Relevant bibliographies by topics / Cellulase enzymes

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Academic literature on the topic 'Cellulase enzymes'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 February 2022

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Journal articles on the topic "Cellulase enzymes"

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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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Dissertations / Theses on the topic "Cellulase enzymes"

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Hu, Gang. "Adsorpton and Activity of Cellulase Enzymes on Various of Cellulose Substrates." NCSU, 2009. http://www.lib.ncsu.edu/theses/available/etd-04222009-234535/.

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The objective of this research is to understand the interfacial behavior of cellulase enzymes and its effect on cellulose hydrolysis. This research began with an in-situ monitoring of cellulose hydrolysis using a piezoelectric based quartz crystal microbalance. The time-course kinetics was modeled using a dose response model. The adsorption indicated by the frequency drop followed a Langmuir model as cellulase enzyme increased. Another important part of this research is the development of a new cellulase activity assay based on the piezoelectric technique. This assay provides an easier and more user friendly method for cellulase enzyme activity measurement. It also helps to clarify an element of the interpretation of frequency drops after the injection of cellulase solutions in the hydrolysis of cellulose film, which has been neglected in previous research. Interfacial adsorption of cellulase protein was also investigated using the depletion method. The effects of substrate properties, primarily the crystallinity, which was characterized using X-ray diffraction, were investigated. The effect of surface area, which was measured using both laser light scattering and BET adsorption, on cellulase adsorption were also investigated. It was found that crystallinity played a more important role in cellulase adsorption than surface areas of cellulosic substrate. In characterization of cellulosic substrates, the water retention value (WRV) was also investigated. The results indicated that lower crystallintiy substrates have higher water retention ability. The cellulase adsorption, as well as desorption, was also studied by using sodium dodecyle sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The adsorption results followed the same trend as indicated by the depletion methods. The various isozymes demonstrated a uniform adsorption in proportion to their concentrations. Desorption appeared uniform. Higher pH was found to create higher desorption for a particular cellulase from a particular substrates. It was also found that cellulase from Trichoderma reesei had higher affinity to cellulosic substrates used in this work than the one from Aspergillus niger.
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Linder, Markus. "Structure-function relationships in fungal cellulose-binding domains /." Espoo, Finland : VTT, Technical Research Centre of Finland, 1996. http://www.vtt.fi/inf/pdf/publications/1996/P294.pdf.

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Imai, Makiko. "Analysis of interaction between cellulosic biomass and saccharification enzymes." Kyoto University, 2020. http://hdl.handle.net/2433/252998.

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Ubhayasekera, Wimal. "Structural studies of cellulose and chitin active enzymes /." Uppsala : Dept. of Molecular Biology, Swedish University of Agricultural Sciences, 2005. http://epsilon.slu.se/200518.pdf.

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Chakrabarti, Ajoy Chuni Carleton University Dissertation Biology. "One-step conversion of cellulose to fructose using co-immobilized cellulase, B-glucosidase and glucose isomerase." Ottawa, 1988.

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Reichstädter, Marek. "Imobilizace vybraných glykanohydroláz." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2015. http://www.nusl.cz/ntk/nusl-217152.

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The theoretical part of this thesis deals with cellulolytic enzymes, their microbial producers, the possibilities of using such enzymes in the industry and how can be enzymes - not only cellulolytic - immobilized. Experimental part examines the preparations created by immobilizing various amounts of the commercially used cellulolytic complex Cellulast 1.5L onto various synthetic carriers made of polyethylene terephthalate - commercially used Sorsilen, PET carrier and glutaraldehyde-treated PET carrier. Enzyme activity of these preparations was determined by Somogyi - Nelson method by spectrophotometry. For the highest activity immobilized preparation was determined the temperature- and the pH-optimum. The difference in effects change between the free and immobilized enzyme by measuring viscosity decrease of the substrate depending on the degradation of glycosidic bonds was also studied.
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Kyriacou, Andreas. "Characterization and adsorption of the cellulase components from Trichoderma reesei." Thesis, McGill University, 1987. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=75770.

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The cellulase enzyme system of the fungus Trichoderma reesei Rut C-30 was fractionated by DEAE ion exchange chromatography into four groups according to their substrate specificity. By analytical isoelectric focusing and activity stains it was revealed that fraction EGI is comprised of endoglucanases specific to cellulosic substrates, and that fractions EGII and EGIII are non-specific endoglucanases that hydrolyze cellulose as well as xylan substrates. The major protein fraction CBHI was shown to be a cellobiohydrolase. Turbidimetric measurement phase contrast microscopy and analysis of the products resulting from the hydrolysis of swollen cellulose demonstrated differences between endoglucanases and cellobiohydrolases. The enzyme component CBHII, previously described as a cellobiohydrolases was shown to be an endoglucanase.<br>The adsorption behavior of the four enzyme fractions was examined, with respect to pH, temperature and ionic strength. This was accomplished by using ($ sp3$H) radiolabeled cellulase fractions as tracers. The adsorption of the cellulases occurred within 60 minutes, and was described by a Langmuir type correlation. Increasing the adsorption temperature increased the saturation uptake of the endoglucanases but not of the cellobiohydrolases. Changes in pH and ionic strength affected both the degree and strength of adsorption of all the fractions, likely due to protein structure conformational changes.<br>Direct evidence of exchange between adsorbed and free enzymes was obtained for each component using ($ sp3$H) and ($ sp{14}$C) radiolabeled tracers. In simultaneous adsorption of enzyme pairs, CBHI was shown to predominate adsorption. Endoglucanase EGI was preferentially adsorbed over EGII and EGIII. Sequential adsorption studies have shown that interaction between enzyme components largely determine the degree of their adsorption. Evidence suggested both common and distinct adsorption sites exist, and that their occupation depends on which components are involved.<br>Light microscopy and monitoring of sugar production during cellulose hydrolysis indicated that conditions which limit predominance in adsorption by any one of the cellulase components, enhance synergism and increase degree of hydrolysis.
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Lucena, Guilherme Nunes. "Enzyme modified magnetic nanoparticles : an approach for biomass conversion processes /." Araraquara, 2020. http://hdl.handle.net/11449/192507.

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Orientador: Rodrigo Fernando Costa Marques<br>Resumo: A biomassa lignocelulósica vem se destacando como uma matéria-prima essencial para a produção de muitos produtos químicos de interesse industrial em áreas como a produção de energia, alimentos, fármacos, agricultura, meio ambiente e assim por diante. Apesar disso, muitas aplicações vêm esbarrando em uma série de dificuldades encontradas nos processos de conversão enzimática, como instabilidade operação das enzimas, alto custo de produção e purificação, reações de inibição e problemas de recuperação e reciclo. Para contornar esses problemas, muitos métodos de imobilização enzimática têm surgido, entre os quais, destaca-se a obtenção de agregados enzimáticos reticulados magnéticos (MCLEAs). Esta classe de materiais é obtida a partir da reação de reticulação entre agregados físicos de enzimas e suportes magnéticos, o qual pode unir as importantes propriedades catalíticas dos agregados físicos (como resultado da manutenção da estrutura nativa da enzima) à capacidade de recuperação e reciclo do suporte magnético (devido suas propriedades magnéticas intrínsecas). Frente a isso, esse trabalho relata a síntese, caracterização e potencial aplicação de MCLEAs de enzimas celulases em processos de conversão de celulose. Dividido em três capítulos, primeiramente é apresentado um review sobre o estado da arte no que diz respeito a obtenção de produtos de valor agregado a partir da biomassa lignocelulósica utilizando MCLEAs. No segundo capítulo, diferentes MCLEAs foram preparados na presenç... (Resumo completo, clicar acesso eletrônico abaixo)<br>Abstract: Lignocellulosic biomass has highlighted as an essential renewable raw material for production of many value-added chemicals of industrial interest in field as energy production, food, pharmaceutical, agriculture, environment and so on. Despite it, many applications have wrought with a series of difficulties in regarding enzymatic conversion processes, as enzyme operational instability, high production and purification cost, inhibition reactions, and issues of recovery and recycle. To overcome these issues, many enzyme immobilization methods have emerged, among which highlights the obtention of magnetic-cross linked enzyme aggregates (MCLEAs). This materials class is obtained from cross-linking reaction between enzyme physical aggregates and magnetic supports, which can gather the important catalytic properties of the physical aggregates (as a result of enzyme native structure maintenance) to recovery and recycle capacity of magnetic nanoparticles (as result of its intrinsic magnetic properties). Faced it, this work reports the synthesis, characterization and potential application of different cellulases MCLEAs in the cellulose enzymatic conversion process. Sectioned in three chapters, firstly is presented a review about the state of art in concern to obtention of value-added chemicals from lignocellulosic biomass using MCLEAs. In the second chapter, different MCLEAs were prepared in the presence of quitosana-coated magnetic nanoparticles with three different precipitation age... (Complete abstract click electronic access below)<br>Doutor
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McKenzie, Belinda, and s9907915@student rmit edu au. "Heterologous expression of cellulase enzymes in transplastidic Nicotiana tabacum cv. Petit Havana." RMIT University. Applied Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20080805.120923.

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Extensive research into enzyme-induced bio-conversion of lignocellulose to soluble sugars has been conducted and research continues in this area. Several approaches have been taken to attempt to alleviate the economic problems associated with utilisation of lignocellulose in fuel ethanol production. By expressing cellulase genes in planta, it is hoped that the cost of enzyme-mediated hydrolysis of cellulose to its soluble sugar monomers, will be reduced. Some accomplishments have been made in this area using nuclear genetic transformation (Abdeev et al., 2003; Abdeev et al., 2004; Austin-Phillips et al., 1999; Biswas et al., 2006; Dai et al., 2000a,b; Dai et al., 2005; Jin et al., 2003; Kawazu et al., 1999; Sakka et al., 2000; Ziegelhoffer et al., 1999; Ziegelhoffer et al., 2001; Ziegler et al., 2000), but more research is required to bring the levels of cellulase enzyme expression in plants to levels that will make the process economically competitive. Chloroplasts of N. tabacum were selected as a target for transformation for high level expression due to their extremely high rates of transcription and translation. These were transformed with two genes, the e1 gene from A. cellulolyticus, and the cbh1 gene from T. reesei. Further aims included the investigation of the effects of using different promoters, and the novel use of both nuclear and chloroplast-based expression in a single plant, on the level of protein production in the heterologous host. Heterologous expression of the cbh1 gene was not successful. This is thought to be due to toxicity of the protein in a prokaryotic environment. Future studies should focus on trying to avoid this toxicity by targeting of the chloroplast-expressed enzyme to specific tissues, such as the thylakoid membrane, for containment, creating a codon-optimised synthetic gene that better mimics the codon usage of the plant to be used for expression, or placing the expression under a reactive cascade that is only activated upon exposure to an external trigger. Heterologous expression of the full length gene for E1 from A. cellulolyticus was successful. Chloroplast homology vectors under the constitutive promoter Prrn, and the inducible promoter T7, were constructed and these were used to successfully transform N. tabacum cv. Petit Havana chloroplasts. Stable transgenic plants were produced and evaluated by a variety of means, with the heterologously expressed enzyme showing activity against the soluble substrate analogue MUC of up to 3122 ± 466 pmol 4-MU/mg TSP/min and an E1 accumulation level of up to 0.35% ± 0.06 of the total soluble protein. Lastly, chloroplast transformation was combined with nuclear transformation to create novel dual-transgenic plants simultaneously expressing E1 from both the nuclear and chloroplast genomes. The combination of these technologies was very successful, with the heterologously expressed enzyme showing activity against the soluble substrate analogue MUC of up to 35706 ± 955 pmol 4-MU/mg TSP/min and an E1 accumulation level of up to 4.78% ± 0.13 of the total soluble protein, and provides a new approach for increasing the accumulation levels of plant-produced cellulase enzymes.
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McCabe, Bernadette K., of Western Sydney Macarthur University, and Faculty of Business and Technology. "Production of cellulolytic enzymes using immobilised anaerobic fungi." THESIS_FBT_XXX_Mccabe_B.xml, 1998. http://handle.uws.edu.au:8081/1959.7/83.

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An investigation was made into the isolation and screening of highly cellulolytic anaerobic fungi and their production of cellulolytic enzymes using immobilised rhizomycelia. A total of 46 anaerobic fungi were isolated on cellulosic substrates from ruminant and non-ruminant herbivores. Primary screening of these isolates was performed using dye release from cellulose-azure which qualitatively detected cellulolytic activity. Twelve isolates were chosen on the basis of their maximum solubilisation rates of the labelled cellulose and then subjected to secondary screening which involved the quantification of enzyme activity. The enzyme mixtures were characterised by carboxymethylcellulase, xylanase, B-glucosidase, B-xylosidase and cellobiase assays, measured by the production of either reducing sugars, p-nitrophenol or glucose. All strains produced a number of enzymes that allowed them to hydrolyse straw and highest enzyme activity was measured in static cultures grown on 0.5% straw. A monocentric isolate, Piromyces strain KSX1 from a red kangaroo, and a cattle polycentric isolate, Orpinomyces strain 478P1, were selected for study of cellulolytic enzyme production on the basis of high fibre digestion capability and amenability toward encapsulation. The immobilised polycentric strain proved to be operationally superior to strain KSX1 as strain 478P1 did not produce any viable growth in the culture liquor. Studies into single batch cultures of free cells of strains KSX1 and 478P1 revealed that the maximum specific rate of B-glucosidase production occurred concomitantly with maximum specific growth rate suggesting that the immobilised fungus must grow for continuous enzyme production to occur. Although the physiology of cellulase synthesis in strains KSX1 and 478P1 was found to be growth-associated, immobilisation of the fungus offered the advantage of the repeat-batch use of cells with the accumulation of extracellular enzymes after each batch. Thus, operational gains were the key issues in assessing the potential application of immobilised anaerobic fungi in the production of cellulolytic enzymes. The repeat-batch system was operationally more efficient than the free cell batch cultures because immobilisation removed the need of reculturing the cells for every single batch.<br>Doctor of Philosophy (PhD)
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Books on the topic "Cellulase enzymes"

1

Linder, Markus. Structure-function relationships in fungal cellulose-binding domains. VTT, Technical Research Centre of Finland, 1996.

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Koivula, Anu. Structure-function studies of two polysaccharide-degrading enzymes: Bacillus strearothermophilus Ü-amylase and trichoderma reesei cellobiohydrolase II. VTT, Technical Research Centre of Finland, 1996.

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Heikinheimo, Lea. Trichoderma reesei cellulases in processing of cotton. VTT Technical Research Centre of Finland, 2002.

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Aro, Nina. Characterization of novel transcription factors ACEI and ACEII involved in regulation of cellulase and xylanase genes in Trichoderma reesei. VTT Technical Research Centre of Finland, 2003.

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Rosevear, A. Immobilised enzymes and cells. A. Hilger, 1987.

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Biological barriers to cellulosic ethanol. Nova Science Publishers, 2009.

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King, William James. Autoimmune cellular responses towards neutrophil granule enzymes in systemic vasculitis. University of Birmingham, 1998.

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1932-, Hervé Guy, ed. Molecular and cellular enzymology. Springer, 2010.

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TRICEL Symposium on Trichoderma Reesei Cellulases and Other Hydrolases (2nd 1993 Espoo, Finland). Trichoderma reesei cellulases and other hydrolases: Enzyme structures, biochemistry, genetics, and applications : proceedings of the TRICEL93 Symposium, June 2-5, 1993, Espoo, Finland. Foundation for Biotechnical and Industrial Fermentation Research, 1993.

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W, Kreutzberg Georg, Reddington Martin 1947-, and Zimmermann Herbert 1944-, eds. Cellular biology of ectoenzymes: Proceedings of the International Erwin-Riesch-Symposium on Ectoenzymes, May 1984. Springer-Verlag, 1986.

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Book chapters on the topic "Cellulase enzymes"

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Sun, Fubao, Marie Rose Mukasekuru, Danyang Chen, et al. "Determination of Cellulase Activities and Model for Lignocellulose Saccharification." In Fungal Cellulolytic Enzymes. Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0749-2_12.

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Gunjal, Aparna B., Neha N. Patil, and Sonali S. Shinde. "Cellulase in Degradation of Lignocellulosic Wastes." In Enzymes in Degradation of the Lignocellulosic Wastes. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-44671-0_2.

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Ghosh, B. K., A. Ghosh, and Adrian Salnar. "Cellulase Secretion from a Hypercellulolytic Mutant of Trichoderma Reesei Rut-C30." In Extracellular Enzymes of Microorganisms. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-1274-1_20.

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Hu, Jinguang, Rui Zhai, Dong Tian, and Jack N. Saddler. "Substrate Factors that Influence Cellulase Accessibility and Catalytic Activity During the Enzymatic Hydrolysis of Lignocellulosic Biomass." In Fungal Cellulolytic Enzymes. Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0749-2_13.

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Rahkamo, L., M. Vehviläinen, L. Viikari, P. Nousiainen, and J. Buchert. "Modification of Dissolving Pulp by Hydrolysis with Cellulase Enzymes." In ACS Symposium Series. American Chemical Society, 1998. http://dx.doi.org/10.1021/bk-1998-0687.ch026.

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Irfan, Muhammad, Misbah Ghazanfar, Amad Ur Rehman, and Asma Siddique. "Strategies to Reuse Cellulase: Immobilization of Enzymes (Part II)." In Fungal Biology. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-14726-6_9.

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Stowers, Chris C., Elizabeth M. Ferguson, and Robert D. Tanner. "Development of Activity-based Cost Functions for Cellulase, Invertase, and Other Enzymes." In Biotechnology for Fuels and Chemicals. Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-526-2_45.

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Saharay, Moumita, Hao-Bo Guo, Jeremy C. Smith, and Hong Guo. "QM/MM Analysis of Cellulase Active Sites and Actions of the Enzymes on Substrates." In ACS Symposium Series. American Chemical Society, 2010. http://dx.doi.org/10.1021/bk-2010-1052.ch007.

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Paul, Jaishree. "Pretreatment of Agricultural Residues by Cellulase and Xylanase Enzymes Produced by a Bacillus sp." In Environmental Biotechnology. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-017-1435-8_34.

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Deejing, Somkid, and Duangpen Dittamart. "Isolation and Screening of Cellulase-Producing Microorganisms and the Study of Some Characteristics of Enzymes." In Biology Education and Research in a Changing Planet. Springer Singapore, 2015. http://dx.doi.org/10.1007/978-981-287-524-2_16.

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Conference papers on the topic "Cellulase enzymes"

1

Sumardi, Salman Farisi, Christina N. Ekowati, and Cahya I. Listiyorini. "Isolation and Characterization Bacillus sp. Producing Cellulase Enzymes from Hanura Mangrove." In International Conference on Sustainable Biomass (ICSB 2019). Atlantis Press, 2021. http://dx.doi.org/10.2991/aer.k.210603.004.

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Kuzikova, Irina, Irina Kuzikova, Vera Safronova, Vera Safronova, Nadezda Medvedeva, and Nadezda Medvedeva. "IMPACT OF NONYLPHENOL ON THE PHYSIOLOGICAL ACTIVITY OF FUNGI FROM THE COASTAL AREA OF THE GULF OF FINLAND." In Managing risks to coastal regions and communities in a changing world. Academus Publishing, 2017. http://dx.doi.org/10.21610/conferencearticle_58b431765a62a.

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Nonylphenol (NP) is the most abundant environmental estrogen listed as one of the priority hazardous substances in the Water Framework Directive (EC 2000) and the priority pollutant of Baltic Sea (HELCOM 2010). The present study aims to compare the effects of technical nonylphenol (tNP) on the cellulase, amylase and protease activity of the terrestrial fungal strains played a significant role in aquatic ecosystems due to their high adaptive capacity and a large range of functional activity. The study also attempts to understand the mechanisms behind the varying sensitivity of the terrestrial fungi to tNP. The fungal strains were isolated from the bottom sediments of the coastal area of the eastern part of the Gulf of Finland. The terrestrial fungi were identified based on their morphological characteristics and nucleotide sequence analysis of internal transcribed space region. One reason for significant differences in sensitivity to the toxicant studied among the fungi is the change in the fungal cell permeability, in particular in cell membrane permeability, induced by NP. Environmentally relevant concentrations of tNP cause significant changes in activity of hydrolytic enzymes in the terrestrial fungi Aspergillus tubingensis, Penicillium expansum, Penicillium glabrum, and Cadophora fastigiata involved in organic matter degradation in bottom sediments. There can be increasing or decreasing trend, depending on both the type of enzyme and the tNP concentration. The revealed changes may disrupt the destructive processes in bottom sediments, as well as succession and stability of microbial communities functioning in the aquatic environment. It was found that tNP contributes to the activation of proteolytic enzymes, considered as potential fungal virulence factors. This may lead to emergence fungal strains with enhanced virulence in aquatic microbiocenoses. The investigations of the physiological responses of terrestrial fungi under nonylphenol will be important for biochemical processes dynamics and their environmental consequences evaluation.
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Kuzikova, Irina, Irina Kuzikova, Vera Safronova, Vera Safronova, Nadezda Medvedeva, and Nadezda Medvedeva. "IMPACT OF NONYLPHENOL ON THE PHYSIOLOGICAL ACTIVITY OF FUNGI FROM THE COASTAL AREA OF THE GULF OF FINLAND." In Managing risks to coastal regions and communities in a changing world. Academus Publishing, 2017. http://dx.doi.org/10.31519/conferencearticle_5b1b93c5890b52.86067390.

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Nonylphenol (NP) is the most abundant environmental estrogen listed as one of the priority hazardous substances in the Water Framework Directive (EC 2000) and the priority pollutant of Baltic Sea (HELCOM 2010). The present study aims to compare the effects of technical nonylphenol (tNP) on the cellulase, amylase and protease activity of the terrestrial fungal strains played a significant role in aquatic ecosystems due to their high adaptive capacity and a large range of functional activity. The study also attempts to understand the mechanisms behind the varying sensitivity of the terrestrial fungi to tNP. The fungal strains were isolated from the bottom sediments of the coastal area of the eastern part of the Gulf of Finland. The terrestrial fungi were identified based on their morphological characteristics and nucleotide sequence analysis of internal transcribed space region. One reason for significant differences in sensitivity to the toxicant studied among the fungi is the change in the fungal cell permeability, in particular in cell membrane permeability, induced by NP. Environmentally relevant concentrations of tNP cause significant changes in activity of hydrolytic enzymes in the terrestrial fungi Aspergillus tubingensis, Penicillium expansum, Penicillium glabrum, and Cadophora fastigiata involved in organic matter degradation in bottom sediments. There can be increasing or decreasing trend, depending on both the type of enzyme and the tNP concentration. The revealed changes may disrupt the destructive processes in bottom sediments, as well as succession and stability of microbial communities functioning in the aquatic environment. It was found that tNP contributes to the activation of proteolytic enzymes, considered as potential fungal virulence factors. This may lead to emergence fungal strains with enhanced virulence in aquatic microbiocenoses. The investigations of the physiological responses of terrestrial fungi under nonylphenol will be important for biochemical processes dynamics and their environmental consequences evaluation.
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Cekmecelioglu, Deniz, and Ali Demirci. "<i>Evaluating fungal co-production of cellulase and xylanase enzymes at shake-flask scale using distillers dried grains with solubles (DDGS) and its validation in benchtop fermenters </i>." In 2018 Detroit, Michigan July 29 - August 1, 2018. American Society of Agricultural and Biological Engineers, 2018. http://dx.doi.org/10.13031/aim.201800332.

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Gaikwad, Swapnil, Avinash P. Ingle, Felipe A. F. Antunes, Júlio C. dos Santos, Mahendra Rai, and Silvio Silvério da Silva. "Cellulase Enzyme Immobilization on Magnetic Nanoparticles for Clean Sugar Production from Cellulose." In The 3rd World Congress on Recent Advances in Nanotechnology. Avestia Publishing, 2018. http://dx.doi.org/10.11159/icnb18.103.

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Kato, Yoko. "The Role of Protein as a Deformation Controller in Cellulose Tissue." In ASME 2012 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/imece2012-89313.

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The tunic of Halocynthia roretzi is composed of cellulose Iβ, mostly in crystalline form. It was recently revealed that the tunic can actively deform in response to mechanical stimuli and acetylcholine and that the tunic has F-actin, elastic fibers, acetylcholinesterase, and neurofilaments, which are involved in this process. Most of the hemocytes in the tunic secrete an enzyme whose substrate is the same as that of α-chymotrypsin; however, the enzyme’s role has not yet been determined. In this study, it was hypothesized that the enzyme hydrolyzes the protein in the tunic to induce tunic deformation. The results show that administration of α-chymotrypsin results in deformation of the tunic in an inward direction. Tunic deformation can be induced by the secretion of hemocytes due to greater hydrolysis of protein in the inner rather than outer regions. The deformation pattern is the same as that induced by both mechanical stimuli and acetylcholine. Moreover, stimulation with an electrical field (3.4 × 102 V/m), which is too weak to deform cellulose, still causes tunic deformation, indicating involvement of the nervous system. These characteristics will be helpful for the design of an active composite material containing cellulose.
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Petlamul, Wanida, Thawatchai Sripornngam, Narawadee Buakwan, Sawai Buakaew, and Kuntapon Mahamad. "The Capability of Beauveria Bassiana for Cellulase Enzyme Production." In the 7th International Conference. ACM Press, 2017. http://dx.doi.org/10.1145/3051166.3051167.

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Caner, Nazli, and Jeffrey W. Ruberti. "Detection of MMP-13 Activity on Intentionally Strain-Released Type-II Collagen Network in Bovine Articular Cartilage." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53913.

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Articular cartilage is a specialized avascular connective tissue found at the contact regions of diarthrodial joints. Cartilage has few cells (&lt; 5% of the volume), though these cells can maintain the balance of turnover in healthy tissue, when the tissue is damaged, they are not able to repair the defects [1–3]. Extra cellular matrix (ECM) in cartilage comprises water, collagen (principally type II), proteoglycans and noncollagenous proteins. The type II collagen network, which is the dominant structural protein in cartilage ECM, constrains the expansion of the resident PGs and is generally held in mechanical tension. In osteoarthritis (OA), the balance of cartilage tissue production/degradation is thought to be affected by abnormal mechanical stimuli leading to net matrix resorption through production of excess degradative enzymes (e.g. matrix metalloproteinases (MMP) and aggrecanases) [4–8]. In OA tissue the amount of MMP-13 is thought to be increased relative to healthy tissue. OA typically occurs in older adults where, as cartilage ages, there is a marked decrease in the fixed charge density (FCD), the hydration and, consequently, mechanical tension on the collagen type II network [9–11]. We have hypothesized that loss of tension on the collagen network accelerates degradation by MMP. Detection of the effect of MMP on loaded, native cartilage could lead to insight about cartilage degradation kinetics in OA. However, it is quite difficult to controllably deliver MMP to cartilage, to activate the MMP during detensioning of the collagen network and to detect the effect on the cartilage mechanics (because cost limits the amount of MMP used). We have developed a transpirational enzyme loading method which is capable of precisely dosing bovine cartilage explants with a small, known quantity of MMP-13. Following enzyme insertion, we are able to detect the activity of the MMP on osmotically compressed cartilage (i.e. cartilage with a detensioned collagen network) via a simple hydration measurement.
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Green, Abby M., Sebastien Landry, James P. Evans, Sophia Shalhout, Ashok S. Bhagwat, and Matthew D. Weitzman. "Abstract 3016: APOBEC3 enzymes induce damage to the cellular genome during DNA replication." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3016.

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Yang Hu and Jeffrey M Catchmark. "Incorporation of Cellulosic Degrading Enzymes into Bacterial Cellulose for Controlled Degradation in Wound Care Applications." In 2010 Pittsburgh, Pennsylvania, June 20 - June 23, 2010. American Society of Agricultural and Biological Engineers, 2010. http://dx.doi.org/10.13031/2013.29705.

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Reports on the topic "Cellulase enzymes"

1

Author, Not Given. Probing Product Binding in Cellulase Enzymes (Fact Sheet). Office of Scientific and Technical Information (OSTI), 2012. http://dx.doi.org/10.2172/1049585.

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Gladden, John. Production of extremophilic bacterial cellulase enzymes in aspergillus niger. Office of Scientific and Technical Information (OSTI), 2013. http://dx.doi.org/10.2172/1096445.

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Eveleigh, D., and J. Macmillan. Cellulase: A key enzyme for fermentation stocks. Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/6949102.

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Eveleigh, D. Cellulase: A key enzyme for fermentation feedstocks. Office of Scientific and Technical Information (OSTI), 1988. http://dx.doi.org/10.2172/6810692.

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Eveleigh, D., and J. Macmillan. Cellulase: A key enzyme for fermentation stocks. Office of Scientific and Technical Information (OSTI), 1989. http://dx.doi.org/10.2172/7101141.

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Renganathan, V. Oxidative enzymes involved in fungal cellulose degradation. Progress report, [May 15, 1992--May 14, 1994]. Office of Scientific and Technical Information (OSTI), 1992. http://dx.doi.org/10.2172/10156512.

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Eveleigh, D. E., and J. D. Macmillan. Cellulase - A Key Enzyme for Fermentation Feedstocks. Final report, Proposed Experimentation and Revised Budget. Office of Scientific and Technical Information (OSTI), 2000. http://dx.doi.org/10.2172/761224.

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Glycosylation Helps Cellulase Enzymes Bind to Plant Cell Walls (Fact Sheet). Office of Scientific and Technical Information (OSTI), 2012. http://dx.doi.org/10.2172/1044446.

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Computer Simulations Reveal Multiple Functions for Aromatic Residues in Cellulase Enzymes (Fact Sheet). Office of Scientific and Technical Information (OSTI), 2012. http://dx.doi.org/10.2172/1046309.

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The study of redox-active inorganic substituents of cellulase enzymes. Quarterly report, 25 August--25 November 1993. Office of Scientific and Technical Information (OSTI), 1993. http://dx.doi.org/10.2172/10145923.

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