Relevant bibliographies by topics / Cellulase

Academic literature on the topic 'Cellulase'

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Published: 4 June 2021
Last updated: 28 July 2024

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Journal articles on the topic "Cellulase"

1

Ilić, Nevena, Marija Milić, Sunčica Beluhan, and Suzana Dimitrijević-Branković. "Cellulases: From Lignocellulosic Biomass to Improved Production." Energies 16, no. 8 (April 21, 2023): 3598. http://dx.doi.org/10.3390/en16083598.

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Cellulases are enzymes that are attracting worldwide attention because of their ability to degrade cellulose in the lignocellulosic biomass and transform it into highly demanded bioethanol. The enzymatic hydrolysis of cellulose by cellulases into fermentable sugars is a crucial step in biofuel production, given the complex structure of lignocellulose. Due to cellulases’ unique ability to hydrolyze the very recaltricant nature of lignocellulosic biomass, the cellulase market demand is rapidly growing. Although cellulases have been used in industrial applications for decades, constant effort is being made in the field of enzyme innovation to develop cellulase mixtures/cocktails with improved performance. Given that the main producers of cellulases are of microbial origin, there is a constant need to isolate new microorganisms as potential producers of enzymes important for biofuel production. This review provides insight into current research on improving microbial cellulase production as well as the outlook for the cellulase market with commercial cellulase preparation involved in industrial bioethanol production.
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Tokuda, Gaku, and Hirofumi Watanabe. "Hidden cellulases in termites: revision of an old hypothesis." Biology Letters 3, no. 3 (March 20, 2007): 336–39. http://dx.doi.org/10.1098/rsbl.2007.0073.

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The intestinal flagellates of termites produce cellulases that contribute to cellulose digestion of their host termites. However, 75% of all termite species do not harbour the cellulolytic flagellates; the endogenous cellulase secreted from the midgut tissue has been considered a sole source of cellulases in these termites. Using the xylophagous flagellate-free termites Nasutitermes takasagoensis and Nasutitermes walkeri , we successfully solubilized cellulases present in the hindgut pellets. Zymograms showed that the hindguts of these termites possessed several cellulases and contained up to 59% cellulase activity against crystalline cellulose when compared with the midgut. Antibiotic treatment administered to N. takasagoensis significantly reduced cellulase activity in the hindgut, suggesting that these cellulases were produced by symbiotic bacteria.
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Liu, Jun, and Huiren Hu. "The role of cellulose binding domains in the adsorption of cellulases onto fibers and its effect on the enzymatic beating of bleached kraft pulp." BioResources 7, no. 1 (January 11, 2012): 878–92. http://dx.doi.org/10.15376/biores.7.1.878-892.

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The adsorption of cellulases onto fibers may be one of the most important factors affecting the enzymatic reaction between cellulases and fibers. This study investigated the adsorption kinetics involved, using isothermal adsorption equations. Cellulose binding domains (CBDs) were isolated from a commercial cellulase, and their role in the adsorption and enzymatic reaction was evaluated. Approximately 13% to 24% of the refining energy was saved after northern bleached softwood kraft pulp samples were pretreated with full cellulase, CBDs, or cellulase lacking CBDs under optimal conditions. The absence of CBDs in cellulase resulted in less effective enzyme adsorption and hydrolysis of the fibers. These data suggest that pretreatment of northern bleached softwood kraft pulp with CBDs may not only improve the beating degree of the pulp and reduce refining energy consumption but also improve the tensile index of the handsheet. Analysis of the degree of cellulose crystallinity and fiber surface morphology by X-ray diffraction and scanning electron microscopy revealed that the CBDs in cellulase help modify the crystalline area and facilitate the enzymatic degradation of cellulose. The adsorption parameters of the cellulases calculated from isothermal adsorption experiments confirmed the role of CBDs in the adsorption of cellulases onto fibers.
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Brumm, Phillip, Phillip Brumm, Dan Xie, Dan Xie, Larry Allen, Larry Allen, David A. Mead, and David A. Mead. "Hydrolysis of Cellulose by Soluble Clostridium Thermocellum and Acidothermus Cellulolyticus Cellulases." Journal of Enzymes 1, no. 1 (April 26, 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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Feng, Yue, Hui-Qin Liu, Run-Cang Sun, and Jian-Xin Jiang. "Enzymatic hydrolysis of cellulose from steam-pretreated Lespedeza stalk (Lespedeza crytobotrya) with four Trichoderma cellulases." BioResources 6, no. 3 (June 7, 2011): 2776–89. http://dx.doi.org/10.15376/biores.6.3.2776-2789.

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The hydrolytic potential of cellulases produced by Trichoderma viride, Trichoderma pseudokoningii, Trichoderma koningii, and Trichoderma reesei with addition of exogenous β-glucosidase was evaluated on cellulose of steam-pretreated Lespedeza. The T. viride enzyme achieved the highest glucose conversion (90.09%), while T. pseudokoningii cellulase achieved the highest ratio of cellobiose to glucose (4.94%) at the end of hydrolysis. Enzymatic adsorption on the substrate was evaluated on filter paper activity and β-glucosidase activity in the corresponding digest with the obtained T. cellulases. T. viride cellulase possessed an efficient adsorption-desorption on the substrate and reached the highest FPA difference (0.72 U/mL) among enzyme activities, indicating to its excellent hydrolysis capability. However, β-glucosidase in T. viride cellulase system showed close bonding on the substrate, suggesting that efficiencies of adsorption-desorption on the cellulose are different between the entire cellulase system and β-glucosidase. T. viride cellulase, with active endogenous β-glucosidase (1.60 U/mL), has compatible synergism with the additional exogenous β-glucosidase.
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Aro, Nina, Marja Ilmén, Anu Saloheimo, and Merja Penttilä. "ACEI of Trichoderma reesei Is a Repressor of Cellulase and Xylanase Expression." Applied and Environmental Microbiology 69, no. 1 (January 2003): 56–65. http://dx.doi.org/10.1128/aem.69.1.56-65.2003.

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ABSTRACT We characterized the effect of deletion of the Trichoderma reesei (Hypocrea jecorina) ace1 gene encoding the novel cellulase regulator ACEI that was isolated based on its ability to bind to and activate in vivo in Saccharomyces cerevisiae the promoter of the main cellulase gene, cbh1. Deletion of ace1 resulted in an increase in the expression of all the main cellulase genes and two xylanase genes in sophorose- and cellulose-induced cultures, indicating that ACEI acts as a repressor of cellulase and xylanase expression. Growth of the strain with a deletion of the ace1 gene on different carbon sources was analyzed. On cellulose-based medium, on which cellulases are needed for growth, the Δace1 strain grew better than the host strain due to the increased cellulase production. On culture media containing sorbitol as the sole carbon source, the growth of the strain with a deletion of the ace1 gene was severely impaired, suggesting that ACEI regulates expression of other genes in addition to cellulase and xylanase genes. A strain with a deletion of the ace1 gene and with a deletion of the ace2 gene coding for the cellulase and xylanase activator ACEII expressed cellulases and xylanases similar to the Δace1 strain, indicating that yet another activator regulating cellulase and xylanase promoters was present.
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Nicomrat, Duongruitai, and Jirasak Tharajak. "Synergistic Effects of Cellulase-Producing Microorganisms for Future Bioconversion of Lignocellulosic Biomass." Applied Mechanics and Materials 804 (October 2015): 255–58. http://dx.doi.org/10.4028/www.scientific.net/amm.804.255.

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Lignocellulosic biomass can nowadays be bioconverted to value-added biofuels by numerous cellulases purified from diverse microbes. In nature, complex microbial communities produce multifunctional cellulase systems with broader substrate utilization and act sequentially in the synergistic action by subsequently converting cellulose into an utilizable energy source and glucose. This research was to apply cellulase producing isolates based on their possible synergistic action to degrade complex cellulose containing biomass. In the study, the microorganism species, isolated species from durian peels after macerated for 3 days and shown for their high biodegradation activity, Bacillus spp. (B12, B13, and B16) and Pseudomonas spp., (B23 and B55), could express high cellulase activity on carboxymethylcellulose (CMC) and filter paper (FP). Bacillus spp. B13 and B16 showed high cellulase activity on soluble cellulose of CMC while B12 and B55 displayed high cellulase activity on crystalline insoluble cellulose of FP. To observe the synergistic effect of the cellulase-producing consortia, co-cultures of B12,B23 and F23 were grew well on both CMC and FP. Therefore, these findings of synergistic effects of microbial consortia could bring us a future work to develop high efficient cellulase producing systems for further industry application.
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Singh, Nivisti, Bishop Bruce Sithole, and Roshini Govinden. "Optimisation of β-Glucosidase Production in a Crude Aspergillus japonicus VIT-SB1 Cellulase Cocktail Using One Variable at a Time and Statistical Methods and its Application in Cellulose Hydrolysis." International Journal of Molecular Sciences 24, no. 12 (June 9, 2023): 9928. http://dx.doi.org/10.3390/ijms24129928.

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Pulp and paper mill sludge (PPMS) is currently disposed of into landfills which are reaching their maximum capacity. Valorisation of PPMS by enzymatic hydrolysis using cellulases is an alternative strategy. Existing commercial cellulases are expensive and contain low titres of β-glucosidases. In this study, β-glucosidase production was optimised by Aspergillus japonicus VIT-SB1 to obtain higher β-glucosidase titres using the One Variable at a Time (OVAT), Plackett Burman (PBD), and Box Behnken design (BBD)of experiments and the efficiency of the optimised cellulase cocktail to hydrolyse cellulose was tested. β-Glucosidase production was enhanced from 0.4 to 10.13 U/mL, representing a 25.3-fold increase in production levels after optimisation. The optimal BBD production conditions were 6 days of fermentation at 20 °C, 125 rpm, 1.75% soy peptone, and 1.25% wheat bran in (pH 6.0) buffer. The optimal pH for β-glucosidase activity in the crude cellulase cocktail was (pH 5.0) at 50 °C. Optimal cellulose hydrolysis using the crude cellulase cocktail occurred at longer incubation times, and higher substrate loads and enzyme doses. Cellulose hydrolysis with the A. japonicus VIT-SB1 cellulase cocktail and commercial cellulase cocktails resulted in glucose yields of 15.12 and 12.33 µmol/mL glucose, respectively. Supplementation of the commercial cellulase cocktail with 0.25 U/mg of β-glucosidase resulted in a 19.8% increase in glucose yield.
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Hwang, In Sun, Eom-Ji Oh, Han Beoyl Lee, and Chang-Sik Oh. "Functional Characterization of Two Cellulase Genes in the Gram-Positive Pathogenic Bacterium Clavibacter michiganensis for Wilting in Tomato." Molecular Plant-Microbe Interactions® 32, no. 4 (April 2019): 491–501. http://dx.doi.org/10.1094/mpmi-08-18-0227-r.

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Diverse plant pathogens secrete cellulases to degrade plant cell walls. Previously, the plasmid-borne cellulase gene celA was shown to be important for the virulence of the gram-positive bacterium Clavibacter michiganensis in tomato. However, details of the contribution of cellulases to the development of wilting in tomato have not been well-determined. To better understand the contribution of cellulases to the virulence of C. michiganensis in tomato, a mutant lacking cellulase activity was generated and complemented with truncated forms of certain cellulase genes, and virulence of those strain was examined. A celA mutant of the C. michiganensis type strain LMG7333 lost its cellulase activity and almost all its ability to cause wilting in tomato. The cellulase catalytic domain and cellulose-binding domain of CelA together were sufficient for both cellulase activity and the development of wilting in tomato. However, the expansin domain did not affect virulence or cellulase activity. The celA ortholog of Clavibacter sepedonicus restored the full virulence of the celA mutant of C. michiganensis. Another cellulase gene, celB, located in the chromosome, carries a single-base deletion in most C. michiganensis strains but does not carry a functional signal peptide in its N terminus. Nevertheless, an experimentally modified CelB protein with a CelA signal peptide was secreted and able to cause wilting in tomato. These results indicate that cellulases are major virulence factors of C. michiganensis that causes wilting in tomato. Furthermore, there are natural variations among cellulase genes directly affecting their function.
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Zhou, Qingxin, Jintao Xu, Yanbo Kou, Xinxing Lv, Xi Zhang, Guolei Zhao, Weixin Zhang, Guanjun Chen, and Weifeng Liu. "Differential Involvement of β-Glucosidases from Hypocrea jecorina in Rapid Induction of Cellulase Genes by Cellulose and Cellobiose." Eukaryotic Cell 11, no. 11 (September 21, 2012): 1371–81. http://dx.doi.org/10.1128/ec.00170-12.

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ABSTRACTAppropriate perception of cellulose outside the cell by transforming it into an intracellular signal ensures the rapid production of cellulases by cellulolyticHypocrea jecorina. The major extracellular β-glucosidase BglI (CEL3a) has been shown to contribute to the efficient induction of cellulase genes. Multiple β-glucosidases belonging to glycosyl hydrolase (GH) family 3 and 1, however, exist inH. jecorina. Here we demonstrated that CEL1b, like CEL1a, was an intracellular β-glucosidase displayingin vitrotransglycosylation activity. We then found evidence that these two major intracellular β-glucosidases were involved in the rapid induction of cellulase genes by insoluble cellulose. Deletion ofcel1aandcel1bsignificantly compromised the efficient gene expression of the major cellulase gene,cbh1. Simultaneous absence of BglI, CEL1a, and CEL1b caused the induction of the cellulase gene by cellulose to further deteriorate. The induction defect, however, was not observed with cellobiose. The absence of the three β-glucosidases, rather, facilitated the induced synthesis of cellulase on cellobiose. Furthermore, addition of cellobiose restored the productive induction on cellulose in the deletion strains. The results indicate that the three β-glucosidases may not participate in transforming cellobiose beyond hydrolysis to provoke cellulase formation inH. jecorina. They may otherwise contribute to the accumulation of cellobiose from cellulose as inducing signals.
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Dissertations / Theses on the topic "Cellulase"

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Gal, Laurent. "Etude du cellulosome de Clostridium cellulolyticum et de l'un de ses composants : la cellulase CelG." Aix-Marseille 1, 1997. http://www.theses.fr/1997AIX11071.

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Le cellulosome de la bacterie cellulolytique clostridium cellulolyticum atcc 35319 a ete etudie. C'est un complexe de 600 kda, en moyenne, qui degrade efficacement la cellulose cristalline. Il est constitue de plusieurs proteines de masse moleculaire relative variant entre 170 et 30 kda. L'utilisation du minicipc1 biotinyle a permis de montrer qu'au moins treize d'entre elles possedaient une dockerine. Parmi celles-ci, les proteines cela, celc, cele, celf et celg, dont les genes sont clones et sequences, ont ete identifiees. Afin de rechercher de nouveaux genes cel codant pour des proteines possedant une dockerine, une marche sur le chromosome en aval de cele a ete entreprise. Elle a revele l'existence de trois nouveaux genes impliques dans la cellulolyse : cipx, celh et celj. - cipx est une proteine tres originale constituee d'un domaine de type linker et d'une cohesine. - celh et celj, tout comme celg, possedent un domaine catalytique de la famille 9 de la classification des glycosyl-hydrolases, suivi d'un domaine de type cbd de la famille iii et enfin d'une dockerine c-terminale. Pour tenter de comprendre le role joue par ce dernier type de proteines dans la cellulolyse, la caracterisation biochimique de celg a ete entreprise. Le gene celg a ete surexprime chez escherichia coli et la proteine recombinante correspondante a ete purifiee. Celg est une endoglucanase qui degrade efficacement la cmc et le glucane d'orge. Elle est egalement active sur la cellulose amorphe et degrade les cellodextrines ayant un degre de polymerisation superieur ou egal a trois. Contrairement aux autres endoglucanases caracterisees jusqu'a present chez c. Cellulolyticum, celg degrade les celluloses cristallines, et en particulier la bmcc de maniere tres efficace. Pour etudier l'influence relative de chacun des domaines de celg dans ce mecanisme, differentes constructions genetiques, permettant la synthese du domaine catalytique seul ou du domaine de type cbd fusionne derriere la glutathion-s-transferase, ont ete realisees. Dans tous les cas, les proteines recombinantes ne presentent ni activite catalytique ni proprietes d'adhesion a la cellulose. L'ensemble de ces resultats suggere qu'a la difference de la plupart des cellulases, les differents domaines constitutifs de celg ne sont pas independants. La presence d'au moins deux autres proteines homologues a celg (celh et celj) au sein du systeme cellulolytique de c. Cellulolyticum suggere que ces proteines jouent un role fondamental dans les mecanismes de degradation de la cellulose chez cet organisme.
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2

Thomas, D. J. "Microbial cellulase systems." Thesis, Swansea University, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.639202.

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The work presented studies the cellulolytic system of Trichoderma koningii with particular reference to its ability to produce "short fibres" in the early stages of cellulose degradation. The culture filtrate of this organism was shown to produce short fibres from both filter paper (Whatman No.1) and cotton (Texas, non-dewaxed). The optimum conditions for production were identified and an assay system developed to measure this activity. Assay using filter paper was rapid and sensitive in determining short fibre producing activity, all results were subsequently confirmed on the more resistant substrate (cotton). The cellulase system was separated using an ion exchanger with a non-carbohydrate matrix and affinity chromatography on cellulose. Initial separation on ion exchange yielded the main cellobiohydrolase (CBH 1). Another fraction from this column separated on cellulose columns gave purified fractions of β-glucosidase, CM-cellulase and the short fibres forming activity (D2Cc). Only this latter fraction produced short fibres and synergised with CM-cellulase and β-glucosidase to increase short fibre production. Short fibres produced by D2Cc were more susceptible to subsequent hydrolysis by culture filtrate or CBH 1, degraded (bacterial) cellulose showed no physical changes on action of D2Cc but subsequent hydrolysis by CBH 1 or culture filtrate was increased. The main product of D2Cc was cellobiose but some cellotriose was detected from filter paper. D2Cc was inactive against cellobiose and cellotriose, both were potent inhibitors of D2Cc activity. Cellobiose was also an inhibitor of CBH 1 but cellotriose was not. D2Cc was shown to reduce the DP of bacterial cellulose. D2Cc and CBH 1 synergised in hydrolysing degraded cellulose, filter paper and cotton. The suggested role for this enzyme component is that it produces short fibres in concert with CM-cellulase which are then attacked by CBH 1 to produce cellobiose which is utilized by the organism.
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Tchunden, Jeannette. "Cellulolyse Anaérobie Mésophile : étude de l'amélioration de la production de cellulases par Cl. cellulolyticum ATCC 35319." Nancy 1, 1990. http://docnum.univ-lorraine.fr/public/SCD_T_1990_0044_TCHUNDEN.pdf.

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Cl. Cellulolyticum est une bactérie cellulolytique mésophile isolée au laboratoire à partir d'herbes en décomposition. Cette bactérie est capable de dégrader la cellulose en une seule étape en acides organiques et en éthanol. Mais l'activité cellulolytique de la souche reste faible. Pour arriver à une possibilité d'utilisation industrielle de la bactérie, les performances cellulolytiques de la souche doivent être améliorées. L'amélioration de la production de cellulases par cl. Cellulolyticum passe à la fois par l'amélioration de ses conditions de culture et l'amélioration de la souche. Ainsi nous avons montré qu'une culture en fermenteur avec régulation de ph à 7,2 par une solution d'ammoniac 4n conduit à une plus forte production de cellulases. Par l'emploi du rayonnement ultraviolet comme agent mutagène et de cellobiose comme crible de sélection, nous avons isolé le mutant 42 qui produit deux fois plus de cellulases que la souche parent. Nous avons également montré que la cellulose avicel est meilleure inductrice de l'endo et de l'exoglucanase aussi bien chez cl. Cellulolyticum que chez le mutant. L'étude de l'association de cl. Cellulolyticum et du mutant 42 a permis de produire 4,7 fois plus d'activité xylanasique.
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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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Qian, Chen. "Adsorption of Xyloglucan onto Cellulose and Cellulase onto Self-assembled Monolayers." Thesis, Virginia Tech, 2012. http://hdl.handle.net/10919/42496.

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Adsorption of xyloglucan (XG) onto thin desulfated nanocrystalline cellulose (DNC) films was studied by surface plasmon resonance spectroscopy (SPR), quartz crystal microbalance with dissipation monitoring (QCM-D), and atomic force microscopy (AFM) measurements. These studies were compared to adsorption studies of XG onto thin sulfated nanocrystalline cellulose (SNC) films and regenerated cellulose (RC) films performed by others. Collectively, these studies show the accessible surface area is the key factor for the differences in surface concentrations observed for XG adsorbed onto the three cellulose surfaces. XG penetrated into the porous nanocrystalline cellulose films. In contrast, XG was confined to the surfaces of the smooth, non-porous RC films. Surprisingly surface charge and cellulose morphology played a limited role on XG adsorption. The effect of the non-ionic surfactant Tween 80 on the adsorption of cellulase onto alkane thiol self-assembled monolayers (SAMs) on gold was also studied. Methyl (-CH3), hydroxyl (-OH) and carboxyl (-COOH) terminated SAMs were prepared. Adsorption of cellulase onto untreated and Tween 80-treated SAMs were monitored by SPR, QCM-D and AFM. The results indicated cellulase adsorption onto SAM-CH3 and SAM-COOH were driven by strong hydrophobic and electrostatic interactions, however, hydrogen bonding between cellulase and SAM-OH was weak. Tween 80 effectively hindered the adsorption of cellulase onto hydrophobic SAM-CH3 substrates. In contrast, it had almost no effect on the adsorption of cellulase onto SAM-OH and SAM-COOH substrates because of its reversible adsorption on these substrates.
Master of Science
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Du, Plessis Lisa. "Co-expression of cellulase genes in Saccharomyces cerevisiae for cellulose degradation." Thesis, Link to the online version, 2008. http://hdl.handle.net/10019/1818.

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Zhu, Zhiguang. "Investigating biomass saccharification for the production of cellulosic ethanol." Thesis, Virginia Tech, 2009. http://hdl.handle.net/10919/32189.

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The production of second generation biofuels -- cellulosic ethanol from renewable lignocellulosic biomass has the potential to lead the bioindustrial revolution necessary to the transition from a fossil fuel-based economy to a sustainable carbohydrate economy. Effective release of fermentable sugars through biomass pretreatment followed by enzymatic hydrolysis is among the most costly steps for emerging cellulosic ethanol biorefineries. In this project, two pretreatment methods (dilute acid, DA, and cellulose solvent- and organic solvent-lignocellulose fractionation, COSLIF) for corn stover were compared. It was found that glucan digestibility of the corn stover pretreated by COSLIF was much higher, along with faster hydrolysis rate, than that by DA- pretreated. This difference was more significant at a low enzyme loading. Quantitative measurements of total substrate accessibility to cellulase (TSAC), cellulose accessibility to cellulase (CAC), and non-cellulose accessibility to cellulase (NCAC) based on adsorption of a non-hydrolytic recombinant protein TGC were established to find out the cause. The COSLIF-pretreated corn stover had a CAC nearly twice that of the DA-pretreated biomass. Further supported by qualitative scanning electron microscopy images, these results suggested that COSLIF treatment disrupted microfibrillar structures within biomass while DA treatment mainly removed hemicelluloses, resulting in a much less substrate accessibility of the latter than of the former. It also concluded that enhancing substrate accessibility was the key to an efficient bioconversion of lignocellulose. A simple method for determining the adsorbed cellulase on cellulosic materials or pretreated lignocellulose was established for better understanding of cellulase adsorption and desorption. This method involved hydrolysis of adsorbed cellulase in the presence of 10 M of NaOH at 121oC for 20 min, followed by the ninhydrin assay for the amino acids released from the hydrolyzed cellulase. The major lignocellulosic components (i.e. cellulose, hemicellulose, and lignin) did not interfere with the ninhydrin assay. A number of cellulase desorption methods were investigated, including pH adjustment, detergents, high salt solution, and polyhydric alcohols. The pH adjustment to 13.0 and the elution by 72% ethylene glycol at a neutral pH were among the most efficient approaches for desorbing the adsorbed cellulase. For the recycling of active cellulase, a modest pH adjustment to 10.0 may be a low-cost method to desorb active cellulase. More than 90% of cellulase for hydrolysis of the pretreated corn stover could be recycled by washing at pH 10.0. This study provided an in-depth understanding of biomass saccharification for the production of cellulosic ethanol for cellulose hydrolysis and cellulase adsorption and desorption. It will be of great importance for developing better lignocellulose pretreatment technologies and improving cellulose hydrolysis by engineered cellulases.
Master of Science
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Mayende, Lungisa. "Isolation of a Clostridium Beijerinckii sLM01 cellulosome and the effect of sulphide on anaerobic digestion." Thesis, Rhodes University, 2007. http://hdl.handle.net/10962/d1004032.

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Cellulose is the most abundant and the most resistant and stable natural organic compound on earth. Enzyme hydrolysis is difficult because of its insolubility and heterogeneity. Some (anaerobic) microorganisms have overcome this by having a multienzyme system called the cellulosome. The aims of the study were to isolate a mesophilic Clostridium sp. from a biosulphidogenic bioreactor, to purify the cellulosome from this culture, to determine the cellulase and endoglucanase activities using Avicel and carboxymethylcellulose (CMC) as substrates and the dinitrosalicyclic (DNS) method. The organism was identified using 16S rDNA sequence analysis. The sequence obtained indicated that a strain of Clostridium beijerinckii was isolated. The cellulosome was purified from the putative C. beijerinckii sLM01 host culture using affinity chromatography purification and affinity digestion purification procedures. The cellulosomal and non-cellulosomal fractions of C. beijerinckii sLM01 were separated successfully, but the majority of the endoglucanase activity was lost during the Sepharose 4B chromatography step. These cellulosomal and non-cellulosomal fractions were characterised with regards to their pH and temperature optima and effector sensitivity. Increased additions of sulphide activated the cellulase activity of the cellulosomal and non-cellulosomal fractions up to 700 %, while increased additions of sulphate either increased the activity slightly or inhibited it dramatically, depending on the cellulosomal and non-cellulosomal fractions. Increased additions of cellobiose, glucose and acetate inhibited the cellulase and endoglucanase activities. pH optima of 5.0 and 7.5 were observed for cellulases and 5.0 for endoglucanases of the cellulosomal fraction. The noncellulosomal fraction exhibited a pH optimum of 7.5 for both cellulase and endoglucanase activities. Both fractions and enzymes exhibited a temperature optimum of 30 °C. The fundamental knowledge gained from the characterisation was applied to anaerobic digestion, where the effect of sulphide on the rate-limiting step was determined. Sulphide activated cellulase and endoglucanase activities and increased the % chemical oxygen demand (COD) removal rate. Levels of volatile fatty acids (VFAs) were higher in the bioreactor containing sulphide, substrate and C. beijerinckii. Sulphide therefore accelerated the rate-limiting step of anaerobic digestion.
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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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Roussos, Sevastianos. "Croissance de Trichoderma harzianum par fermentation en milieu solide : physiologie, sporulation et production de cellulases /." Paris : Ed. de l'ORSTOM, 1987. http://catalogue.bnf.fr/ark:/12148/cb349545941.

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Books on the topic "Cellulase"

1

Clarke, Anthony J. Biodegradation of cellulose: Enzymology and biotechnology. Lancaster, Pa: Technomic Pub. Co., 1996.

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

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Knowles, Jonathan. Cellulase families and their genes. New York: Elsevier, 1987.

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Golan, Adam E. Cellulase: Types and action, mechanism, and uses. New York, N.Y: Nova Science Publishers, 2011.

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Kim, Seung Wook. Cellulase production in an airlift fermenter. Birmingham: University of Birmingham, 1988.

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Hamilton, Lesley Ann. An examination of a fungal cellulase system. Birmingham: University of Birmingham, 1992.

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McGrath, Claire C. Cellulase activity in the freshwater amphipod Gammarus lacustris. Schaumburg, IL: North American Benthological Society, 2000.

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Gough, Clare Linda. Molecular genetics of cellulase production by "Xanthomonas campestris". Norwich: University of EastAnglia, 1989.

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Reade, Austin E. Cellulase from the white-rot fungus, Polyporus anceps. Ottawa: the Branch, 1988.

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Cooper, Victoria Joyce Courtice. Analysis of the major cellulase of Erwinia carotovora. [s.l.]: typescript, 1992.

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Book chapters on the topic "Cellulase"

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Schomburg, Dietmar, and Margit Salzmann. "Cellulase." In Enzyme Handbook 4, 29–39. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_4.

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Gooch, Jan W. "Cellulase." In Encyclopedic Dictionary of Polymers, 127. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_2100.

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Elliston, K. O., M. D. Yablonsky, and D. E. Eveleigh. "Cellulase." In ACS Symposium Series, 290–300. Washington, DC: American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0460.ch022.

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Stellmach, Bruno. "Cellulase." In Bestimmungsmethoden Enzyme, 82–97. Heidelberg: Steinkopff, 1988. http://dx.doi.org/10.1007/978-3-642-93668-5_9.

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Ding, Hanshu, and Feng Xu. "Productive Cellulase Adsorption on Cellulose." In ACS Symposium Series, 154–69. Washington, DC: American Chemical Society, 2004. http://dx.doi.org/10.1021/bk-2004-0889.ch009.

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Zhang, Y. H. Percival, Jiong Hong, and Xinhao Ye. "Cellulase Assays." In Methods in Molecular Biology, 213–31. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-214-8_14.

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Wood, T. M. "Cellulase Mechanisms." In Biodeterioration 7, 333–46. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1363-9_44.

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Adney, William S., Christine I. Ehrman, John O. Baker, Steven R. Thomas, and Michael E. Himmel. "Cellulase Assays." In ACS Symposium Series, 218–35. Washington, DC: American Chemical Society, 1994. http://dx.doi.org/10.1021/bk-1994-0566.ch010.

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Naga Raju, Maddela, Narasimha Golla, and Rangaswamy Vengatampalli. "Soil Cellulase." In SpringerBriefs in Environmental Science, 25–30. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-42655-6_6.

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Wilson, David B., and Maxim Kostylev. "Cellulase Processivity." In Biomass Conversion, 93–99. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-956-3_9.

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Conference papers on the topic "Cellulase"

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Mekhantseva, K. V., N. G. Vasilchenko, and V. A. Chistyakov. "STUDY OF THE CELLULASE ACTIVITY OF BACTERIAL STRAINS, UNDERLYING THE BIOLOGICAL PLANT PROTECTION PRODUCT “CODE OF BALANCE F1”, WHICH ARE POTENTIALLY CAPABLE OF CELLULOSE DECOMPOSITION." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-104.

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When decomposing stable residues, strains that are capable of decomposing cellulose with the help of enzymes from the cellulase group are used. Cellulase activity of bacterial strains isolated from the rhizosphere zone of plants in the Krasnodar Territory was assumed: 8 strains of the genus Bacillus and 2 strains of the genus Paenbacillus. It turned out that 4 strains have high cellulase activity and can be neglected as possible decomposers of crop residues.
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Chen, Xiao-Quan, Xue-Yan Deng, Wen-Hao Shen, and Meng-Yu Jia. "Preparation and Characterization of Spherical Nanosized Cellulose by Enzymatic Hydrolysis of Pulp Fibers." In Advances in Pulp and Paper Research, Oxford 2017. Fundamental Research Committee (FRC), Manchester, 2017. http://dx.doi.org/10.15376/frc.2017.2.785.

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In this work, the pulp fibers were enzymolyzed to prepare the nano-sized cellulose (NC). The as-prepared samples were characterized by optical microscopy, electron microscopy, and Raman spectra. The experimental results indicated that enzymatic hydrolysis of pulp fibers could produce the spherical NC with a mean particle size of about 30 nm, which has the excellent monodispersity and uniformity. When the concentration of complex enzymes was 20 u/mL (cellulase: xylanase = 9:1), the yield of NC was 13.6%. The single cellulase was used, even if the concentration and time reached up to 200 u/mL, only a mixture of trip and granular flocculation were obtained. The positive synergistic effect between xylanase and cellulase could be due to the enzymolysis of hemicellulose located on the cellulose microfibers to favorable of cutting and splitting of the microfibers by the endoglycannase in cellulase. Otherwise, the additive copper sulfate could decrease formation of reducing sugar effectively.
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Sultana, Sharmin, Md Sad Salabi Sawrav, Snygdha Rani Das, Mehfuz Alam, Md Abdul Aziz, Md Al-Amin Hossain, and Md Azizul Haque. "Isolation and Biochemical Characterization of Cellulase Producing Goat Rumen Bacteria." In International Conference on Emerging Trends in Engineering and Advanced Science. AIJR Publisher, 2022. http://dx.doi.org/10.21467/proceedings.123.12.

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Cellulose is the most prevalent polymer on the planet and has long been utilized for a variety of industrial applications. The study's goal was to screen and isolate cellulase-producing bacteria from the rumen of a goat collected from different location of Dinajpur district. To do so, rumen content samples from two distinct goats were collected. In this investigation, rumen cellulase-producing bacteria were isolated and characterized after serial dilution of five isolates up to six fold and inoculation into Nutrient agar. Following that, all of the isolates were underwent Methyl Red (MR) test & Voges-Proskauer (VP) test to identify organism’s metabolic pathway, Triple Sugar Iron Agar (TSI) Test to determine bacterial ability to utilize sugar, Motility Indole and Urease activity test (MIU) to determine motility, Urease utilization and can produce Indole or not, Citrate utilization test to utilize citrate as carbon and energy source, Oxidase test, Catalase test to check the presence of catalytic enzyme. The result revealed the colonial characterization of bacteria and also where proven all five isolates are promising enough and superior in quality to produce cellulose.
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Liu, Yu-San, Yonghua Luo, John O. Baker, Yining Zeng, Michael E. Himmel, Steve Smith, and Shi-You Ding. "A single molecule study of cellulase hydrolysis of crystalline cellulose." In BiOS, edited by Jörg Enderlein, Zygmunt K. Gryczynski, and Rainer Erdmann. SPIE, 2010. http://dx.doi.org/10.1117/12.840975.

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Mari S. Chinn, Sue E. Nokes, and Herbert J. Strobel. "Bacterial Cellulase: A Review." In 2001 Sacramento, CA July 29-August 1,2001. St. Joseph, MI: American Society of Agricultural and Biological Engineers, 2001. http://dx.doi.org/10.13031/2013.7507.

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Krusir, G. V., O. A. Sagdeeva, A. S. Gnezdovsky, and A. L. Tsykalo. "INVESTIGATION OF THE SOLID WASTE ENZYMATIC DEGRADATION OF THE ENTERPRISES OF THE FRUIT AND VEGETABLE CANNING INDUSTRY." In SAKHAROV READINGS 2021: ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. International Sakharov Environmental Institute of Belarusian State University, 2021. http://dx.doi.org/10.46646/sakh-2021-2-184-188.

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The work is devoted to the study of the solid waste enzymatic destruction process from fruit and vegetable canning enterprises for the introduction of an improved technology for their utilization and the creation of an optimally balanced feed additive. Enzymatic destruction of cellulose in the waste composition by cellulase under the microorganisms influence is the basis of the biotechnological process. The main characteristics of the enzymatic destruction process have been determined and data have been obtained for improving the technology of solid waste utilization from enterprises of the canning industry. Comparative analysis of bioconversion of the waste various types proves that enzymatic destruction by cellulase is effective specifically for the fruit and vegetable pomace in the waste composition, allows you to obtain a valuable feed additive from them and reduce the stress level on the environment.
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Song, Bo, Ning Xi, Ruiguo Yang, Zhiyong Sun, and Liangliang Chen. "In situ visualization of dynamic interactions of cellulase and cellulose molecules." In 2014 IEEE 14th International Conference on Nanotechnology (IEEE-NANO). IEEE, 2014. http://dx.doi.org/10.1109/nano.2014.6968134.

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Yue, Wenxi, and Ming Sui. "Diversity analysis of paenibacillus cellulase." In 2017 4th International Conference on Machinery, Materials and Computer (MACMC 2017). Paris, France: Atlantis Press, 2018. http://dx.doi.org/10.2991/macmc-17.2018.73.

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SILVA, H. N. L., G. S. SALOMÃO, T. S. LIRA, and L. M. PINOTTI. "CELLULASE PRODUCTION BY Bacillus subtilis." In XXII Congresso Brasileiro de Engenharia Química. São Paulo: Editora Blucher, 2018. http://dx.doi.org/10.5151/cobeq2018-pt.0907.

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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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Reports on the topic "Cellulase"

1

Doi, R. H. Characterization and expression of Clostridium cellulase genes. Office of Scientific and Technical Information (OSTI), January 1989. http://dx.doi.org/10.2172/5640368.

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

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

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Walker, Larry P. ,. Bergstrom, Gary, Stephane Corgie, Harold Craighead, Donna Gibson, and David Wilson. Addressing the Recalcitrance of Cellulose Degradation through Cellulase Discovery, Nano-scale Elucidation of Molecular Mechanisms, and Kinetic Modeling. Office of Scientific and Technical Information (OSTI), June 2011. http://dx.doi.org/10.2172/1016086.

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

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Jarnigan, Alisha. Enhancing Cellulase Commercial Performance for the Lignocellulosic Biomass Industry. Office of Scientific and Technical Information (OSTI), June 2016. http://dx.doi.org/10.2172/1255837.

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Wilson, D. B. (Studies of the genetic regulation of the Thermomonospora cellulase complex). Office of Scientific and Technical Information (OSTI), January 1992. http://dx.doi.org/10.2172/7239659.

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Walker, L. P., and D. B. Wilson. Optimizing cellulase mixtures for maximum rate and extent of hydrolysis. Final report. Office of Scientific and Technical Information (OSTI), March 1997. http://dx.doi.org/10.2172/468540.

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