Journal articles: 'Cellobiohydrolase I'

1

Wood, T. M., and S. I. McCrae. "The cellulase of Penicillium pinophilum. Synergism between enzyme components in solubilizing cellulose with special reference to the involvement of two immunologically distinct cellobiohydrolases." Biochemical Journal 234, no. 1 (February 15, 1986): 93–99. http://dx.doi.org/10.1042/bj2340093.

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Two immunologically unrelated cellobiohydrolases (I and II), isolated from the extracellular cellulase system elaborated by the fungus Penicillum pinophilum, acted in synergism to solubilize the microcrystalline cellulose Avicel; the ratio of the two enzymes for maximum rate of attack was approx. 1:1. A hypothesis to explain the phenomenon of synergism between two endwise-acting cellobiohydrolases is presented. It is suggested that the cellobiohydrolases may be two stereospecific enzymes concerned with the hydrolysis of the two different configurations of non-reducing end groups that would exist in cellulose. Only one type of cellobiohydrolase has been isolated so far from the cellulases of the fungi Fusarium solani and Trichoderma koningii. Only cellobiohydrolase II of P. pinophilum acted synergistically with the cellobiohydrolase of the fungi T. koningii or F. solani to solubilize Avicel. Cellobiohydrolase II showed no capacity for co-operating with the endo-1,4-beta-glucanase of T. koningii or F. solani to solubilize crystalline cellulose, but cellobiohydrolase I did. These results are discussed in the context of the hypothesis presented.

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DAVIES, Gideon J., A. Marek BRZOZOWSKI, Miroslawa DAUTER, Annabelle VARROT, and Martin SCHÜLEIN. "Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 Å resolution." Biochemical Journal 348, no. 1 (May 9, 2000): 201–7. http://dx.doi.org/10.1042/bj3480201.

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Cellulases are traditionally classified as either endoglucanases or cellobiohydrolases on the basis of their respective catalytic activities on crystalline cellulose, which is generally hydrolysed more efficiently only by the cellobiohydrolases. On the basis of the Trichoderma reesei cellobiohydrolase II structure, it was proposed that the active-site tunnel of cellobiohydrolases permitted the processive hydrolysis of cellulose, whereas the corresponding endoglucanases would display open active-site clefts [Rouvinen, Bergfors, Teeri, Knowles and Jones (1990) Science 249, 380-386]. Glycoside hydrolase family 6 contains both cellobiohydrolases and endoglucanases. The structure of the catalytic core of the family 6 endoglucanase Cel6B from Humicola insolens has been solved by molecular replacement with the known T. reesei cellobiohydrolase II as the search model. Strangely, at the sequence level, this enzyme exhibits the highest sequence similarity to family 6 cellobiohydrolases and displays just one of the loop deletions traditionally associated with endoglucanases in this family. However, this enzyme shows no activity on crystalline substrates but a high activity on soluble substrates, which is typical of an endoglucanase. The three-dimensional structure reveals that the deletion of just a single loop of the active site, coupled with the resultant conformational change in a second ‘cellobiohydrolase-specific’ loop, peels open the active-site tunnel to reveal a substrate-binding groove.

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Shen, H., N. R. Gilkes, D. G. Kilburn, R. C. Miller, and R. A. J. Warren. "Cellobiohydrolase B, a second exo-cellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi." Biochemical Journal 311, no. 1 (October 1, 1995): 67–74. http://dx.doi.org/10.1042/bj3110067.

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The gene cbhB from the cellulolytic bacterium Cellulomonas fimi encodes a polypeptide of 1090 amino acids. Cellobiohydrolase B (CbhB) is 1037 amino acids long, with a calculated molecular mass of 109765 Da. The enzyme comprises five domains: an N-terminal catalytic domain of 643 amino acids, three fibronectin type III repeats of 97 amino acids each, and a C-terminal cellulose-binding domain of 104 amino acids. The catalytic domain belongs to family 48 of glycosyl hydrolases. CbhB has a very low activity on CM-cellulose. Viscometric analysis of CM-cellulose hydrolysis indicates that the enzyme is an exoglucanase. Cellobiose is the major product of hydrolysis of cellulose. In common with two other exoglycanases from C. fimi, CbhB has low but detectable endoglucanase activity. CbhB is the second exo-cellobiohydrolase found in C. fimi. Therefore, the cellulase system of C. fimi resembles those of fungi in comprising multiple endoglucanases and cellobiohydrolases.

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Watson, Brian J., Haitao Zhang, Atkinson G. Longmire, Young Hwan Moon, and Steven W. Hutcheson. "Processive Endoglucanases Mediate Degradation of Cellulose by Saccharophagus degradans." Journal of Bacteriology 191, no. 18 (July 17, 2009): 5697–705. http://dx.doi.org/10.1128/jb.00481-09.

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ABSTRACT Bacteria and fungi are thought to degrade cellulose through the activity of either a complexed or a noncomplexed cellulolytic system composed of endoglucanases and cellobiohydrolases. The marine bacterium Saccharophagus degradans 2-40 produces a multicomponent cellulolytic system that is unusual in its abundance of GH5-containing endoglucanases. Secreted enzymes of this bacterium release high levels of cellobiose from cellulosic materials. Through cloning and purification, the predicted biochemical activities of the one annotated cellobiohydrolase Cel6A and the GH5-containing endoglucanases were evaluated. Cel6A was shown to be a classic endoglucanase, but Cel5H showed significantly higher activity on several types of cellulose, was the highest expressed, and processively released cellobiose from cellulosic substrates. Cel5G, Cel5H, and Cel5J were found to be members of a separate phylogenetic clade and were all shown to be processive. The processive endoglucanases are functionally equivalent to the endoglucanases and cellobiohydrolases required for other cellulolytic systems, thus providing a cellobiohydrolase-independent mechanism for this bacterium to convert cellulose to glucose.

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Nakamura, Akihiko, Daiki Ishiwata, Akasit Visootsat, Taku Uchiyama, Kenji Mizutani, Satoshi Kaneko, Takeshi Murata, Kiyohiko Igarashi, and Ryota Iino. "Domain architecture divergence leads to functional divergence in binding and catalytic domains of bacterial and fungal cellobiohydrolases." Journal of Biological Chemistry 295, no. 43 (August 18, 2020): 14606–17. http://dx.doi.org/10.1074/jbc.ra120.014792.

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Cellobiohydrolases directly convert crystalline cellulose into cellobiose and are of biotechnological interest to achieve efficient biomass utilization. As a result, much research in the field has focused on identifying cellobiohydrolases that are very fast. Cellobiohydrolase A from the bacterium Cellulomonas fimi (CfCel6B) and cellobiohydrolase II from the fungus Trichoderma reesei (TrCel6A) have similar catalytic domains (CDs) and show similar hydrolytic activity. However, TrCel6A and CfCel6B have different cellulose-binding domains (CBDs) and linkers: TrCel6A has a glycosylated peptide linker, whereas CfCel6B's linker consists of three fibronectin type 3 domains. We previously found that TrCel6A's linker plays an important role in increasing the binding rate constant to crystalline cellulose. However, it was not clear whether CfCel6B's linker has similar function. Here we analyze kinetic parameters of CfCel6B using single-molecule fluorescence imaging to compare CfCel6B and TrCel6A. We find that CBD is important for initial binding of CfCel6B, but the contribution of the linker to the binding rate constant or to the dissociation rate constant is minor. The crystal structure of the CfCel6B CD showed longer loops at the entrance and exit of the substrate-binding tunnel compared with TrCel6A CD, which results in higher processivity. Furthermore, CfCel6B CD showed not only fast surface diffusion but also slow processive movement, which is not observed in TrCel6A CD. Combined with the results of a phylogenetic tree analysis, we propose that bacterial cellobiohydrolases are designed to degrade crystalline cellulose using high-affinity CBD and high-processivity CD.

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Suzuki, Hitoshi, Kiyohiko Igarashi, and Masahiro Samejima. "Cellotriose and Cellotetraose as Inducers of the Genes Encoding Cellobiohydrolases in the Basidiomycete Phanerochaete chrysosporium." Applied and Environmental Microbiology 76, no. 18 (July 23, 2010): 6164–70. http://dx.doi.org/10.1128/aem.00724-10.

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ABSTRACT The wood decay basidiomycete Phanerochaete chrysosporium produces a variety of cellobiohydrolases belonging to glycoside hydrolase (GH) families 6 and 7 in the presence of cellulose. However, no inducer of the production of these enzymes has yet been identified. Here, we quantitatively compared the transcript levels of the genes encoding GH family 6 cellobiohydrolase (cel6A) and GH family 7 cellobiohydrolase isozymes (cel7A to cel7F/G) in cultures containing glucose, cellulose, and cellooligosaccharides by real-time quantitative PCR, in order to evaluate the transcription-inducing effect of soluble sugars. Upregulation of transcript levels in the presence of cellulose compared to glucose was observed for cel7B, cel7C, cel7D, cel7F/G, and cel6A at all time points during cultivation. In particular, the transcription of cel7C and cel7D was strongly induced by cellotriose or cellotetraose. The highest level of cel7C transcripts was observed in the presence of cellotetraose, whereas the highest level of cel7D transcripts was found in the presence of cellotriose, amounting to 2.7 × 106 and 1.7 × 106 copies per 105 actin gene transcripts, respectively. These numbers of cel7C and cel7D transcripts were higher than those in the presence of cellulose. In contrast, cellobiose had a weaker transcription-inducing effect than either cellotriose or cellotetraose for cel7C and had little effect in the case of cel7D. These results indicate that cellotriose and cellotetraose, but not cellobiose, are possible natural cellobiohydrolase gene transcription inducers derived from cellulose.

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Takahashi, Machiko, Hideyuki Takahashi, Yuki Nakano, Teruko Konishi, Ryohei Terauchi, and Takumi Takeda. "Characterization of a Cellobiohydrolase (MoCel6A) Produced by Magnaporthe oryzae." Applied and Environmental Microbiology 76, no. 19 (August 13, 2010): 6583–90. http://dx.doi.org/10.1128/aem.00618-10.

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ABSTRACT Three GH-6 family cellobiohydrolases are expected in the genome of Magnaporthe grisea based on the complete genome sequence. Here, we demonstrate the properties, kinetics, and substrate specificities of a Magnaporthe oryzae GH-6 family cellobiohydrolase (MoCel6A). In addition, the effect of cellobiose on MoCel6A activity was also investigated. MoCel6A contiguously fused to a histidine tag was overexpressed in M. oryzae and purified by affinity chromatography. MoCel6A showed higher hydrolytic activities on phosphoric acid-swollen cellulose (PSC), β-glucan, and cellooligosaccharide derivatives than on cellulose, of which the best substrates were cellooligosaccharides. A tandemly aligned cellulose binding domain (CBD) at the N terminus caused increased activity on cellulose and PSC, whereas deletion of the CBD (catalytic domain only) showed decreased activity on cellulose. MoCel6A hydrolysis of cellooligosaccharides and sulforhodamine-conjugated cellooligosaccharides was not inhibited by exogenously adding cellobiose up to 438 mM, which, rather, enhanced activity, whereas a GH-7 family cellobiohydrolase from M. oryzae (MoCel7A) was severely inhibited by more than 29 mM cellobiose. Furthermore, we assessed the effects of cellobiose on hydrolytic activities using MoCel6A and Trichoderma reesei cellobiohydrolase (TrCel6A), which were prepared in Aspergillus oryzae. MoCel6A showed increased hydrolysis of cellopentaose used as a substrate in the presence of 292 mM cellobiose at pH 4.5 and pH 6.0, and enhanced activity disappeared at pH 9.0. In contrast, TrCel6A exhibited slightly increased hydrolysis at pH 4.5, and hydrolysis was severely inhibited at pH 9.0. These results suggest that enhancement or inhibition of hydrolytic activities by cellobiose is dependent on the reaction mixture pH.

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Wood, T. M., S. I. McCrae, and K. M. Bhat. "The mechanism of fungal cellulase action. Synergism between enzyme components of Penicillium pinophilum cellulase in solubilizing hydrogen bond-ordered cellulose." Biochemical Journal 260, no. 1 (May 15, 1989): 37–43. http://dx.doi.org/10.1042/bj2600037.

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Studies on reconstituted mixtures of extensively purified cellobiohydrolases I and II and the five major endoglucanases of the fungus Penicillium pinophilum have provided some new information on the mechanism by which crystalline cellulose in the form of the cotton fibre is rendered soluble. It was observed that there was little or no synergistic activity either between purified cellobiohydrolases I and II, or, contrary to previous findings, between the individual cellobiohydrolases and the endoglucanases. Cotton fibre was degraded to a significant degree only when three enzymes were present in the reconstituted enzyme mixture: these were cellobiohydrolases I and II and some specific endoglucanases. The optimum ratio of the cellobiohydrolases was 1:1. Only a trace of endoglucanase activity was required to make the mixture of cellobiohydrolases I and II effective. The addition of cellobiohydrolases I and II individually to endoglucanases from other cellulolytic fungi resulted in little synergistic activity; however, a mixture of endoglucanases and both cellobiohydrolases was effective. It is suggested that current concepts of the mechanism of cellulase action may be the result of incompletely resolved complexes between cellobiohydrolase and endoglucanase activities. It was found that such complexes in filtrates of P. pinophilium or Trichoderma reesei were easily resolved using affinity chromatography on a column of p-aminobenzyl-1-thio-beta-D-cellobioside.

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Murashima, Koichiro, Akihiko Kosugi, and Roy H. Doi. "Determination of Subunit Composition of Clostridium cellulovorans Cellulosomes That Degrade Plant Cell Walls." Applied and Environmental Microbiology 68, no. 4 (April 2002): 1610–15. http://dx.doi.org/10.1128/aem.68.4.1610-1615.2002.

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ABSTRACT Clostridium cellulovorans produces a cellulase enzyme complex (cellulosome). In this study, we isolated two plant cell wall-degrading cellulosomal fractions from culture supernatant of C. cellulovorans and determined their subunit compositions and enzymatic activities. One of the cellulosomal fractions showed fourfold-higher plant cell wall-degrading activity than the other. Both cellulosomal fractions contained the same nine subunits (the scaffolding protein CbpA, endoglucanases EngE and EngK, cellobiohydrolase ExgS, xylanase XynA, mannanase ManA, and three unknown proteins), although the relative amounts of the subunits differed. Since only cellobiose was released from plant cell walls by the cellulosomal fractions, cellobiohydrolases were considered to be key enzymes for plant cell wall degradation.

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Gielkens, Marco M. C., Ester Dekkers, Jaap Visser, and Leo H. de Graaff. "Two Cellobiohydrolase-Encoding Genes from Aspergillus niger Require d-Xylose and the Xylanolytic Transcriptional Activator XlnR for Their Expression." Applied and Environmental Microbiology 65, no. 10 (October 1, 1999): 4340–45. http://dx.doi.org/10.1128/aem.65.10.4340-4345.1999.

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ABSTRACT Two cellobiohydrolase-encoding genes, cbhA andcbhB, have been isolated from the filamentous fungusAspergillus niger. The deduced amino acid sequence shows that CbhB has a modular structure consisting of a fungus-type cellulose-binding domain (CBD) and a catalytic domain separated by a Pro/Ser/Thr-rich linker peptide. CbhA consists only of a catalytic domain and lacks a CBD and linker peptide. Both proteins are homologous to fungal cellobiohydrolases in family 7 of the glycosyl hydrolases. Northern blot analysis showed that the transcription of thecbhA and cbhB genes is induced byd-xylose but not by sophorose and, in addition, requires the xylanolytic transcriptional activator XlnR.

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11

Wang, Yi Duo, Cong Fa Li, and Si Xin Liu. "Fermentation Condition of Penicillium purpurogenum HBZ003 from Mangrove for 1,4-β-D-cellobiohydrolase Activity." Advanced Materials Research 781-784 (September 2013): 1284–88. http://dx.doi.org/10.4028/www.scientific.net/amr.781-784.1284.

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The cellulolytic enzymes from Penicillium genus showed well-balanced amounts of cellobiohydrolase, endo-cellulase and β-glycosidase. The Fermentation condition of Penicillium purpurogenum HBZ003 from Mangrove for 1,4-β-D-cellobiohydrolase activity was investigated. The optimum fermentation condition of Penicillium purpurogenum HBZ003 was as follows. The medium was composed of 1.6% bran, 0.4% CMC, 0.5% (NH4)2SO4, 0.4% KNO3, 0.6%NaCl, 0.03% CaCl2 and 0.05% Tween 60, and adjusted to initial pH 4.0, and inoculated with 10% seed and cultivated at 160 r/min and 30 °C for 5d. The 1,4-β-D-cellobiohydrolase activity reached 5.54 U with the ratio of 1,4-β-D-cellobiohydrolase, endo-cellulase and β-glycosidase activity being 1:3.26:5.09.

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BHIKHABHAI, RAMAGAURI, GUNNAR JOHANSSON, and GÖRAN PETTERSSON. "Cellobiohydrolase from Trichoderma reesei." International Journal of Peptide and Protein Research 25, no. 4 (January 12, 2009): 368–74. http://dx.doi.org/10.1111/j.1399-3011.1985.tb02187.x.

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Westh, Peter, Kim Borch, Trine Sørensen, Radina Tokin, Jeppe Kari, Silke Badino, Mafalda A. Cavaleiro, et al. "Thermoactivation of a cellobiohydrolase." Biotechnology and Bioengineering 115, no. 4 (January 16, 2018): 831–38. http://dx.doi.org/10.1002/bit.26513.

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Huang, Hsiao-Chuan, Liu-Hong Qi, Yo-Chia Chen, and Li-Chu Tsai. "Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose." Acta Crystallographica Section D Structural Biology 75, no. 12 (November 29, 2019): 1138–47. http://dx.doi.org/10.1107/s2059798319013597.

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The catalytic domain (residues 128–449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 Å, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.

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VARROT, Annabelle, Sven HASTRUP, Martin SCHÜLEIN, and Gideon J. DAVIES. "Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 Å resolution." Biochemical Journal 337, no. 2 (January 8, 1999): 297–304. http://dx.doi.org/10.1042/bj3370297.

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The three-dimensional structure of the catalytic core of the family 6 cellobiohydrolase II, Cel6A (CBH II), from Humicola insolens has been determined by X-ray crystallography at a resolution of 1.92 Å. The structure was solved by molecular replacement using the homologous Trichoderma reesei CBH II as a search model. The H. insolens enzyme displays a high degree of structural similarity with its T. reeseiequivalent. The structure features both O- (α-linked mannose) and N-linked glycosylation and a hexa-co-ordinate Mg2+ ion. The active-site residues are located within the enclosed tunnel that is typical for cellobiohydrolase enzymes and which may permit a processive hydrolysis of the cellulose substrate. The close structural similarity between the two enzymes implies that kinetics and chain-end specificity experiments performed on the H. insolens enzyme are likely to be applicable to the homologous T. reesei enzyme. These cast doubt on the description of cellobiohydrolases as exo-enzymes since they demonstrated that Cel6A (CBH II) shows no requirement for non-reducing chain-ends, as had been presumed. There is no crystallographic evidence in the present structure to support a mechanism involving loop opening, yet preliminary modelling experiments suggest that the active-site tunnel of Cel6A (CBH II) is too narrow to permit entry of a fluorescenyl-derivatized substrate, known to be a viable substrate for this enzyme. Co-ordinates for the structure described in this paper have been deposited with the Brookhaven Protein Data Bank with accession code 1BVW.PDB.

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de Menezes, Alexandre B., Miranda T. Prendergast-Miller, Pabhon Poonpatana, Mark Farrell, Andrew Bissett, Lynne M. Macdonald, Peter Toscas, Alan E. Richardson, and Peter H. Thrall. "C/N Ratio Drives Soil Actinobacterial Cellobiohydrolase Gene Diversity." Applied and Environmental Microbiology 81, no. 9 (February 20, 2015): 3016–28. http://dx.doi.org/10.1128/aem.00067-15.

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ABSTRACTCellulose accounts for approximately half of photosynthesis-fixed carbon; however, the ecology of its degradation in soil is still relatively poorly understood. The role of actinobacteria in cellulose degradation has not been extensively investigated despite their abundance in soil and known cellulose degradation capability. Here, the diversity and abundance of the actinobacterial glycoside hydrolase family 48 (cellobiohydrolase) gene in soils from three paired pasture-woodland sites were determined by using terminal restriction fragment length polymorphism (T-RFLP) analysis and clone libraries with gene-specific primers. For comparison, the diversity and abundance of general bacteria and fungi were also assessed. Phylogenetic analysis of the nucleotide sequences of 80 clones revealed significant new diversity of actinobacterial GH48 genes, and analysis of translated protein sequences showed that these enzymes are likely to represent functional cellobiohydrolases. The soil C/N ratio was the primary environmental driver of GH48 community compositions across sites and land uses, demonstrating the importance of substrate quality in their ecology. Furthermore, mid-infrared (MIR) spectrometry-predicted humic organic carbon was distinctly more important to GH48 diversity than to total bacterial and fungal diversity. This suggests a link between the actinobacterial GH48 community and soil organic carbon dynamics and highlights the potential importance of actinobacteria in the terrestrial carbon cycle.

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KIPPER, Kalle, Priit VÄLJAMÄE, and Gunnar JOHANSSON. "Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as ‘burst’ kinetics on fluorescent polymeric model substrates." Biochemical Journal 385, no. 2 (January 7, 2005): 527–35. http://dx.doi.org/10.1042/bj20041144.

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Reaction conditions for the reducing-end-specific derivatization of cellulose substrates with the fluorogenic compound, anthranilic acid, have been established. Hydrolysis of fluorescence-labelled celluloses by cellobiohydrolase Cel7A from Trichoderma reesei was consistent with the active-site titration kinetics (burst kinetics), which allowed the quantification of the processivity of the enzyme. The processivity values of 88±10, 42±10 and 34±2.0 cellobiose units were found for Cel7A acting on labelled bacterial cellulose, bacterial microcrystalline cellulose and endoglucanase-pretreated bacterial cellulose respectively. The anthranilic acid derivatization also provides an alternative means for estimating the average degree of polymerization of cellulose and, furthermore, allows the quantitative monitoring of the production of reducing end groups on solid cellulose on hydrolysis by cellulases. Hydrolysis of bacterial cellulose by cellulases from T. reesei revealed that, by contrast with endoglucanase Cel5A, neither cellobiohydrolases Cel7A nor Cel6A produced detectable amounts of new reducing end groups on residual cellulose.

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Wang, Tian-Hong, Ti Liu, Zhi-Hong Wu, Shi-Li Liu, Yi Lu, and Yin-Bo Qu. "Novel Cellulase Profile of Trichoderma reesei Strains Constructed by cbh1 Gene Replacement with eg3 Gene Expression Cassette." Acta Biochimica et Biophysica Sinica 36, no. 10 (October 1, 2004): 667–72. http://dx.doi.org/10.1093/abbs/36.10.667.

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Abstract To construct strains of the filamentous fungus Trichoderma reesei with low cellobiohydrolases while high endoglucanase activity, the Pcbh1-eg3-Tcbh1 cassette was constructed and the coding sequence of the cellobiohydrolase I (CBHI) gene was replaced with the coding sequence of the eg3 gene by homologous recombination. Disruption of the cbh1 gene was confirmed by PCR, Southern dot blot and Western hybridization analysis in two transformants denoted as L13 and L29. The filter paper-hydrolyzing activity of strain L29 was 60% of the parent strain Rut C30, and the CMCase activity was increased by 33%. This relatively modest increase suggested that the eg3 cDNA under the control of the cbh1 promoter was not efficiently transcribed as the wild type cbhl gene. However our results confirmed that homologous recombination could be used to construct strains of the filamentous fungus Trichoderma reesei with novel cellulase profile. Such strains are of interest from the basic science perspective and also have potential industrial applications.

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Zafar, Asma, Muhammad Nauman Aftab, Anam Asif, Ahmet Karadag, Liangcai Peng, Hassan Ufak Celebioglu, Muhammad Sohail Afzal, Attia Hamid, and Irfana Iqbal. "Efficient biomass saccharification using a novel cellobiohydrolase from Clostridium clariflavum for utilization in biofuel industry." RSC Advances 11, no. 16 (2021): 9246–61. http://dx.doi.org/10.1039/d1ra00545f.

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Yan, Meng Jiao, Song Wei, Ya Li Dai, and Lin Yuan. "Cloning and Expression of Exo-β-1,4-Cellobiohydrolase Gene from Bacillus pumilus." Advanced Materials Research 647 (January 2013): 150–54. http://dx.doi.org/10.4028/www.scientific.net/amr.647.150.

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The exo-β-1,4-cellobiohydrolase gene(cex) of Bacillus pumilus AC-6 was cloned. The cex gene from AC-6 is 2100bp, and encodes 700 amino acids. The cex gene has 94% similarities to the exo-β-1,4-cellobiohydrolase gene sequence from other Bacillus strains. The cex gene was linked with the vector pGEX-4T-1, and transferred into the competent E. coli BL21 for expression. The result of protein electrophoresis showed that the protein has expressed, whose molecular weight was about 104kDa. Measured the enzyme activity of the expression protein of the recombinant strains was 5.40U/mL, which is 1.20 times as the original strains.

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Sandgren, Mats, Miao Wu, Saeid Karkehabadi, Colin Mitchinson, Bradley R. Kelemen, Edmundo A. Larenas, Jerry Ståhlberg, and Henrik Hansson. "The Structure of a Bacterial Cellobiohydrolase: The Catalytic Core of the Thermobifida fusca Family GH6 Cellobiohydrolase Cel6B." Journal of Molecular Biology 425, no. 3 (February 2013): 622–35. http://dx.doi.org/10.1016/j.jmb.2012.11.039.

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Miettinen-Oinonen, Arja, and Pirkko Suominen. "Enhanced Production of Trichoderma reesei Endoglucanases and Use of the New Cellulase Preparations in Producing the Stonewashed Effect on Denim Fabric." Applied and Environmental Microbiology 68, no. 8 (August 2002): 3956–64. http://dx.doi.org/10.1128/aem.68.8.3956-3964.2002.

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ABSTRACT Trichoderma reesei strains were constructed for production of elevated amounts of endoglucanase II (EGII) with or without cellobiohydrolase I (CBHI). The endoglucanase activity produced by the EGII transformants correlated with the copy number of the egl2 expression cassette. One copy of the egl2 expression cassette in which the egl2 was under the cbh1 promoter increased production of endoglucanase activity 2.3-fold, and two copies increased production about 3-fold above that of the parent strain. When the enzyme with elevated EGII content was used, an improved stonewashing effect on denim fabric was achieved. A T. reesei strain producing high amounts of EGI and -II activities without CBHI and -II was constructed by replacing the cbh2 locus with the coding region of the egl2 gene in the EGI-overproducing CBHI-negative strain. Production of endoglucanase activity by the EG-transformant strain was increased fourfold above that of the host strain. The filter paper-degrading activity of the endoglucanase-overproducing strain was lowered to below detection, presumably because of the lack of cellobiohydrolases.

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Poças-Fonseca, Marcio J., Ildinete Silva-Pereira, Bruno B. Rocha, and Maristella de O. Azevedo. "Substrate-dependent differential expression ofHumicola griseavar.thermoideacellobiohydrolase genes." Canadian Journal of Microbiology 46, no. 8 (August 1, 2000): 749–52. http://dx.doi.org/10.1139/w00-051.

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Transcription of fungal cellulase genes may be affected by substrate induction. We studied the expression of Humicola grisea var. thermoidea cellobiohydrolase genes (cbh1.1 and cbh1.2) under induction by several soluble and insoluble carbon sources. Using the RT-PCR technique, the cbh1.2 transcript was detected in all the conditions assayed along the growth curve. Catabolite repression, which frequently occurs in other fungal cellulolytic systems, was not observed. On the other hand, cbh1.1 transcription was shown to be driven by insoluble and complex lignocellulosic substrates. In summary, the cbh1.2 gene product is constitutively produced, while cbh1.1 seems to respond to a distinct regulatory mechanism.Key words: Humicola, cellobiohydrolase genes, gene expression, carbon sources, lignocellulosic substrates.

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Igarashi, Kiyohiko, Masahisa Wada, Ritsuko Hori, and Masahiro Samejima. "Surface density of cellobiohydrolase on crystalline celluloses." FEBS Journal 273, no. 13 (July 2006): 2869–78. http://dx.doi.org/10.1111/j.1742-4658.2006.05299.x.

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Liu, Yu-San, John O. Baker, Yining Zeng, Michael E. Himmel, Thomas Haas, and Shi-You Ding. "Cellobiohydrolase Hydrolyzes Crystalline Cellulose on Hydrophobic Faces." Journal of Biological Chemistry 286, no. 13 (January 31, 2011): 11195–201. http://dx.doi.org/10.1074/jbc.m110.216556.

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Abuja, Peter M., Ingrid Pilz, Marc Claeyssens, and Peter Tomme. "Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: Close resemblance to cellobiohydrolase I." Biochemical and Biophysical Research Communications 156, no. 1 (October 1988): 180–85. http://dx.doi.org/10.1016/s0006-291x(88)80821-0.

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Zafar, Asma, Muhammad Nauman Aftab, Anam Asif, Ahmet Karadag, Liangcai Peng, Hasan Ufak Celebioglu, Muhammad Sohail Afzal, Attia Hamid, and Irfana Iqbal. "Correction: Efficient biomass saccharification using a novel cellobiohydrolase from Clostridium clariflavum for utilization in biofuel industry." RSC Advances 11, no. 19 (2021): 11387. http://dx.doi.org/10.1039/d1ra90090k.

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Correction for ‘Efficient biomass saccharification using a novel cellobiohydrolase from Clostridium clariflavum for utilization in biofuel industry’ by Asma Zafar et al., RSC Adv., 2021, 11, 9246–9261, DOI: 10.1039/D1RA00545F.

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Tsai, Li-Chu, Imamaddin Amiraslanov, Hung-Ren Chen, Yun-Wen Chen, Hsiao-Lin Lee, Po-Huang Liang, and Yen-Chywan Liaw. "Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage." Acta Crystallographica Section F Structural Biology Communications 71, no. 10 (September 23, 2015): 1264–72. http://dx.doi.org/10.1107/s2053230x15015915.

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Exoglucanase/cellobiohydrolase (EC 3.2.1.176) hydrolyzes a β-1,4-glycosidic bond from the reducing end of cellulose and releases cellobiose as the major product. Three complex crystal structures of the glycosyl hydrolase 48 (GH48) cellobiohydrolase S (ExgS) from Clostridium cellulovorans with cellobiose, cellotetraose and triethylene glycol molecules were solved. The product cellobiose occupies subsites +1 and +2 in the open active-site cleft of the enzyme–cellotetraose complex structure, indicating an enzymatic hydrolysis function. Moreover, three triethylene glycol molecules and one pentaethylene glycol molecule are located at active-site subsites −2 to −6 in the structure of the ExgS–triethylene glycol complex shown here. Modelling of glucose into subsite −1 in the active site of the ExgS–cellobiose structure revealed that Glu50 acts as a proton donor and Asp222 plays a nucleophilic role.

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Henriksson, Hongbin, Stefan Jönsson, Roland Isaksson, and Göran Pettersson. "Chiral separation based on immobilized intact and fragmented cellobiohydrolase II (CBH II): A comparison with cellobiohydrolase I (CBH I)." Chirality 7, no. 6 (1995): 415–24. http://dx.doi.org/10.1002/chir.530070606.

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Edwards, Ivan P., Rima A. Upchurch, and Donald R. Zak. "Isolation of Fungal Cellobiohydrolase I Genes from Sporocarps and Forest Soils by PCR." Applied and Environmental Microbiology 74, no. 11 (April 11, 2008): 3481–89. http://dx.doi.org/10.1128/aem.02893-07.

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ABSTRACT Cellulose is the major component of plant biomass, and microbial cellulose utilization is a key step in the decomposition of plant detritus. Despite this, little is known about the diversity of cellulolytic microbial communities in soil. Fungi are well known for their cellulolytic activity and mediate key functions during the decomposition of plant detritus in terrestrial ecosystems. We developed new oligonucleotide primers for fungal exocellulase genes (cellobiohydrolase, cbhI) and used these to isolate distinct cbhI homologues from four species of litter-decomposing basidiomycete fungi (Clitocybe nuda, Clitocybe gibba, Clitopilus prunulus, and Chlorophyllum molybdites) and two species of ascomycete fungi (Xylaria polymorpha and Sarcoscypha occidentalis). Evidence for cbhI gene families was found in three of the four basidiomycete species. Additionally, we isolated and cloned cbhI genes from the forest floor and mineral soil of two upland forests in northern lower Michigan, one dominated by oak (Quercus velutina, Q. alba) and the other dominated by sugar maple (Acer saccharum) and American basswood (Tilia americana). Phylogenetic analysis demonstrated that cellobiohydrolase genes recovered from the floor of both forests tended to cluster with Xylaria or in one of two unidentified groups, whereas cellobiohydrolase genes recovered from soil tended to cluster with Trichoderma, Alternaria, Eurotiales, and basidiomycete sequences. The ability to amplify a key fungal gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ.

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Fujita, Yasuya, Junji Ito, Mitsuyoshi Ueda, Hideki Fukuda, and Akihiko Kondo. "Synergistic Saccharification, and Direct Fermentation to Ethanol, of Amorphous Cellulose by Use of an Engineered Yeast Strain Codisplaying Three Types of Cellulolytic Enzyme." Applied and Environmental Microbiology 70, no. 2 (February 2004): 1207–12. http://dx.doi.org/10.1128/aem.70.2.1207-1212.2004.

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ABSTRACT A whole-cell biocatalyst with the ability to induce synergistic and sequential cellulose-degradation reaction was constructed through codisplay of three types of cellulolytic enzyme on the cell surface of the yeast Saccharomyces cerevisiae. When a cell surface display system based on α-agglutinin was used, Trichoderma reesei endoglucanase II and cellobiohydrolase II and Aspergillus aculeatus β-glucosidase 1 were simultaneously codisplayed as individual fusion proteins with the C-terminal-half region of α-agglutinin. Codisplay of the three enzymes on the cell surface was confirmed by observation of immunofluorescence-labeled cells with a fluorescence microscope. A yeast strain codisplaying endoglucanase II and cellobiohydrolase II showed significantly higher hydrolytic activity with amorphous cellulose (phosphoric acid-swollen cellulose) than one displaying only endoglucanase II, and its main product was cellobiose; codisplay of β-glucosidase 1, endoglucanase II, and cellobiohydrolase II enabled the yeast strain to directly produce ethanol from the amorphous cellulose (which a yeast strain codisplaying β-glucosidase 1 and endoglucanase II could not), with a yield of approximately 3 g per liter from 10 g per liter within 40 h. The yield (in grams of ethanol produced per gram of carbohydrate consumed) was 0.45 g/g, which corresponds to 88.5% of the theoretical yield. This indicates that simultaneous and synergistic saccharification and fermentation of amorphous cellulose to ethanol can be efficiently accomplished using a yeast strain codisplaying the three cellulolytic enzymes.

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Woon, James Sy-Keen, Mukram M. Mackeen, Rosli M. Illias, Nor M. Mahadi, William J. Broughton, Abdul Munir Abdul Murad, and Farah Diba Abu Bakar. "Cellobiohydrolase B ofAspergillus nigerover-expressed inPichia pastorisstimulates hydrolysis of oil palm empty fruit bunches." PeerJ 5 (October 12, 2017): e3909. http://dx.doi.org/10.7717/peerj.3909.

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BackgroundAspergillus niger, along with many other lignocellulolytic fungi, has been widely used as a commercial workhorse for cellulase production. A fungal cellulase system generally includes three major classes of enzymes i.e., β-glucosidases, endoglucanases and cellobiohydrolases. Cellobiohydrolases (CBH) are vital to the degradation of crystalline cellulose present in lignocellulosic biomass. However,A. nigernaturally secretes low levels of CBH. Hence, recombinant production ofA. nigerCBH is desirable to increase CBH production yield and also to allow biochemical characterisation of the recombinant CBH fromA. niger.MethodsIn this study, the gene encoding a cellobiohydrolase B (cbhB) fromA. nigerATCC 10574 was cloned and expressed in the methylotrophic yeastPichia pastorisX-33. The recombinant CBHB was purified and characterised to study its biochemical and kinetic characteristics. To evaluate the potential of CBHB in assisting biomass conversion, CBHB was supplemented into a commercial cellulase preparation (Cellic®CTec2) and was used to hydrolyse oil palm empty fruit bunch (OPEFB), one of the most abundant lignocellulosic waste from the palm oil industry. To attain maximum saccharification, enzyme loadings were optimised by response surface methodology and the optimum point was validated experimentally. Hydrolysed OPEFB samples were analysed using attenuated total reflectance FTIR spectroscopy (ATR-FTIR) to screen for any compositional changes upon enzymatic treatment.ResultsRecombinant CBHB was over-expressed as a hyperglycosylated protein attached toN-glycans. CBHB was enzymatically active towards soluble substrates such as 4-methylumbelliferyl-β-D-cellobioside (MUC),p-nitrophenyl-cellobioside (pNPC) andp-nitrophenyl-cellobiotrioside (pNPG3) but was not active towards crystalline substrates like Avicel®and Sigmacell cellulose. Characterisation of purified CBHB using MUC as the model substrate revealed that optimum catalysis occurred at 50 °C and pH 4 but the enzyme was stable between pH 3 to 10 and 30 to 80 °C. Although CBHB on its own was unable to digest crystalline substrates, supplementation of CBHB (0.37%) with Cellic®CTec2 (30%) increased saccharification of OPEFB by 27%. Compositional analyses of the treated OPEFB samples revealed that CBHB supplementation reduced peak intensities of both crystalline cellulose Iαand Iβ in the treated OPEFB samples.DiscussionSince CBHB alone was inactive against crystalline cellulose, these data suggested that it might work synergistically with other components of Cellic®CTec2. CBHB supplements were desirable as they further increased hydrolysis of OPEFB when the performance of Cellic®CTec2 was theoretically capped at an enzyme loading of 34% in this study. Hence,A. nigerCBHB was identified as a potential supplementary enzyme for the enzymatic hydrolysis of OPEFB.

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33

Ruttersmith, L. D., and R. M. Daniel. "Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp. strain FjSS3-B.1. Purification and properties." Biochemical Journal 277, no. 3 (August 1, 1991): 887–90. http://dx.doi.org/10.1042/bj2770887.

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Exo-1,4-beta-cellobiohydrolase (EC 3.2.1.91) was isolated from the culture supernatant of Thermotoga sp. strain FjSS3-B.1, an extremely thermophilic eubacterium that grows optimally at 80 degrees C. The enzyme was purified to homogeneity as determined by SDS/PAGE and has an Mr of 36,000. The enzyme is the most thermostable cellulase reported to date, with a half-life at 108 degrees C of 70 min in buffer. In a 40 min assay, maximal activity was recorded at 105 degrees C. Cellobiohydrolase from strain FjSS3-B.1 is active against amorphous cellulose and CM-cellulose but only effects limited hydrolysis of filter paper or Sigmacell 20. The only product identified by h.p.l.c. is the disaccharide cellobiose. The enzyme has a pH optimum around neutral and is stabilized by the presence of 0.8 M-NaCl.

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Tang, Shu-Lun, Patricia Bubner, Stefan Bauer, and Chris R. Somerville. "O-Glycan analysis of cellobiohydrolase I fromNeurospora crassa." Glycobiology 26, no. 6 (January 13, 2016): 670–77. http://dx.doi.org/10.1093/glycob/cww004.

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35

Cheng, Cheng, Norihiro Tsukagoshi, and Shigezo Udaka. "Nucleotide sequence of the cellobiohydrolase gene fromTrichoderma viride." Nucleic Acids Research 18, no. 18 (1990): 5559. http://dx.doi.org/10.1093/nar/18.18.5559.

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Ossowski, Ingemar von, Tuula Teeri, Nisse Kalkkinen, and Christian Oker-Blom. "Expression of a Fungal Cellobiohydrolase in Insect Cells." Biochemical and Biophysical Research Communications 233, no. 1 (April 1997): 25–29. http://dx.doi.org/10.1006/bbrc.1997.6391.

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Kunii, Mizuho, Mami Yasuno, Yuki Shindo, and Takefumi Kawata. "A Dictyostelium cellobiohydrolase orthologue that affects developmental timing." Development Genes and Evolution 224, no. 1 (November 16, 2013): 25–35. http://dx.doi.org/10.1007/s00427-013-0460-x.

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Uozumi, Nobuyuki, Akihiro Hayashi, Takaomi Ito, Arunwanich Patthra, Ichiro Yamashita, Shinji Iijima, and Takeshi Kobayashi. "Secretion of thermophilic bacterial cellobiohydrolase in Saccharomyces cerevisiae." Journal of Fermentation and Bioengineering 75, no. 6 (January 1993): 399–404. http://dx.doi.org/10.1016/0922-338x(93)90084-l.

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Xin, Donglin, Xiaoyan Ge, Zongping Sun, Liisa Viikari, and Junhua Zhang. "Competitive inhibition of cellobiohydrolase I by manno-oligosaccharides." Enzyme and Microbial Technology 68 (January 2015): 62–68. http://dx.doi.org/10.1016/j.enzmictec.2014.09.009.

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40

Hu, P., S. K. Kahrs, T. Chase, and D. E. Eveleigh. "Cloning of aMicrobispora bispora cellobiohydrolase gene inEscherichia coli." Journal of Industrial Microbiology 10, no. 2 (August 1992): 103–10. http://dx.doi.org/10.1007/bf01583842.

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41

Li, Guo Qing, Chang Sheng Chai, Song Fan, and Lin Guo Zhao. "Cloning of a Cellobiohydrolase Gene (cbh1) from Aspergillus niger and Heterogenous Expression in Pichia pastoris." Advanced Materials Research 347-353 (October 2011): 2443–47. http://dx.doi.org/10.4028/www.scientific.net/amr.347-353.2443.

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A gene encoding a cellobiohydrolase (CBH) was isolated from Aspergillus niger-NL-1 and designated as cbh1. The cbh1 gene contains 1,515 nucleotides with three introns and encodes a 452-amino acid protein with a molecular weight of approximately 60 kDa. The amino acid sequence encoded by cbh1 shows high homology with the sequence of glycoside hydrolase fimily 7. The cellobiohydrolase (cbh1) gene was succussfully expressed in Pichia pastoris KM71H. The recombinant CBHⅠshowed an optimal working condition at 60 °C, pH 4.0 with Kmand Vmaxtoward CMC-Na of 13.81 mM and 0.269 μmol/min, respectively. The enzyme retained more than 80 % of its initial activity after 2 h of incubation at 90 °C and was stable in pH range 1.0～10.0. Because of its moderately stable at high temperature and stability through wide range of pH, this enzyme has potential in various industrial applications.

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42

Igarashi, Kiyohiko, Takayuki Uchihashi, Anu Koivula, Masahisa Wada, Satoshi Kimura, Tetsuaki Okamoto, Merja Penttilä, Toshio Ando, and Masahiro Samejima. "Traffic Jams Reduce Hydrolytic Efficiency of Cellulase on Cellulose Surface." Science 333, no. 6047 (September 1, 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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Konstantinidis, A. K., I. Marsden, and M. L. Sinnott. "Hydrolyses of α- and β-cellobiosyl fluorides by cellobiohydrolases of Trichoderma reesei." Biochemical Journal 291, no. 3 (May 1, 1993): 883–88. http://dx.doi.org/10.1042/bj2910883.

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Cellobiohydrolase II hydrolyses alpha- and beta-D-cellobiosyl fluorides to alpha-cellobiose at comparable rates, according to Michaelis-Menten kinetics. The stereochemistry, absence of transfer products and strict hyperbolic kinetics of the hydrolysis of alpha-cellobiosyl fluoride suggest that the mechanism for the alpha-fluoride may be the enzymic counterpart of the SNi reaction observed in the trifluoroethanolysis of alpha-glucopyranosyl fluoride [Sinnott and Jencks (1980) J. Am. Chem. Soc. 102, 2026-2032]. The absolute factors by which this enzyme accelerates fluoride ion release are small and greater for the alpha-fluoride than for the beta, suggesting that its biological function may not be just glycoside hydrolysis. Cellobiohydrolase I hydrolyses only beta-cellobiosyl fluoride, which is, however, an approx. 1-3% contaminant in alpha-cellobiosyl fluoride as prepared and purified by conventional methods. Instrumental assays for the various components of the cellulase complex are discussed.

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Sadana, Jai C., and Rajkumar V. Patil. "Endo-type mode of action of (1 → 4)-β-D-glucan cellobiohydrolase from Sclerotium rolfsii." Canadian Journal of Biochemistry and Cell Biology 63, no. 12 (December 1, 1985): 1250–52. http://dx.doi.org/10.1139/o85-156.

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Sclerotium (1 → 4)-β-D-glucan cellobiohydrolase has two types of activities: an endo-type mode of action forming insoluble short fibres from native cotton and its endwise action of removing cellobiosyl units from the nonreducing chain ends of β-1,4-glucans.

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Kondo, H., K. Yaoi, M. Suzuki, N. Noro, S. Tsuda, and Y. Mitsuishi. "X-ray crystal structure analysis of Oligoxyloglucan reducing end-specific cellobiohydrolase." Seibutsu Butsuri 43, supplement (2003): S36. http://dx.doi.org/10.2142/biophys.43.s36_1.

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Korotkova, O. G., E. A. Rubtsova, I. A. Shashkov, A. A. Volchok, E. G. Kondratieva, О. А. Sinitsyna, A. M. Rozhkova, et al. "Comparison Analysis of the Composition and Properties of Fodder Enzyme Preparations." Kataliz v promyshlennosti 18, no. 4 (July 23, 2018): 72–78. http://dx.doi.org/10.18412/1816-0387-2018-4-72-78.

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The composition and properties of a wide range of domestic and foreign enzyme preparations (EP), used as additives to feeds of farm animals and poultry, are analyzed. The content of the main active enzymes – endoglucanases (beta-glucanases), cellobiohydrolases and xylanases, leading to biocatalytic destruction of non-starch polysaccharides, which are anti-nutritional factors of feeds and causing their incomplete digestion, is determined. It is shown that, based on the data on the component composition and the level of different types of activity, the studied enzyme preparations can be divided into three groups: a) with high xylanase and low cellulase (endoglucanase and cellobiohydrolase) content, b) high cellulase and low xylanase content, c) containing cellobiohydrolases, endoglucanases and xylanases in a different ratio, but without significant predominant of any of these enzymes. The ability of EP to reduce the viscosity of water-soluble non-starch polysaccharides – xylans and beta-glucans- has been studied. Among the enzyme preparations that have xylanase in their composition and belong to groups b) and c), a number of preparations have been determined which, at the same dosage according to xylanase activity, most effectively reduced the viscosity of the aqueous extract of rye containing xylans (Econase XT 25, Agroxyl Plus, Agroxyl Premium, Rovabio Max AP, Sunzyme). It was shown that the xylanase of precisely these EP is not inhibited by protein inhibitors of rye. At the same dosage for beta-glucanase activity, the viscosity of water-soluble beta-glucans of barley was most effectively reduced by the EP Xybeten CELL, Cellulase, Agroxyl, Agrocell, Axtra XB 201, Rovabio Max AP and Vilzyme. For all studied EP, no inhibitory effect of the barley extract on beta-glucanase activity was found.

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Textor, Larissa C., Francieli Colussi, Rodrigo L. Silveira, Viviane Serpa, Bruno L. de Mello, João Renato C. Muniz, Fabio M. Squina, Nei Pereira, Munir S. Skaf, and Igor Polikarpov. "Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I fromTrichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity." FEBS Journal 280, no. 1 (November 29, 2012): 56–69. http://dx.doi.org/10.1111/febs.12049.

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Hori, Chiaki, Hitoshi Suzuki, Kiyohiko Igarashi, and Masahiro Samejima. "Transcriptional Response of the Cellobiose Dehydrogenase Gene to Cello- and Xylooligosaccharides in the Basidiomycete Phanerochaete chrysosporium." Applied and Environmental Microbiology 78, no. 10 (March 9, 2012): 3770–73. http://dx.doi.org/10.1128/aem.00150-12.

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ABSTRACTCellobiose dehydrogenase (CDH) gene transcripts were quantified by reverse transcription-PCR (RT-PCR) in cultures ofPhanerochaete chrysosporiumsupplemented with various cello- and xylooligosaccharides in order to elucidate the mechanism of enhanced CDH production in xylan/cellulose culture. Cellotriose and cellotetraose inducedcdhexpression, while xylobiose and xylotriose induced expression of cellobiohydrolase genes, especiallycel7C.

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Tachioka, Mikako, Akihiko Nakamura, Takuya Ishida, Kiyohiko Igarashi, and Masahiro Samejima. "Crystal structure of a family 6 cellobiohydrolase from the basidiomycetePhanerochaete chrysosporium." Acta Crystallographica Section F Structural Biology Communications 73, no. 7 (June 17, 2017): 398–403. http://dx.doi.org/10.1107/s2053230x17008093.

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Cellobiohydrolases belonging to glycoside hydrolase family 6 (CBH II, Cel6A) play key roles in the hydrolysis of crystalline cellulose. CBH II from the white-rot fungusPhanerochaete chrysosporium(PcCel6A) consists of a catalytic domain (CD) and a carbohydrate-binding module connected by a linker peptide, like other known fungal cellobiohydrolases. In the present study, the CD ofPcCel6A was crystallized without ligands, andp-nitrophenyl β-D-cellotrioside (pNPG3) was soaked into the crystals. The determined structures of the ligand-free andpNPG3-soaked crystals revealed that binding of cellobiose at substrate subsites +1 and +2 induces a conformational change of the N-terminal and C-terminal loops, switching the tunnel-shaped active site from the open to the closed form.

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Ekborg, Nathan A., Wendy Morrill, Adam M. Burgoyne, Li Li, and Daniel L. Distel. "CelAB, a Multifunctional Cellulase Encoded by Teredinibacter turnerae T7902T, a Culturable Symbiont Isolated from the Wood-Boring Marine Bivalve Lyrodus pedicellatus." Applied and Environmental Microbiology 73, no. 23 (October 12, 2007): 7785–88. http://dx.doi.org/10.1128/aem.00876-07.

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ABSTRACT We characterized a multifunctional cellulase (CelAB) encoded by the endosymbiont Teredinibacter turnerae T7902T. CelAB contains two catalytic and two carbohydrate-binding domains, each separated by polyserine linker regions. CelAB binds cellulose and chitin, degrades multiple complex polysaccharides, and displays two catalytic activities, cellobiohydrolase (EC 3.2.1.91) and β-1,4(3) endoglucanase (EC 3.2.1.4).

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Journal articles on the topic 'Cellobiohydrolase I'

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