Relevant bibliographies by topics / Cellobiohydrolase I

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Academic literature on the topic 'Cellobiohydrolase I'

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

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Journal articles on the topic "Cellobiohydrolase I"

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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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Dissertations / Theses on the topic "Cellobiohydrolase I"

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Miller, Laurie. "Studies on CBH1 : a cellobiohydrolase of Sclerotinia sclerotiorum." Thesis, University of Sheffield, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364190.

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Zulu, Joseph. "Cloning and regulation of the cellobiohydrolase I gene from Pleurotus sajor-caju." Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285568.

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Lamour, Jarryd. "Expression of stress-tolerance related genes in Saccharomyces cerevisiae producing heterologous cellobiohydrolase." University of the Western Cape, 2017. http://hdl.handle.net/11394/5885.

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Magister Scientiae - MSc (Biotechnology)
Cellulose is the most abundant naturally occurring renewable biopolymer on earth and a major structural component in plant cell walls, making it an ideal source of renewable energy. Consolidated bioprocessing (CBP) is a cost effective method of converting cellulose to liquid fuels such as ethanol. For CBP to be achieved an organism needs to be able hydrolyze cellulose and produce high yields of ethanol. The yeast Saccharomyces cerevisiae is an ideal CBP candidate, however wild type strains do not produce cellulases and these activities need to be engineered into yeast. In addition, the generally low secretion titers achieved by this yeast will have to be overcome.
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Keawsompong, Suttipun. "Cloning of a cellobiohydrolase II gene and its expression in Pleurotus sajor-caju." Thesis, University of Nottingham, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.368231.

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Voltatodio, Maria Luiza. "Caracterização bioquímica e biofísica da Celobiohidrolase II do fungo Trichoderma harzianum IOC3844 produzida por expressão homóloga." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/76/76132/tde-19102012-090550/.

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O esgotamento das reservas, especialmente do petróleo mais fino, aliado à crescente demanda energética e à necessidade inadiável de reduzir as emissões de carbono para a atmosfera, sinalizam para a necessidade da busca de novas fontes de energia renováveis e limpas. As preocupações com o aquecimento global têm feito crescer o interesse mundial pelos biocombustíveis. O novo conceito de biocombustíveis de segunda geração corresponde à produção de etanol combustível a partir de biomassa lignocelulósica como matéria-prima. No entanto, para tornar possível a utilização da biomassa é necessária a conversão das moléculas constituintes da parede celular em açúcares fermentáveis. A tecnologia mais promissora para a conversão dessa biomassa lignocelulósica à etanol combustível é com base na hidrólise enzimática da celulose usando celulases. Alguns microrganismos como o fungo Trichoderma SSP. secretam um eficiente complexo enzimático de celulases. Tendo as celobiohidrolases, elevada importância na hidrólise primária da celulose, o objetivo desse trabalho foi realizar a caracterização bioquímica e biofísica a celobiohidrolase II (CBHII) do complexo de celulases do fungo filamentoso Trichoderma harzianum IOC 3844. A enzima depois de purificada mostrou uma melhor atividade contra o substrato pNPC a 60°C em pH 4,8. Estudos de eletroforese capilar mostraram apenas moléculas com uma unidade de glicose para um substrato simples inicial contendo 5 glicoses. Análises de dicroísmo circular mostraram um padrão de estrutura secundária predominante em alfa hélice, e na análise da estrutura terciária, o espectro de emissão da CBHII mostrou um comprimento de onda de fluorescência máxima a 333nm em pH5,0, indicando que os triptofanos estão parcialmente expostos ao solvente. Ensaios utilizando a técnica de espalhamento de luz a baixo ângulo, permitiram a geração de um modelo tridimensional o qual mostrou-se domínios globulares unidos por um linker, e as posições relativas entre eles, demonstrando grande similaridade com enzimas CBHII já descritas na literatura, e sendo assim, de grande interesse biotecnológico para hidrólises de biomassas.
The depletion of reserves, especially of refined oil , with increased energy demands and the urgent need to reduce the carbon emissions on the atmosphere, signals the necessity to search for new sources of energy renewable and clean. Concerns about global warming have led to an increased world interest in biofuels. The new concept of second generation biofuels corresponds to fuel ethanol production from biomass lignocellulosic feedstock. However, to make possible the use of biomass is necessary the conversion of cell-wall molecules into fermentable sugars. The most promising technology for the conversion of lignocellulosic biomass to ethanol fuel is based on the enzymatic degradation of cellulose using cellulase. Some microorganisms such Trichoderma ssp. secretes an efficient enzymatic complex of cellulase. Since the cellobiohydrolases are highly importance in the primary hydrolysis of cellulose, the objective of this study was to perform the biochemical and biophysical characterization of cellobiohydrolase II (CBHII) present into the cellulase complex from the Trichoderma harzianum IOC 3844. The enzyme showed its better activity against pNPC at 60°C and pH 4,8. Capillary electrophoresis showed only glucose molecules as the final product of C5 oligosaccharide hydrolysis. Circular dichroism analysis showed a pattern of secondary structure mainly composed of alpha helix, and the tertiary structure analysis by the emission spectrum of the CBHII showed a wavelength of maximum fluorescence at 33nm at pH 5, indicating that the tryptophans are exposed to solvent. The three dimensional model generated by SAXS showed a structure with two globular domains joined by a linker, and the relative positions among them exhibited great similarity with CBHII described on the literature, and thus, presenting a great biotechnological interest for hydrolysis of biomass.
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Tokunaga, Yuki. "Interaction analysis between lignin and carbohydrate-binding module of cellobiohydrolase I from Trichoderma reesei." Doctoral thesis, Kyoto University, 2021. http://hdl.handle.net/2433/263699.

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Nutt, Anu. "Hydrolytic and Oxidative Mechanisms Involved in Cellulose Degradation." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Universitetsbiblioteket [distributör], 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-6888.

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Koivula, Anu. "Structure-function studies of two polysacchride-degrading enzymes : Bacillus stearothermophilus [alpha]-amylase and Trichoderma reese cellobiohydrolase II /." Espoo : Technical Research Centre of Finland, 1996. http://www.vtt.fi/inf/pdf/publications/1996/P277.pdf.

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Texier, Helene. "Ingénierie des xylanases de Penicillium funiculosum IMI 378536 : amélioration de la robustesse de l'activité xylanolytique dans la préparation commerciale Rovabio Excel™." Thesis, Toulouse, INSA, 2012. http://www.theses.fr/2012ISAT0048.

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Le Rovabio Excel ™ est un cocktail enzymatique complexe sécrété par le champignon filamenteux Penicillium funiculosum. La société ADISSEO commercialise cet additif alimentaire destiné à la nutrition animale car les principales enzymes qui le constituent dégradent les polymères contenus dans les céréales, tels que les polysaccharides non amylacés. Ainsi, le Rovabio Excel™ permet d’améliorer la digestibilité et d’augmenter la valeur nutritionnelle des matières premières agricoles en réduisant la viscosité du bol alimentaire des animaux. Dans le but d’augmenter sa compétitivité, ADISSEO a fait conduire des études sur cette solution pour la caractériser biochimiquement et optimiser son potentiel xylanolytique.Ces travaux de thèse s’inscrivent dans ces projets industriels et ont poursuivi deux objectifs distincts. Le premier correspondait à l’augmentation de la thermostabilité de la protéine XynB du Rovabio Excel™, pour lui permettre de résister à la granulation. Le second concernait XynA, la protéine majoritaire de la solution multienzymatique, qui a été caractérisée biochimiquement. Les premiers résultats de caractérisation biochimique de XynA ont montré que la protéine était 100 fois plus active sur β-1,4-glucane que sur xylane. Des tests complémentaires sur pNP-cellobiose et pNP-β-D-Lactopyranose ont révélé que XynA était 5,2 fois plus active sur pNP-cellobiose et possédait une activité « exo ». Enfin, l’analyse des produits d’hydrolyse d’oligosaccharides composés de 2 à 5 unités de glucose a confirmé que la protéine XynA était une cellobiohydrolase de type I, très sensible à l’inhibition par le cellobiose (IC50 - C2 = 17,7 µM). L’étude la thermostabilité de XynB a confirmé que cette protéine n’était pas naturellement thermostable. Les résultats des travaux d’ingénierie avec l’ajout d’un pont disulfure pour rigidifier la structure 3D de la protéine n’ont pas été probants. En revanche, la création de protéines chimères à partir de protéines plus thermostables (TfxA de Thermomonospora fusca et XynII de Trichoderma reesei) a permis d’améliorer la stabilité thermodynamique de XynB avec des Tm augmentés de plus de 10°C
The Rovabio Excel™ is a complex enzymatic cocktail secreted by the filamentous fungus Penicillium funiculosum. The ADISSEO company sells it as food additive for animal feed because the main enzymes degrade polymers contained in grains, such as non-starch polysaccharides. Thus, the Rovabio Excel™ improves the digestibility and increases the nutritional value of agricultural raw materials by reducing the viscosity of the diet of animals. In order to increase its competitiveness, ADISSEO did conduct studies on this solution to characterize it biochemically and maximize its xylanolytic potential.This thesis takes part of this industrial project and have pursued two distinct objectives. The first corresponds to the increase in the thermostability of the protein XynB from the Rovabio Excel™, to enable it to resist at the granulation process. The second was XynA, the major protein of the multienzyme solution, which was characterized biochemically.Initial results of biochemical characterization of XynA showed that the protein was 100 times more active on β-1,4-glucan on xylan. Additional tests on pNP-cellobiose and pNP-β-D-Lactopyranose revealed that XynA was 5.2 times more active on pNP-cellobiose and possess an "exo-acting" activity. Finally, the analysis of products from oligosaccharides hydrolysis, composed of 2 to 5 units of glucose, confirmed that the protein XynA was a type I cellobiohydrolase, very sensitive to inhibition by cellobiose (IC50-C2 = 17.7 µM).The thermostability of XynB study has confirmed that this protein was not thermostable naturally. The results of the engineering work with the addition of a disulfide bridge to rigidify the 3D structure of the protein were not conclusive. However, the creation of chimeric proteins with more thermostable proteins (TfxA from Thermomonospora fusca and XynII from Trichoderma reesei) has improved the thermodynamic stability of XynB with Tm increased by more than 10°C
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Sibanda, Ntsako. "Evaluation of high recombinant protein secretion phenotype of saccharomyces cerevisiae segregant." Thesis, University of Limpopo, 2016. http://hdl.handle.net/10386/1803.

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Thesis (MSc. (Biochemistry)) --University of Limpopo, 2016
The ever increasing cost of fossil-based fuels and the accompanying concerns about their impact on the environment is driving research towards clean and renewable sources of energy. Bioethanol has the potential to be a replacement for liquid transportation fuels. In addition to its near zero nett carbon dioxide emissions, bio-ethanol has a high energy to weight ratio and can easily be stored in high volumes. To produce bioethanol at economically competitive prices, the major cost in the production process needs to be addressed. The addition of enzymes to hydrolyse the lignocellulosic fraction of the agricultural waste to simple sugars is considered to be the major contributor to high production cost. A consolidated bioprocess (CBP) which ideally combines all the steps that are currently accomplished in different reactors by different microorganisms into a single process step would be a more economically feasible solution. In this study the potential of yeast hybridization with a CBP approach was used. In order to evaluate the reduction or elimination of the addition of cellulolytic and hemi-cellulolytic enzymes to the ethanol production process. High cellobiohydrolase I secreting progeny from hybridization of an industrial bioethanol yeast strain, S. cerevisiae M0341, and a laboratory strain S. cerevisiae Y294 were isolated. In order to determine if this characteristic was specific to cellobiohydrolase I secretion, these strains were evaluated for their ability to secrete other relevant recombinant hydrolase enzymes for CBP-based ethanol production. A total of seven S. cerevisiae strains were chosen from a progeny pool of 28 supersecreting hybrids and reconstructed to create two parental strains; S. cerevisiae M0341 and S. cerevisiae Y294, together with their hybrid segregants strains H3M1, H3M28, H3H29, H3K27 and H3O23. Three episomal plasmids namely pNS201, pNS202 and pNS203 were constructed; these plasmids together with two already available plasmids, namely pRDH166 and pRDH182 contained genes for different reporter enzymes, namely β-glucosidase I, xylanase II, endoglucanase lll, cellobiohydrolase l and α-glucuronidase. To allow for selection of the episomal plasmids, homologous recombination was used to replace the functional URA3 gene of selected strains, with the non-functional ura3 allele from the Y294 strain. Enzyme activity was used as an indicator of the amount of enzyme secreted. Fermentation studies in a bioreactor were used to determine the metabolic burden imposed on the segregants expressing the cellobiohydrolase at high levels. In addition all segregants were tested for resistance to inhibitors commonly found in pre-treated lignocellulosic material. The M28_Cel7A was found to be the best secretor of Cel7A (Cellobiohydrolase l); however it seems as though this phenomenon imposes a significant metabolic burden on the yeast. The supersecreting hybrid strains cannot tolerate lignocellulosic inhibitors at concentrations commonly produced during pretreatment
The National Research Foundation - Renewable Energy Scholarship (NRF-RSES)
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Books on the topic "Cellobiohydrolase I"

1

Müller, Ulrike. Struktur, Expression und gezielte Inaktivierung von cell, einem vermutlich Cellobiohydrolase-codierenden Gen von Claviceps purpurea. Berlin: J. Cramer, 1997.

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

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Harjunpaa, Vesa. Enzymes hydrolysing wood polysaccharides: A progress curve study of oligosaccharide hydrolysis by two cellobiohydrolases and three Ý-mannanases. Espoo, Finland: VTT, Technical Research Centre of Finland, 1998.

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Hedeland, Mikael. Cellobiohydrolase I As a Chiral Selector. Uppsala Universitet, 1999.

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Srisodsuk, Malee. Mode of action of Trichoderma reesei cellobiohydrolase I on crystalline cellulose. 1994.

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Struktur, Expression Und Gezielte Inaktivierung Von Cell, Einem Vermutlich Cellobiohydrolase - Codierenden Gen Von Claviceps Purpurea (Bibliotheca Mycologica,). Gebruder Borntraeger Verlagsbuchhandlung, 1997.

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Reinikainen, Tapani. The cellulose-binding domain of cellobiohydrolase I from Trichoderma reesei: Interaction with cellulose and application in protein immobilization. 1994.

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Reinikainen, Tapani. The cellulose-binding domain of cellobiohydrolase I from Trichoderma reesei: Interaction with cellulose and application in protein immobilization. 1994.

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Sangseethong, Kunruedee. Immobilized cellooligosaccharides in the study of trichoderma reesei cellobiohydrolases. 1999.

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Book chapters on the topic "Cellobiohydrolase I"

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Sharma, Hem Kanta, Wensheng Qin, and Chunbao Xu. "Cellobiohydrolase (CBH) Activity Assays." In Cellulases, 185–99. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7877-9_14.

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Barnett, C., L. Sumner, R. Berka, S. Shoemaker, H. Berg, M. Gritzali, and R. Brown. "Properties of Native and Site-Mutagenized Cellobiohydrolase II." In ACS Symposium Series, 220–32. Washington, DC: American Chemical Society, 1993. http://dx.doi.org/10.1021/bk-1993-0516.ch018.

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Adney, William S., Yat-Chen Chou, Stephen R. Decker, Shi-You Ding, John O. Baker, Glenna Kunkel, Todd B. Vinzant, and Michael E. Himmel. "Heterologous Expression ofTrichoderma reesei1,4-β-D-Glucan Cellobiohydrolase (Cel 7A)." In ACS Symposium Series, 403–37. Washington, DC: American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0855.ch023.

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Donner, T. R., B. R. Evans, K. A. Affholter, and J. Woodward. "Role of Cellulose-Binding Domain of Cellobiohydrolase I in Cellulose Hydrolysis." In ACS Symposium Series, 75–83. Washington, DC: American Chemical Society, 1994. http://dx.doi.org/10.1021/bk-1994-0566.ch004.

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Ding, H., E. Vlasenko, C. Shoemaker, and S. Shoemaker. "Absorption of Endoglucanase I and Cellobiohydrolase I ofTrichoderma reeseiduring Hydrolysis of Microcrystalline Cellulose." In ACS Symposium Series, 131–43. Washington, DC: American Chemical Society, 2000. http://dx.doi.org/10.1021/bk-2001-0769.ch008.

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Dai, Ziyu, Brian S. Hooker, Ryan D. Quesenberry, and Jianwei Gao. "Expression of Trichoderma reesei Exo-Cellobiohydrolase l in Transgenic Tobacco Leaves and Calli." In Twentieth Symposium on Biotechnology for Fuels and Chemicals, 689–99. Totowa, NJ: Humana Press, 1999. http://dx.doi.org/10.1007/978-1-4612-1604-9_63.

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Laymon, Robert A., William S. Adney, Ali Mohagheghi, Michael E. Himmel, and Steven R. Thomas. "Cloning and Expression of Full-Length Trichoderma reesei Cellobiohydrolase I cDNAs in Escherichia Coli." In Seventeenth Symposium on Biotechnology for Fuels and Chemicals, 389–97. Totowa, NJ: Humana Press, 1996. http://dx.doi.org/10.1007/978-1-4612-0223-3_35.

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Lindeberg, Gunnar, Per Hansen, Jerry Ståhlberg, and Göran Pettersson. "Analogs of the cellulose binding domain of cellobiohydrolase I from Trichoderma reesei: Synthesis and binding." In Peptides 1992, 780–81. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_358.

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Annamalai, Neelamegam, Mayavan Veeramuthu Rajeswari, and Nallusamy Sivakumar. "Cellobiohydrolases: Role, Mechanism, and Recent Developments." In Biofuel and Biorefinery Technologies, 29–35. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43679-1_2.

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Srivastava, Neha, P. K. Mishra, and S. N. Upadhyay. "Cellobiohydrolase: role in cellulosic bioconversion." In Industrial Enzymes for Biofuels Production, 63–79. Elsevier, 2020. http://dx.doi.org/10.1016/b978-0-12-821010-9.00004-8.

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Conference papers on the topic "Cellobiohydrolase I"

1

Woon, J. S. K., A. M. A. Murad, and F. D. Abu Bakar. "Isolation, molecular cloning and expression of cellobiohydrolase B (CbhB) from Aspergillus niger in Escherichia coli." In THE 2015 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2015 Postgraduate Colloquium. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4931225.

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Kuutti, L., L. Laaksonen, and T. Teeri. "Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling." In Advances in biomolecular simulations. AIP, 1991. http://dx.doi.org/10.1063/1.41322.

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Muammar, Arief, Suci Aulia Ratu Fajrin, and Endah Retnaningrum. "Cellobiohydrolase A (CBHA) gene cloning from Aspergillus niger to the yeast expression vector as a stages to create cellulosic ethanol strain." In THE 6TH INTERNATIONAL CONFERENCE ON BIOLOGICAL SCIENCE ICBS 2019: “Biodiversity as a Cornerstone for Embracing Future Humanity”. AIP Publishing, 2020. http://dx.doi.org/10.1063/5.0016145.

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Reports on the topic "Cellobiohydrolase I"

1

Himmel, M. Investigations of the in Planta Expression of Active Cellobiohydrolase I: Cooperative Research and Development Final Report, CRADA Number CRD-07-219. Office of Scientific and Technical Information (OSTI), February 2011. http://dx.doi.org/10.2172/1008191.

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Beckham, G. T., and M. E. Himmel. Defining the Interactions of Cellobiohydrolase with Substrate through Structure Function Studies: Cooperative Research and Development Final Report, CRADA Number CRD-10-409. Office of Scientific and Technical Information (OSTI), July 2013. http://dx.doi.org/10.2172/1087790.

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