Relevant bibliographies by topics / Cellulolytic bacteria; Hydrolytic; Cellulases

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Academic literature on the topic 'Cellulolytic bacteria; Hydrolytic; Cellulases'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 February 2022

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Journal articles on the topic "Cellulolytic bacteria; Hydrolytic; Cellulases"

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Stålbrand, Henrik, Shawn D. Mansfield, John N. Saddler, Douglas G. Kilburn, R. Antony J. Warren, and Neil R. Gilkes. "Analysis of Molecular Size Distributions of Cellulose Molecules during Hydrolysis of Cellulose by Recombinant Cellulomonas fimiβ-1,4-Glucanases." Applied and Environmental Microbiology 64, no. 7 (July 1, 1998): 2374–79. http://dx.doi.org/10.1128/aem.64.7.2374-2379.1998.

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ABSTRACT Four β-1,4-glucanases (cellulases) of the cellulolytic bacteriumCellulomonas fimi were purified from Escherichia coli cells transformed with recombinant plasmids. Previous analyses using soluble substrates had suggested that CenA and CenC were endoglucanases while CbhA and CbhB resembled the exo-acting cellobiohydrolases produced by cellulolytic fungi. Analysis of molecular size distributions during cellulose hydrolysis by the individual enzymes confirmed these preliminary findings and provided further evidence that endoglucanase CenC has a more processive hydrolytic activity than CenA. The significant differences between the size distributions obtained during hydrolysis of bacterial microcrystalline cellulose and acid-swollen cellulose can be explained in terms of the accessibility of β-1,4-glucan chains to enzyme attack. Endoglucanases and cellobiohydrolases were much more easily distinguished when the acid-swollen substrate was used.
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Uchiyama, Taku, Takayuki Uchihashi, Akihiko Nakamura, Hiroki Watanabe, Satoshi Kaneko, Masahiro Samejima, and Kiyohiko Igarashi. "Convergent evolution of processivity in bacterial and fungal cellulases." Proceedings of the National Academy of Sciences 117, no. 33 (August 3, 2020): 19896–903. http://dx.doi.org/10.1073/pnas.2011366117.

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Cellulose is the most abundant biomass on Earth, and many microorganisms depend on it as a source of energy. It consists mainly of crystalline and amorphous regions, and natural degradation of the crystalline part is highly dependent on the degree of processivity of the degrading enzymes (i.e., the extent of continuous hydrolysis without detachment from the substrate cellulose). Here, we report high-speed atomic force microscopic (HS-AFM) observations of the movement of four types of cellulases derived from the cellulolytic bacteriaCellulomonas fimion various insoluble cellulose substrates. The HS-AFM images clearly demonstrated that two of them (CfCel6B andCfCel48A) slide on crystalline cellulose. The direction of processive movement ofCfCel6B is from the nonreducing to the reducing end of the substrate, which is opposite that of processive cellulase Cel7A of the fungusTrichoderma reesei(TrCel7A), whose movement was first observed by this technique, whileCfCel48A moves in the same direction asTrCel7A. WhenCfCel6B andTrCel7A were mixed on the same substrate, “traffic accidents” were observed, in which the two cellulases blocked each other’s progress. The processivity ofCfCel6B was similar to those of fungal family 7 cellulases but considerably higher than those of fungal family 6 cellulases. The results indicate that bacteria utilize family 6 cellulases as high-processivity enzymes for efficient degradation of crystalline cellulose, whereas family 7 enzymes have the same function in fungi. This is consistent with the idea of convergent evolution of processive cellulases in fungi and bacteria to achieve similar functionality using different protein foldings.
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Gupta, Pratima, Kalpana Samant, and Avinash Sahu. "Isolation of Cellulose-Degrading Bacteria and Determination of Their Cellulolytic Potential." International Journal of Microbiology 2012 (2012): 1–5. http://dx.doi.org/10.1155/2012/578925.

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Eight isolates of cellulose-degrading bacteria (CDB) were isolated from four different invertebrates (termite, snail, caterpillar, and bookworm) by enriching the basal culture medium with filter paper as substrate for cellulose degradation. To indicate the cellulase activity of the organisms, diameter of clear zone around the colony and hydrolytic value on cellulose Congo Red agar media were measured. CDB 8 and CDB 10 exhibited the maximum zone of clearance around the colony with diameter of 45 and 50 mm and with the hydrolytic value of 9 and 9.8, respectively. The enzyme assays for two enzymes, filter paper cellulase (FPC), and cellulase (endoglucanase), were examined by methods recommended by the International Union of Pure and Applied Chemistry (IUPAC). The extracellular cellulase activities ranged from 0.012 to 0.196 IU/mL for FPC and 0.162 to 0.400 IU/mL for endoglucanase assay. All the cultures were also further tested for their capacity to degrade filter paper by gravimetric method. The maximum filter paper degradation percentage was estimated to be 65.7 for CDB 8. Selected bacterial isolates CDB 2, 7, 8, and 10 were co-cultured withSaccharomyces cerevisiaefor simultaneous saccharification and fermentation. Ethanol production was positively tested after five days of incubation with acidified potassium dichromate.
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Thomas, A., M. Laxmi, and A. Benny. "Bioethanol Production of Cellulase Producing Bacteria from Soils of Agrowaste Field." Journal of Scientific Research 13, no. 2 (May 1, 2021): 643–55. http://dx.doi.org/10.3329/jsr.v13i2.50574.

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With decades of studies on cellulose bioconversion, cellulases have been playing an important role in producing fermentable sugars from lignocellulosic biomass. Copious microorganisms that are able to degrade cellulose have been isolated and identified. The present study has been undertaken to isolate and screen the cellulase producing bacteria from soils of agrowaste field. Cellulase production has been qualitatively analyzed in carboxy methylcellulose (CMC) agar medium after congo red staining and NaCl treatment by interpretation with zones around the potent colonies. Out of the seven isolates, only two showed cellulase production. The morphogical and molecular characterization revealed its identity as Escherichia coli and Staphylococcus aureus. The potential of organisms for bioethanol production has been investigated using two substrates, namely, paper and leaves by subjecting with a pre-treatment process using acid hydrolysis to remove lignin which acts as physical barrier to cellulolytic enzymes. Ethanolic fermentation was done using Saccharomyces cerevisiae for 24-48 h and then the bioethanol produced was qualitatively proved by iodoform assay. These finding proves that ethanol can be made from the agricultural waste and the process is recommended as a means of generating wealth from waste.
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Neesa, Lutfun, Nasrin Jahan, Md Abdullah Al Noman Khan, and Mohammad Shahedur Rahman. "Cellulolytic Bacillus May or May Not Produce β -Glucosidase Due to Their Environmental Origin – A Case Study." Journal of Microbiology and Biotechnology Research 7, no. 6 (December 5, 2017): 30. http://dx.doi.org/10.24896/jmbr.2017764.

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Microbial cellulases have been drawing attention worldwide because of their massive capacity to process the most abundant cellulosic biomass into sustainable biofuels and other valuable products. Profitable biomass conversion processes are highly dependent on the use of efficient enzymes for lignocellulose degradation. Among the cellulose degrading enzymes, β-glucosidases are essential for efficient hydrolysis of cellulosic biomass as they relieve the inhibition of the cellobiohydrolases and endoglucanases by reducing cellobiose accumulation. In this study cellulolytic bacteria with potential β-glucosidases activity were isolated and screened from biogas plant effluent and dairy effluent near Jahangirnagar University campus. From initial screening a total of 16 isolates were found to have cellulolytic activity, among them three isolates (B1, B5, D4) were selected based on their superior results. All the three bacterial isolates were identified as B. subtilis (B1), Bacillus amyloliquefaciens (B5) and B. subtilis (D4) respectively based on their morphological, biochemical and molecular characteristics. The β-glucosidases activity of these three potential cellulolytic bacteria was performed by measuring the release of PNP using pNPG as a substrate and interestingly D4 strain was resulted with β-glucosidases negative where B1 strain was found to have efficient for β-glucosidases activity.
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Janatunaim, Rifqi Zahroh, Radhiyah Mardhiyah Hamid, Ghea Putri Christy, Yekti Asih Purwestri, and Woro Anindito Sri Tunjung. "Identification of BSA B1 Bacteria and Its Potency of Purified Cellulase to Hydrolyze Chlorella zofingiensis." Indonesian Journal of Biotechnology 20, no. 1 (November 8, 2016): 77. http://dx.doi.org/10.22146/ijbiotech.15277.

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Cellulase has been widely used as biocatalyst in industries. Production of cellulase from microorganismshas many advantages such as short production time and less expense. Our previous study indicated that oneof cellulolytic bacteria from digestive tract of milkfish (Chanos chanos), namely BSA B1, showed the highestcellulase activity. The objective of this study was to determine the phylogenetic of BSA B1 strain using 16SrRNA gene sequence. Furthermore, this study also determine the specific activity of purified cellulase from BSAB1 strain and its potency to hydrolyze Chlorella zofingiensis cellulose. Cellulase was purified using ammoniumsulphate precipitation, dialysis, and ion exchange chromatography. The purified cellulase was used to hydrolyzecellulose of C. zofingiensis. The result demonstrated that BSA B1 strain was closely related with Bacillus aeriusand Bacillus licheniformis. The specific activity of the crude enzyme was 1.543 U mL-1; after dialysis was 4.384 UmL-1; and after chromatography was 7.543 U mL-1. Purified cellulase exhibited activity in hydrolyzed both CMCand C. zofingiensis. Compared to commercial cellulase, purified cellulase had lower activity in hydrolyzed CMCbut higher activity in hydrolyzed C. zofingiensis. Ethanol dehydration could potentially increase the reducingsugar yield in cellulose hydrolysis when used appropriately. Morphology of C. zofingiensis cell has changedafter incubation with cellulases and ethanol dehydration indicated degradation of cell wall.
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Saini, Anita, Neeraj K. Aggarwal, Anuja Sharma, and Anita Yadav. "Actinomycetes: A Source of Lignocellulolytic Enzymes." Enzyme Research 2015 (December 17, 2015): 1–15. http://dx.doi.org/10.1155/2015/279381.

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Lignocellulose is the most abundant biomass on earth. Agricultural, forest, and agroindustrial activities generate tons of lignocellulosic wastes annually, which present readily procurable, economically affordable, and renewable feedstock for various lignocelluloses based applications. Lignocelluloses are the focus of present decade researchers globally, in an attempt to develop technologies based on natural biomass for reducing dependence on expensive and exhaustible substrates. Lignocellulolytic enzymes, that is, cellulases, hemicellulases, and lignolytic enzymes, play very important role in the processing of lignocelluloses which is prerequisite for their utilization in various processes. These enzymes are obtained from microorganisms distributed in both prokaryotic and eukaryotic domains including bacteria, fungi, and actinomycetes. Actinomycetes are an attractive microbial group for production of lignocellulose degrading enzymes. Various studies have evaluated the lignocellulose degrading ability of actinomycetes, which can be potentially implemented in the production of different value added products. This paper is an overview of the diversity of cellulolytic, hemicellulolytic, and lignolytic actinomycetes along with brief discussion of their hydrolytic enzyme systems involved in biomass modification.
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Chatterjee, Soumya, Sonika Sharma, Rajesh Kumar Prasad, Sibnarayan Datta, Dharmendra Dubey, Mukesh K. Meghvansi, Mohan G. Vairale, and Vijay Veer. "Cellulase Enzyme based Biodegradation of Cellulosic Materials: An Overview." South Asian Journal of Experimental Biology 5, no. 6 (March 11, 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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Bharadwaj, Vivek S., Brandon C. Knott, Jerry Ståhlberg, Gregg T. Beckham, and Michael F. Crowley. "The hydrolysis mechanism of a GH45 cellulase and its potential relation to lytic transglycosylase and expansin function." Journal of Biological Chemistry 295, no. 14 (February 13, 2020): 4477–87. http://dx.doi.org/10.1074/jbc.ra119.011406.

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Family 45 glycoside hydrolases (GH45) are endoglucanases that are integral to cellulolytic secretomes, and their ability to break down cellulose has been successfully exploited in textile and detergent industries. In addition to their industrial relevance, understanding the molecular mechanism of GH45-catalyzed hydrolysis is of fundamental importance because of their structural similarity to cell wall–modifying enzymes such as bacterial lytic transglycosylases (LTs) and expansins present in bacteria, plants, and fungi. Our understanding of the catalytic itinerary of GH45s has been incomplete because a crystal structure with substrate spanning the −1 to +1 subsites is currently lacking. Here we constructed and validated a putative Michaelis complex in silico and used it to elucidate the hydrolytic mechanism in a GH45, Cel45A from the fungus Humicola insolens, via unbiased simulation approaches. These molecular simulations revealed that the solvent-exposed active-site architecture results in lack of coordination for the hydroxymethyl group of the substrate at the −1 subsite. This lack of coordination imparted mobility to the hydroxymethyl group and enabled a crucial hydrogen bond with the catalytic acid during and after the reaction. This suggests the possibility of a nonhydrolytic reaction mechanism when the catalytic base aspartic acid is missing, as is the case in some LTs (murein transglycosylase A) and expansins. We calculated reaction free energies and demonstrate the thermodynamic feasibility of the hydrolytic and nonhydrolytic reaction mechanisms. Our results provide molecular insights into the hydrolysis mechanism in HiCel45A, with possible implications for elucidating the elusive catalytic mechanism in LTs and expansins.
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Gilbert, H. J., J. E. Rixon, R. S. Sharp, A. G. O'Donnell, and G. P. Hazlewood. "The use of genetically Lactobacillus plantarum in the ensilage process." Proceedings of the British Society of Animal Production (1972) 1993 (March 1993): 155. http://dx.doi.org/10.1017/s030822960002479x.

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Silage inoculants consisting of primarily Lactobacillus plantarum, are widely used to ensure that lactic acid bacteria dominate the fermentation of water soluble carbohydrates (WSC) during the ensilage process. Previous studies have shown that the supplementation of ensiled forage crops with cellulases can also improve the quality of silage through i) increasing the generation of WSC, and therefore ensuring an adequate supply of substrate for L. plantanim; ii) Partial hydrolysis of the plant cell wall increasing the rate of cellulose hydrolysis within the rumen. From the above discussion it is apparent that the use of an L.plantarum strain, with the capacity to hydrolyse cellulose, could be beneficial in the ensiling process. No celluloytic lactic bacterium has been isolated from microbial ecosystems. However, the advent of recombinant DNA technology affords us the possibility of engineering a cellulolytic derivative of L. plantarum. This report describes progress towards this objective.
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Dissertations / Theses on the topic "Cellulolytic bacteria; Hydrolytic; Cellulases"

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Torres, Marco Tulio Rincon. "Cellulosome organisation of plant cell wall degrading enzymes in Ruminococcus flavefaciens 17." Thesis, University of Aberdeen, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.327013.

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Book chapters on the topic "Cellulolytic bacteria; Hydrolytic; Cellulases"

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Mitsumori, Makoto. "Isolation of Cellulolytic Bacteria from the Rumen." In Cellulases, 57–65. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7877-9_5.

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Weimer, Paul J., and Christine L. Odt. "Cellulose Degradation by Ruminai Microbes: Physiological and Hydrolytic Diversity Among Ruminai Cellulolytic Bacteria." In ACS Symposium Series, 291–304. Washington, DC: American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1995-0618.ch018.

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