Cloning of a gene encoding thermostable cellobiohydrolase from the thermophilic fungus<i>Chaetomium thermophilum</i>and its expression in<i>Pichia pastoris</i>

Li, Y.-L.; Li, H.; Li, A.-N.; Li, D.-C.

doi:10.1111/j.1365-2672.2009.04171.x

Cited by 37 publications

(15 citation statements)

References 52 publications

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“…Transformation of T. reesei with two endochitinase genes from Melanocarpus albomyces resulted in an increase in cellulase activity several times higher than that of the parental M. albomyces strain [23]. The majority of the recombinant cellulases expressed in yeast and filamentous fungi are glycosylated [16, 18]. Both the strain and culture conditions can affect the type and extent of the glycosylation [29].…”

Section: Cloning Expression and Regulation Of Cellulase Genes Fromentioning

confidence: 99%

Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential

Papageorgiou

2011

Enzyme Research

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Thermophilic fungal cellulases are promising enzymes in protein engineering efforts aimed at optimizing industrial processes, such as biomass degradation and biofuel production. The cloning and expression in recent years of new cellulase genes from thermophilic fungi have led to a better understanding of cellulose degradation in these species. Moreover, crystal structures of thermophilic fungal cellulases are now available, providing insights into their function and stability. The present paper is focused on recent progress in cloning, expression, regulation, and structure of thermophilic fungal cellulases and the current research efforts to improve their properties for better use in biotechnological applications.

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Section: Cloning Expression and Regulation Of Cellulase Genes Fromentioning

confidence: 99%

Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential

Papageorgiou

2011

Enzyme Research

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“…Heterologous expression in hosts such as Pichia pastoris, Escherichia coli, or S. cerevisiae is attractive, especially because they have low background of potentially interfering activities [13]. Many fungal glycosyl hydrolases and other proteins have been successfully expressed in P. pastoris [e.g., 25,32,36]. There are two problems associated with purification from native sources and expression in heterologous systems, namely, glycosylation heterogeneity and abnormal glycosylation, respectively (other posttranslational modifications can also complicate the issue-see Lappalainen et al [33]).…”

Section: Progress In Enzyme Research In the Doe Great Lakes Bioenergymentioning

confidence: 99%

Improving Enzymes for Biomass Conversion: A Basic Research Perspective

2010

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The cost of enzymes for converting plant biomass materials to fermentable sugars is a major impediment to the development of a practical lignocellulosic ethanol industry. Research on enzyme optimization with the goal of reducing the cost of converting biomass materials such as corn stover into glucose, xylose, and other sugars is being actively pursued in private industry, academia, and government laboratories. Under the auspices of the Department of Energy Great Lakes Bioenergy Research Center, we are taking several approaches to address this problem, including "bioprospecting" for superior key enzymes, protein engineering, and high-level expression in plants. A particular focus is the development of synthetic enzyme mixtures, in order to learn which of the hundreds of known enzymes are important and in what ratios. A core set comprises cellobiohydrolase, endoglucanase, β-glucosidase, endoxylanase, and β-glucosidase. Accessory enzymes include esterases, proteases, nonhydrolytic proteins, and glycosyl hydrolases that cleave the less frequent chemical linkages found in plant cell walls.

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“…Cellulose constitutes bulk of the plant cell wall materials and is the most abundant and renewable non-fossil carbon source on earth (Li et al 2009). Cellulose occurs in municipal wastes, forest products, agriculture, fruits and vegetables.…”

Section: Introductionmentioning

confidence: 99%

Optimization of cellulase production by Penicillium sp.

2016

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The production of cellulolytic enzymes (β-exoglucanase, β-endoglucanase and β-glucosidase) by Penicillium sp. on three different media in liquid shake culture conditions was compared. The organism exhibited relatively highest activity of endoglucanase among three enzymes measured at 7-day interval during the course of its growth on Czapek-Dox medium supplemented with 0.5 % (w/v) cellulose. Cellulose at 0.5 %, lactose at 0.5 %, sawdust at 0.5 %, yeast extract at 0.2 % as a nitrogen source, pH 5.0 and 30 °C temperature were found to be optimal for growth and cellulase production by Penicillium sp. Yields of Fpase, CMCase and β-glucosidase, attained on optimized medium with Penicillium sp. were 8.7, 25 and 9.52 U/ml, respectively with increment of 9.2, 5.9 and 43.8-folds over titers of the respective enzyme on unoptimised medium. Cellulase of the fungal culture with the ratio of β-glucosidase to Fpase greater than one will hold potential for biotechnological applications.

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Cloning of a gene encoding thermostable cellobiohydrolase from the thermophilic fungusChaetomium thermophilumand its expression inPichia pastoris

Cited by 37 publications

References 52 publications

Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential

Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential

Improving Enzymes for Biomass Conversion: A Basic Research Perspective

Optimization of cellulase production by Penicillium sp.

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