis showed that the optimum combination of both enzymes contributed the most at the highest temperature where the rate of degradation decreased. Brightness analysis showed that bio-deinking had met the quality requirements for newsprint paper in SNI 7273:2008. Our findings show that the combination of cellulase and laccase enzymes at the same ratio can produce optimal bio-deinked pulp for paper fabrication with excellent characteristics in brightness, thermal, and physical properties.
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Chatterjee, Soumya, Sonika Sharma, Rajesh Kumar Prasad, et al. "Cellulase Enzyme based Biodegradation of Cellulosic Materials: An Overview." South Asian Journal of Experimental Biology 5, no. 6 (2016): 271–82. http://dx.doi.org/10.38150/sajeb.5(6).p271-282.
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Cellulose, a macromolecule of β -D- anhydroglucopyranose units linked by β (1,4)-glycosidic bonds, is the world’s most abundant organic polymer and is the main component of plant biomass that provides stability. Due to its sta-ble fibrous property, it has become one of the most important commercial raw materials for many industries. However, accumulation of waste cellulose due to natural and/or anthropogenic sources is a matter of concern in terms of environmental pollution. Wastes cellulosic substrates can be utilized as sources of energy through controlled hydrolysis using cellulases- a complex group of enzymes capable of degrading all types of cellulosic waste materials. A number of bacteria, fungi and insects are having the capability to degrade cellulose by production of cellulase enzymes. Further, the symbiotic insect-microbe relationships present in the insect gut microbiome for the production of cellulolytic system is of immense importance as this would lead to applications in different fields like biodegradation of cellulosic wastes, pollution reduction, biofuel production, insect/pest control etc. Cel-lulase gene can also be improved by genetic or protein engineering methods using recent technological advances. This review deals with the advances of cellulase enzymes and its utilization for different application.
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Vazana, Yael, Sarah Moraïs, Yoav Barak, Raphael Lamed, and Edward A. Bayer. "Interplay between Clostridium thermocellum Family 48 and Family 9 Cellulases in Cellulosomal versus Noncellulosomal States." Applied and Environmental Microbiology 76, no. 10 (2010): 3236–43. http://dx.doi.org/10.1128/aem.00009-10.
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ABSTRACT The anaerobic, thermophilic cellulolytic bacterium Clostridium thermocellum is known for its elaborate cellulosome complex, but it also produces a separate free cellulase system. Among the free enzymes, the noncellulosomal enzyme Cel9I is a processive endoglucanase whose sequence and architecture are very similar to those of the cellulosomal enzyme Cel9R; likewise, the noncellulosomal exoglucanase Cel48Y is analogous to the principal cellulosomal enzyme Cel48S. In this study we used the designer cellulosome approach to examine the interplay of prominent cellulosomal and noncellulosomal cellulases from C. thermocellum. Toward this end, we converted the cellulosomal enzymes to noncellulosomal chimeras by swapping the dockerin module of the cellulosomal enzymes with a carbohydrate-binding module from the free enzyme analogues and vice versa. This enabled us to study the importance of the targeting effect of the free enzymes due to their carbohydrate-binding module and the proximity effect for cellulases on the designer cellulosome. C. thermocellum is the only cellulosome-producing bacterium known to express two different glycoside hydrolase family 48 enzymes and thus the only bacterial system that can currently be used for such studies. The different activities with crystalline cellulose were examined, and the results demonstrated that the individual chimeric cellulases were essentially equivalent to the corresponding wild-type analogues. The wild-type cellulases displayed a synergism of about 1.5-fold; the cellulosomal pair acted synergistically when they were converted into free enzymes, whereas the free enzymes acted synergistically mainly in the wild-type state. The targeting effect was found to be the major factor responsible for the elevated activity observed for these specific enzyme combinations, whereas the proximity effect appeared to play a negligible role.
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Natarajan, Sujatha, Sangilimuthu Alagar Yadav, and Sowmya Priya Manoharan. "Influence of macerating enzyme - Cellulase on the extraction of valuable compounds: Carotenoid and Camptothecin." International Journal of Research in Pharmaceutical Sciences 9, no. 1 (2018): 115. http://dx.doi.org/10.26452/ijrps.v9i1.1200.
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Macerating enzymes breaks long chain compounds during maceration for extraction of industrially important phytomolecules. Cellulase is an important class of enzyme which helps in the extraction process of phytomolecules such as carotenoids, camptothecin from their natural sources as macerating enzyme. The extraction of phytoconstituents like carotenoids, camptothecin holds high commercial value. The uses of macerating enzymes help to the extraction process of phytomolecules and increase its yield. Quality of the product is also improved in terms of stability, texture and viscosity. Camptothecin is an important drug with potential anti-cancer activity. In this work, the effect of cellulase on the extraction of carotenoid from carrot, tomato and sweet potato have been studied. As a pioneer work, the production of camptothecin from endophytic fungi Aspergillus niger has been carried out using cellulase. The quantitative analysis of pharmaceutical important phytomolecules such as carotenoids and camptothecin were performed using UV-Visible spectrophotometer, HPLC with respective standard compounds. Carotenoid extraction was made from tomato, carrot and sweet potato with cellulose enzyme found 2.5±0.25µg/g, 2.2 ±0.18µg/g, 18± 1.75 µg/g respectively. Carotenoid extracted from carrot using enzyme yielded 1.47 times higher amount of carotenoid than that of without enzyme. Carotenoid extracted from tomato, showed the maximum difference of being 7.3 times higher with enzyme than without enzyme. The another industrially important phytomolecule camptothecin extraction was made from Aspergillus niger with cellulase enzyme yielded 0.5512 mg/g which is more than the camptothecin, extracted without enzyme (0.175 mg/g). Thus, it was observed that the use of cellulase enhanced the yield of both carotenoid and camptothecin from natural sources such as plants and fungi.
 Keywords: Camptothecin; Carotenoid; Cellulase enzyme; Extraction; HPLC
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Li, Hongkun, Meijia Dou, Xinyu Wang, et al. "Optimization of Cellulase Production by a Novel Endophytic Fungus Penicillium oxalicum R4 Isolated from Taxus cuspidata." Sustainability 13, no. 11 (2021): 6006. http://dx.doi.org/10.3390/su13116006.
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Endophytic fungi inside a plant can degrade a portion of plant lignin and cellulose. Endophytic Penicillium is one of the industrial microorganisms with the advantage of producing enzymes with a complete enzyme system that can be secreted into the extracellular space. The natural evolution of ancient tree species from special natural geographic environments to screen out cellulase-producing strains with excellent characteristics provides a promising direction for future industrial enzymes. The present study successfully isolated and screened a novel fungal endophyte, Penicillium oxalicum R4, with higher cellulase activity from Taxus cuspidata. Under the optimized culture conditions obtained by a Box–Behnken design (BBD) and an artificial neural network–genetic algorithm (ANN–GA), yields of Filter Paperase (FPase), Carboxymethyl Cellulase (CMCase) and β-glucosidase (βGLase) produced by P. oxalicum R4 were 1.45, 5.27 and 6.35 U/mL, which were approximately 1.60-fold, 1.59-fold and 2.16-fold higher than those of the non-optimized culture, respectively. The discovery of cellulase-producing strains of endophytic fungi located in special natural geographic environments, such as Taxus cuspidata, which is known as a living plant fossil, provides new research directions for future industrial enzymes.
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Yoshioka, Yuki, Toshiaki Tanabe, and Akira Iguchi. "The presence of genes encoding enzymes that digest carbohydrates in coral genomes and analysis of their activities." PeerJ 5 (November 28, 2017): e4087. http://dx.doi.org/10.7717/peerj.4087.
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Numerous enzymes that digest carbohydrates, such as cellulases and chitinases, are present in various organisms (e.g., termites, nematodes, and so on). Recently, the presence of cellulases and chitinases has been reported in marine organisms such as urchin and bivalves, and their several roles in marine ecosystems have been proposed. In this study, we reported the presence of genes predicted to encode proteins similar to cellulases and chitinases in the genome of the coral Acropora digitifera, their gene expression patterns at various life stages, and cellulose- and chitin-degrading enzyme activities in several coral species (A. digitifera, Galaxea fascicularis, Goniastrea aspera, Montipora digitata, Pavona divaricata, Pocillopora damicornis, and Porites australiensis). Our gene expression analysis demonstrated the expressions of these cellulase- and chitinase-like genes during various life stages, including unfertilized eggs, fertilized eggs, zygotes, planula larvae, primary polyps and adults of A. digitifera. Agar plate assays confirmed cellulase and chitinase activities in the tissues extracted from adult branches of several coral species. These results suggested that corals are able to utilize cellulases and chitinases in their life histories.
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TOYOHARA, HARUHIKO. "Ⅲ-2. Cellulase and environmental enzymes." NIPPON SUISAN GAKKAISHI 83, no. 5 (2017): 825. http://dx.doi.org/10.2331/suisan.wa2442-11.
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TARVAINEN, K., L. KANERVA, O. TUPASELA, et al. "Allergy from cellulase and xylanase enzymes." Clinical Experimental Allergy 21, no. 5 (1991): 609–15. http://dx.doi.org/10.1111/j.1365-2222.1991.tb00854.x.
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Yambe, Yoshiko, and Kiyotoshi Takeno. "Improvement of Rose Achene Germination by Treatment with Macerating Enzymes." HortScience 27, no. 9 (1992): 1018–20. http://dx.doi.org/10.21273/hortsci.27.9.1018.
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The germination percentage of Rosa multiflora Thunb. achenes was greatly increased when they were treated with 1% Driselase, a macerating enzyme, for 36 hours. The seeds germinated more rapidly when the achenes were treated with the enzyme for a longer period. Treatment with Cellulase Onozuka improved seed germination at a lower concentration than did Driselase. Pure preparations of pectinase and cellulase had effects similar to treatment with the enzymes noted. Treatment with pectinase was more efficient than treatment with cellulase. These enzymes likely loosened the bond between cells along the suture of the pericarp and forced the pericarp to split.
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Padil, Padil, Siti Syamsiah, Muslikhin Hidayat, and Rina Sri Kasiamdari. "KINERJA ENZIM GANDA PADA PRETREATMENT MIKROALGA UNTUK PRODUKSI BIOETANOL." Jurnal Bahan Alam Terbarukan 5, no. 2 (2017): 92–100. http://dx.doi.org/10.15294/jbat.v5i2.7564.
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The use of biomass of microalgae as a feedstock to produce bioethanol is very promising, it is caused by a large amount of carbohydrates contained in microalgae physiology cell. The main obstacle of enzymatic hydrolysis in order to produce bioethanol is the bound starch granules in a rigid cell wall. Therefore, pre-treatment steps needed to remove and convert complex carbohydrates into simple sugars before the fermentation process. Tetraselmis Chuii microalgae species are green microalgae (Chlorophyta) in which the cell wall containing cellulose and hemicellulose as the main constituent, therefore, this study observe the effect of the use of cellulase enzymes and xylanase as a strategy to open up the cell walls of microalgae. Another investigated parameter is the enzyme concentration, temperature, pH, and methods of use of enzymes. The results showed that the highest yield of glucose obtained was 31.912% (w / w) and is achieved under the conditions of a temperature of 45oC, pH of 4.5, the amount of biomass of microalgae as 5 g/L, the concentration of cellulase enzymes and xilanase 30% (w / w) at 40 minute at mechanism using cellulase and xylanase enzymes simultaneously.
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Andreaus, J., H. Azevedo, and A. Cavaco-Paulo. "Effects of temperature on the cellulose binding ability of cellulase enzymes." Journal of Molecular Catalysis B: Enzymatic 7, no. 1-4 (1999): 233–39. http://dx.doi.org/10.1016/s1381-1177(99)00032-6.
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Lovrien, Rex E., Karl K. Williams, Mark L. Ferrey, and David A. Ammend. "Calorimetric versus Growth Microbial Analysis of Cellulase Enzymes Acting on Cellulose." Applied and Environmental Microbiology 53, no. 12 (1987): 2935–41. http://dx.doi.org/10.1128/aem.53.12.2935-2941.1987.
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Haryanto, Mas Gunawan, Siswa Setyahadi, Muhammad Sahlan, et al. "Characterization of cellulase from E. coli BPPTCC-EGRK2." E3S Web of Conferences 52 (2018): 00024. http://dx.doi.org/10.1051/e3sconf/20185200024.
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Cellulase enzymes are widely used in various industries such as detergent industry, bioethanol, animal feed, textile and paper. This research focused on characterization of cellulase produced from Eschericia coli BPPT-CC EgRK2, which is a recombinant that can produce protein enzymes endo- β-1,4-glucanase. Eschericia coli BPPT-CC EgRK2 was cultured in 1 litre liquid medium Luria Bertani. Because the bacteria is intracellular, sonication is needed for cell disruption to get the cellulase enzyme. The enzyme activity was then analyzed by CMC substrate at different concentration. The protein content analysis was carried out using Bradford method; the molecular weight analysis was done using SDS-PAGE; while the enzyme kinetics was plotted using Michaelis-Menten model. Our results showed the highest enzyme activity was 2.403 U/ml and the protein concentration was 5.352 mg/ml. The Michaelis-Menten constant (Km) and maximum velocity (Vmax) for CMC substrate hydrolysis were 0.07 μmol/ml and 2.49 μmol/ml/sec, respectively. The cellulase molecular weight was 58 kDa using SDS-PAGE with 7.5% stacking gel. The results indicated that Eschericia coli BPPT-CC EgRK2 is a promising renewable source for cellulase production for industrial application.
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Khandoker, Nusrat, Arafat Al Mamun, Tanvir Noor Nafiz, Shakila Nargis Khan, and Md Mozammel Hoq. "Strain Improvement of Trichoderma Viride through Mutation for Enhanced Production of Cellulase." Bangladesh Journal of Microbiology 30, no. 1-2 (2016): 43–47. http://dx.doi.org/10.3329/bjm.v30i1-2.28452.
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Microbial fungal cellulases are very important for their applications in biopolishing of textile fibres, in poultry feed and paper and pulp industries. The main purpose of this study was to improve the wild strain Trichoderma viride for enhanced production of cellulase by random mutation technique employing ultraviolet (UV) irradiation and Ethidium bromide (EtBr) treatments. The wild strain exhibited the highest cellulase activity 5.52 U/ml on carboxy methyl cellulose (1.0%) and a comparable activity 4.74 U/ml on wheat bran (1.0%) as substrate under the optimum temperature 30°C and pH 4.0. Upon mutation by UV exposure the fungi produced cellulase 11.28 U/ml where as EtBr treated mutant showed 14.61 U/ml cellulase activities. Both the enzymes from wild and mutant T. viride demonstrated the highest activity at the assay temperature of 40ºC. The enzyme was applied for bio-polishing of jeans at prototype experiment and showed effective result as compared to one of the commercial enzymes.Bangladesh J Microbiol, Volume 30, Number 1-2,June-Dec 2013, pp 43-47
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Babalola, Olubukola O. "Pectinolytic and Cellulolytic Enzymes EnhanceFusarium compactumVirulence on Tubercles Infection of Egyptian Broomrape." International Journal of Microbiology 2010 (2010): 1–7. http://dx.doi.org/10.1155/2010/273264.
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The use of enzyme could facilitate pathogen penetration into plant host. Here the combination of cellulase and pectinase was ascertained on the pathogenicity ofF. compactum(1.4×106 propagules ml−1) on broomrape tubercles.F. compactumalone infected all the inoculated tubercles but did not kill any significant number. Infested tomato roots that were inoculated with mycelia plus pectinase (20 U ml−1) had over 50% tubercles dead one week after treatment. Those inoculated with mycelia plus cellulase (20 U ml−1) had above 60% mortality. Mixtures of mycelial plus the two enzymes (10 U ml−1of each enzyme) showed synergy. The activity catalyzed by an enzyme is a measure of the amount of enzyme present. It was shown that, in a 1 mg (10 U mg−1) cellulase used, 0.055 mg pectinase (1.1 U mg−1) is present. This explains why mycelial plus cellulase mix contends with mycelial plus the two enzymes.
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Mansour, Samira R., Ahmed M. Abdel-Azeem, and Samy Salem Soliman Abo-Deraz. "A new record of Actinobacteria isolated from soil in Jerusalem and their enzymatic potential." F1000Research 4 (January 14, 2015): 11. http://dx.doi.org/10.12688/f1000research.3257.1.
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Actinobacteria are well recognized for their bioactive compounds.They are considered as a promising source of wide range of important enzymes, some of which are produced on an industrial scale. In this study, 35 isolates of actinomycetes were isolated from soil samples collected in the area of Al-Aqsa Mosque in Jerusalem, Israel. To our knowledge, this is the first study of actinomycetes from this terrestrial environment. The efficiency of the isolated actinobacteria in the production of amylase, cellulase, protease, tyrosinase, lipase, catalase and phosphatase was studied. Isolates obtained showed some activity and other completely failed to produce such enzymes. From total 35 isolates, only three isolates (8.6%) showed ability to produce protease, four isolates (11.4%) for lipase, five isolates (14.3%) for tyrosinase and two isolates (5.7%) for phosphatase enzymes. However, all isolates were positive for amylase and catalase enzymes; vice versa for cellulase enzyme all isolates failed to degrade cellulose in the form of carboxymethylcellulose.
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Bernardi, Aline Vianna, Luis Eduardo Gerolamo, Paula Fagundes de Gouvêa, et al. "LPMO AfAA9_B and Cellobiohydrolase AfCel6A from A. fumigatus Boost Enzymatic Saccharification Activity of Cellulase Cocktail." International Journal of Molecular Sciences 22, no. 1 (2020): 276. http://dx.doi.org/10.3390/ijms22010276.
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Cellulose is the most abundant polysaccharide in lignocellulosic biomass, where it is interlinked with lignin and hemicellulose. Bioethanol can be produced from biomass. Since breaking down biomass is difficult, cellulose-active enzymes secreted by filamentous fungi play an important role in degrading recalcitrant lignocellulosic biomass. We characterized a cellobiohydrolase (AfCel6A) and lytic polysaccharide monooxygenase LPMO (AfAA9_B) from Aspergillus fumigatus after they were expressed in Pichia pastoris and purified. The biochemical parameters suggested that the enzymes were stable; the optimal temperature was ~60 °C. Further characterization revealed high turnover numbers (kcat of 147.9 s−1 and 0.64 s−1, respectively). Surprisingly, when combined, AfCel6A and AfAA9_B did not act synergistically. AfCel6A and AfAA9_B association inhibited AfCel6A activity, an outcome that needs to be further investigated. However, AfCel6A or AfAA9_B addition boosted the enzymatic saccharification activity of a cellulase cocktail and the activity of cellulase Af-EGL7. Enzymatic cocktail supplementation with AfCel6A or AfAA9_B boosted the yield of fermentable sugars from complex substrates, especially sugarcane exploded bagasse, by up to 95%. The synergism between the cellulase cocktail and AfAA9_B was enzyme- and substrate-specific, which suggests a specific enzymatic cocktail for each biomass by up to 95%. The synergism between the cellulase cocktail and AfAA9_B was enzyme- and substrate-specific, which suggests a specific enzymatic cocktail for each biomass.
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Bae, Jungu, Kouichi Kuroda, and Mitsuyoshi Ueda. "Proximity Effect among Cellulose-Degrading Enzymes Displayed on the Saccharomyces cerevisiae Cell Surface." Applied and Environmental Microbiology 81, no. 1 (2014): 59–66. http://dx.doi.org/10.1128/aem.02864-14.
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ABSTRACTProximity effect is a form of synergistic effect exhibited when cellulases work within a short distance from each other, and this effect can be a key factor in enhancing saccharification efficiency. In this study, we evaluated the proximity effect between 3 cellulose-degrading enzymes displayed on theSaccharomyces cerevisiaecell surface, that is, endoglucanase, cellobiohydrolase, and β-glucosidase. We constructed 2 kinds of arming yeasts through genome integration: ALL-yeast, which simultaneously displayed the 3 cellulases (thus, the different cellulases were near each other), and MIX-yeast, a mixture of 3 kinds of single-cellulase-displaying yeasts (the cellulases were far apart). The cellulases were tagged with a fluorescence protein or polypeptide to visualize and quantify their display. To evaluate the proximity effect, we compared the activities of ALL-yeast and MIX-yeast with respect to degrading phosphoric acid-swollen cellulose after adjusting for the cellulase amounts. ALL-yeast exhibited 1.25-fold or 2.22-fold higher activity than MIX-yeast did at a yeast concentration equal to the yeast cell number in 1 ml of yeast suspension with an optical density (OD) at 600 nm of 10 (OD10) or OD0.1. At OD0.1, the distance between the 3 cellulases was greater than that at OD10 in MIX-yeast, but the distance remained the same in ALL-yeast; thus, the difference between the cellulose-degrading activities of ALL-yeast and MIX-yeast increased (to 2.22-fold) at OD0.1, which strongly supports the proximity effect between the displayed cellulases. A proximity effect was also observed for crystalline cellulose (Avicel). We expect the proximity effect to further increase when enzyme display efficiency is enhanced, which would further increase cellulose-degrading activity. This arming yeast technology can also be applied to examine proximity effects in other diverse fields.
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Vuong, Thu V., and David B. Wilson. "Processivity, Synergism, and Substrate Specificity of Thermobifida fusca Cel6B." Applied and Environmental Microbiology 75, no. 21 (2009): 6655–61. http://dx.doi.org/10.1128/aem.01260-09.
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ABSTRACT A relationship between processivity and synergism has not been reported for cellulases, although both characteristics are very important for hydrolysis of insoluble substrates. Mutation of two residues located in the active site tunnel of Thermobifida fusca exocellulase Cel6B increased processivity on filter paper. Surprisingly, mixtures of the Cel6B mutant enzymes and T. fusca endocellulase Cel5A did not show increased synergism or processivity, and the mutant enzyme which had the highest processivity gave the poorest synergism. This study suggests that improving exocellulase processivity might be not an effective strategy for producing improved cellulase mixtures for biomass conversion. The inverse relationship between the activities of many of the mutant enzymes with bacterial microcrystalline cellulose and their activities with carboxymethyl cellulose indicated that there are differences in the mechanisms of hydrolysis for these substrates, supporting the possibility of engineering Cel6B to target selected substrates.
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Poole, D. M., A. J. Durrant, G. P. Hazlewood, and H. J. Gilbert. "Characterization of hybrid proteins consisting of the catalytic domains of Clostridium and Ruminococcus endoglucanases, fused to Pseudomonas non-catalytic cellulose-binding domains." Biochemical Journal 279, no. 3 (1991): 787–92. http://dx.doi.org/10.1042/bj2790787.
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The N-terminal 160 or 267 residues of xylanase A from Pseudomonas fluorescens subsp. cellulosa, containing a non-catalytic cellulose-binding domain (CBD), were fused to the N-terminus of the catalytic domain of endoglucanase E (EGE') from Clostridium thermocellum. A further hybrid enzyme was constructed consisting of the 347 N-terminal residues of xylanase C (XYLC) from P. fluorescens subsp. cellulosa, which also constitutes a CBD, fused to the N-terminus of endoglucanase A (EGA) from Ruminococcus albus. The three hybrid enzymes bound to insoluble cellulose, and could be eluted such that cellulose-binding capacity and catalytic activity were retained. The catalytic properties of the fusion enzymes were similar to EGE' and EGA respectively. Residues 37-347 and 34-347 of XYLC were fused to the C-terminus of EGE' and the 10 amino acids encoded by the multiple cloning sequence of pMTL22p respectively. The two hybrid proteins did not bind cellulose, although residues 39-139 of XYLC were shown previously to constitute a functional CBD. The putative role of the P. fluorescens subsp. cellulosa CBD in cellulase action is discussed.
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Darijani, Mojdeh, and Ashraf Kariminik. "Screening of cellulase producing bacteria from tomato waste materials for lycopene extraction." International Journal of Life Sciences 9, no. 2 (2015): 43–47. http://dx.doi.org/10.3126/ijls.v9i2.12055.
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Cellulase is one of the industrially important enzymes that has the ability to degrade cellulose. This enzyme is produced by a variety of microorganisms. It has numerous commercial applications like malting, wood processing, and preparation of denim fabrics in textile industries, maceration of protoplasts from plant tissues and de-inking process in recycling of printed papers. The aim of the present study was the isolation, identification and screening of extracellular cellulase producing bacteria with high cellulase activity from tomato waste materials and their identification by phenotypic, biochemical and molecular tests. Cellulose degrading bacteria were isolated after serial dilution preparation from tomato waste matraials and surface culturing on CMC agar medium. 40 bacteria were isolated. Bacteria were further identified by morphological, biochemical and molecular tests. All of the isolates were Gram positive endospore forming rods, thus they were identified as Bacillus sp. The obtained isolates were screened for cellulase production and lycopene extraction in submerged fermentation process. The best isolate was Bacillus axarquiensis strain CHMS1B6 based on molecular analysis. The bacteria was subjected to different optimum conditions include pH, temperature and time of incubation. The highest cellulase activity was obtained in pH 7 and the optimum temperature at 30°C after 72 hours incubation period. Our findings indicate that the tomato waste materials are as attractive sources for the study of novel cellulolytic bacteria and effective enzymes for cellulose biodegradation and lycopene extraction.DOI: http://dx.doi.org/10.3126/ijls.v9i2.12055 International Journal of Life Sciences 9 (2) : 2015; 43-47
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Fon, Fabian Nde, Ignatius Verla Nsahlai, Peter Frank Scogings, and Nasreldin Abdelrahim Dafaalla Basha. "In Vitro Cellulase Production from Five Herbivore Microbial Ecosystems and Consortia." Annals of Animal Science 14, no. 2 (2014): 329–40. http://dx.doi.org/10.2478/aoas-2014-0001.
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Abstract As the most abundant biomass in nature, cellulose is the main chemical component in herbivore forages. The energy locked in these complex polymers can only be released by cellulolytic enzymes. Therefore, research aiming to increase the expression of cellulolytic enzymes or browsing uncultured microbial ecosystem in search of potential fibrolytic enzymes is imperative. The main objectives were to: (a) investigate the variation of cellulase enzymes in cow (CW), horse (H), miniature horse (mH), wildebeest (WB) and zebra (ZB); and (b) identify their presence and activeness in microbial consortia, N1 (H+WB), N2 (H+ZB), N3 (WB+ZB) and N4 (H+WB+ZB). Fresh faecal or rumen inocula were cultured in the laboratory on maize stover and lucerne (1:1) with salivary buffer for 72 h at 38°C. Crude proteins (CPZ) were precipitated from both fresh and cultured inocula using 60% ammonium sulfate for enzyme assays and zymography. Endocellulases and their activity were identified on 1% (m/v) carboxymethyl cellulose (CMC) zymograms stained with Congo red. All CPZ extracts were active as reducing sugars were produced after incubation with crystalline cellulose, CMC and xylan. The number and types of proteins with endocellulase activity varied (P<0.05) among and within the different animal species CW (15), H (14), mH (14), WB (13) and ZB (13). Microbial consortia were active with relatively higher number of endocellulases, N1 (17), N3 (14), N4 (14), and N2 (13). Cellulase enzymes vary among and within herbivore species grazing on the same or different fields. Therefore, identifying specific enzymes and microbes with higher fibrolytic potentials from different ecosystems for transinoculation could play a vital role in improving forage digestibility in ruminants
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Gedela, Ravi. "A Carbohydrate Hydrolysis Enzymes encoding Genes in Neurospora crassa." JOURNAL OF ADVANCES IN BIOTECHNOLOGY 5, no. 3 (2015): 711–27. http://dx.doi.org/10.24297/jbt.v5i3.1539.
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Neurospora crassa, NCU05882.7 (423aa) and NCU09774.7 (303 aa) (NCU, Neurospora 7 crassa unit) genes encoding a Cellulase, which hydrolysis the Cellulose. In addition to that, 8 reporting here other 35 Carbohydrate hydrolysis enzymes encoding genes in N.crassa. A 9 metagenomic analysis for multiple sequences alignment and Phylogenetics analysis, the evaluated 10 result showed high sequence similarity and 99% homology to the other class of fungi; in the 11 bacterial species showed extremely very less sequence similarities and 100 % homology. 12 Where as in inter species between fungi and bacteria, the results showed extremely less sequence 13 similarities and 97 % homology. The studies on physiochemical properties of Cellulase using 14 GeneDoc, the evaluated results showed Cellulase was an amphoteric (polor), aromatic, aliphatic 15 and highly repeated amino acids of glycine and proline. These metagenomic studies could help 16 to straightforward isolation of Cellulase enzymes from NCU05882.7 (Chromosome/Linkage 17 Group-VII), NCU09774.7 (Chromosome Linkage Group- II) and other 35 Carbohydrate 18 hydrolysis enzymes encoding genes in N.crassa.
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Woods, F. M., J. S. Kotrola, D. G. Himelrick, T. M. Brasher та F. M. Basiouny. "Role of β-Galactosidase, Cellulase, Pectinesterase, and Polygalacturonase in Pectin Solubilization in Ripening Rabbiteye Blueberries". HortScience 30, № 4 (1995): 818A—818. http://dx.doi.org/10.21273/hortsci.30.4.818a.
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Fruit of two rabbiteye blueberries (Vaccinium ashei Read cvs. Premier and Tifblue) were analyzed at five stages of growth and development for cell wall softening enzymes in relation to pectin solubilization. The enzymes examined were β-galactosidase, cellulase, pectinesterase, and polygalacturonase. The decrease in fruit firmness was associated with increased activities of cellulase, polygalacturonase, and pectinesterase, which preceded the former enzymes. The activity of β-galactosidase remained relatively unchanged throughout. The pattern of enzyme activities from both cultivars were similar. Results from this study indicate that these enzymes may play a crucial role in overall fruit shelf life and hence postharvest marketing duration.
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Maftukhah, Siti. "Cellulase Enzyme Production Using Solid State Fermentation Method From Waste – A Review." UNISTEK 6, no. 2 (2019): 22–27. http://dx.doi.org/10.33592/unistek.v6i2.197.
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Solid fermentation (SSF) has built credibility in recent years in the biotechnology industry because its application has the potential to produce biologically active secondary metabolites, in addition to animal feed, fuel, food, industrial chemicals and pharmaceutical products, it has also emerged as an alternative interesting method that replaces the submerged fermentation method(SmF). This paper reviews the meaning of SSF, the factors that influence the success of SSF, the advantages and disadvantages of SSF, the meaning of cellulase enzymes, the use of cellulase enzymes and the production of cellulase enzymes using SSF from waste. The waste consists of agricultural waste and food processing waste with various microorganisms, optimization and pretreatment. So that the various levels of enzyme activity produced depend on the type of waste.
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Xu, Hui, Dongmei Han, and Zhaohui Xu. "Expression of Heterologous Cellulases inThermotogasp. Strain RQ2." BioMed Research International 2015 (2015): 1–11. http://dx.doi.org/10.1155/2015/304523.
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The ability ofThermotogaspp. to degrade cellulose is limited due to a lack of exoglucanases. To address this deficiency, cellulase genes Csac_1076 (celA) and Csac_1078 (celB) fromCaldicellulosiruptor saccharolyticuswere cloned intoT.sp. strain RQ2 for heterologous overexpression. Coding regions of Csac_1076 and Csac_1078 were fused to the signal peptide of TM1840 (amyA) and TM0070 (xynB), resulting in three chimeric enzymes, namely, TM1840-Csac_1078, TM0070-Csac_1078, and TM0070-Csac_1076, which were carried byThermotoga-E. colishuttle vectors pHX02, pHX04, and pHX07, respectively. All three recombinant enzymes were successfully expressed inE. coliDH5αandT.sp. strain RQ2, rendering the hosts with increased endo- and/or exoglucanase activities. InE. coli, the recombinant enzymes were mainly bound to the bacterial cells, whereas inT.sp. strain RQ2, about half of the enzyme activities were observed in the culture supernatants. However, the cellulase activities were lost inT.sp. strain RQ2 after three consecutive transfers. Nevertheless, this is the first time heterologous genes bigger than 1 kb (up to 5.3 kb in this study) have ever been expressed inThermotoga, demonstrating the feasibility of using engineeredThermotogaspp. for efficient cellulose utilization.
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Wu, Shuai, Xiaojuan Ma, Shilin Cao, Lihui Chen, Liulian Huang, and Fang Huang. "Application of enzymes for the reduction of PFI revolutions in the secondary pulping process and characteristics of thermomechanical pulp." BioResources 15, no. 4 (2020): 7487–502. http://dx.doi.org/10.15376/biores.15.4.7487-7502.
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Three enzymes, mannanase, xylanase, and cellulase, were applied for hydrolysis of thermomechanical pulp (TMP) primary discharge prior to PFI refining, aiming to study the effect of enzymatic hydrolysis on the required number of PFI revolutions. The quantity of reducing sugar was used as an indicator for enzyme hydrolysis efficiency. Then, under the optimized enzyme loading, treated and un-treated pulp were refined with different PFI revolutions. Subsequent fiber characteristics, such as fiber length and fines content were examined. Under the optimized enzyme loadings and a given 20000 PFI revolutions, in comparison with the control pulp, mannanase and xylanase pre-treatment could save PFI refining revolutions by 20% and 25%, respectively. There was no significant energy savings for the cellulase-treated pulp. During the hydrolysis, the enzyme broke down TMP fibers into shorter pieces and yielded more fines than the control pulp. Among the three enzymes, cellulase showed the highest efficiency in fiber breakdown, mannanase in the middle, xylanase the lowest. Longer hydrolysis time (more than one hour) had no evident effect on the pulp freeness reduction and reducing sugar production. Among the three enzymes, under the optimized enzyme loading, cellulase was the most efficient for enhancing production of reducing sugars.
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Fauzi, Muhammad, Nisa Rachmania Mubarik, and Anuraga Jayanegara. "Screening of cellulose- and lignin-degrading fungi for improving nutritive quality of ruminant feed." MATEC Web of Conferences 197 (2018): 06001. http://dx.doi.org/10.1051/matecconf/201819706001.
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This experiment aimed to screen some cellulose- and lignin-degrading fungal species for improving nutritive quality of ruminant feed. Fungal species used were Ganoderma lucidum, Pleurotus ostreatus, Phanerochaete chrysosporium, and Trametes visicolor. These fungal species were grown on Potato Dextrose Broth (PDB) medium that added with 0.5 g substrate, i.e. either rice straw, rice bran or carboxymethyl cellulose for 12 days at room temperature. Harvesting was performed in order to separate fungal mycelium and supernatant that contained crude cellulase enzyme. Among the fungi observed, Ganoderma lucidum had the highest cellulase activity, i.e. 4.02 U/mg. Cellulase activities of Pleurotus ostreatus, Phanerochaete chrysosporium, and Trametes visicolor were 1.53, 1.08, and 0.13 U/mg, respectively. Ganoderma lucidum was further investigated for its ligninolytic enzyme activity, i.e. laccase and manganese peroxidase. It was observed that the fungi had laccase and manganese peroxidase activities of 368.95 and 33.89 U/mL, respectively. Crude enzymes of Ganoderma lucidum that contain cellulase, laccase and manganese peroxidase were further used to increase nutritive quality of rice straw and subjected to in vitro incubation with rumen fluid of cattle.
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Shreya Kishore, Saravana Dinesh SP, Srirengalakshmi, and Arvind Sivakumar. "Comparing the accuracy of Manual Tracing to Digital Tracing – Angular Measurements." International Journal of Research in Pharmaceutical Sciences 10, no. 2 (2019): 1302–6. http://dx.doi.org/10.26452/ijrps.v10i2.530.
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Macerating enzymes breaks long chain compounds during maceration for extraction of industrially important phytomolecules. Cellulase is an important class of enzyme which helps in the extraction process of phytomolecules such as carotenoids, camptothecin from their natural sources as a macerating enzyme. The extraction of phytoconstituents like carotenoids, camptothecin holds high commercial value. The uses of macerating enzymes help to the extraction process of phytomolecules and increase its yield. Quality of the product is also improved in terms of stability, texture and viscosity. Camptothecin is an important drug with potential anti-cancer activity. In this work, the effect of cellulase on the extraction of carotenoid from carrot, tomato and sweet potato have been studied. As a pioneer work, the production of camptothecin from endophytic fungi Aspergillus niger has been carried out using cellulase. The quantitative analysis of important pharmaceutical phytomolecules such as carotenoids and camptothecin were performed using a UV-Visible spectrophotometer, HPLC with respective standard compounds. Carotenoid extraction was made from tomato, carrot and sweet potato with cellulose enzyme found 2.5±0.25µg/g, 2.2 ±0.18µg/g, 18± 1.75 µg/g respectively. Carotenoid extracted from carrot using enzyme yielded 1.47 times higher amount of carotenoid than that of without enzyme. Carotenoid extracted from tomato showed the maximum difference of being 7.3 times higher with enzyme than without enzyme.