ArticleThe Journal of biological chemistry2012
N-glycoform diversity of cellobiohydrolase I from Penicillium decumbens and synergism of nonhydrolytic glycoform in cellulose degradation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Catalytic Efficiency Improvement in Cellobiohydrolase I by Cross-Species Domain Exchange Engineering.International journal of molecular sciences · 2025Article
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
- Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites.Biotechnology for biofuels · 2020Article
- Three glycoside hydrolase family 12 enzymes display diversity in substrate specificities and synergistic action between each other.Molecular biology reports · 2019Article
- UniqueJournal of biological engineering · 2019Article
- Distinct roles of N- and O-glycans in cellulase activity and stability.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Cellobiohydrolase B ofPeerJ · 2017Article
- Proteomic analysis of the biomass hydrolytic potentials of Penicillium oxalicum lignocellulolytic enzyme system.Biotechnology for biofuels · 2016Article
- Asn124 of Cel5A from Hypocrea jecorina not only provides the N-glycosylation site but is also essential in maintaining enzymatic activity.BMB reports · 2014Article
- Differences in the adsorption of enzymes onto lignins from diverse types of lignocellulosic biomass and the underlying mechanism.Biotechnology for biofuels · 2014Article
- A Dictyostelium cellobiohydrolase orthologue that affects developmental timing.Development genes and evolution · 2014Article
- Article
- Genomic and secretomic analyses reveal unique features of the lignocellulolytic enzyme system of Penicillium decumbens.PloS one · 2013Article
- Endo-exo synergism in cellulose hydrolysis revisited.The Journal of biological chemistry · 2012Article
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Authors and funding
7 authors.
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Abstract
Four cellobiohydrolase I (CBHI) glycoforms, namely, CBHI-A, CBHI-B, CBHI-C, and CBHI-D, were purified from the cultured broth of Penicillium decumbens JU-A10. All glycoforms had the same amino acid sequence but displayed different characteristics and biological functions. The effects of the N-glycans of the glycoforms on CBH activity were analyzed using mass spectrum data. Longer N-glycan chains at the Asn-137 of CBHI increased CBH activity. After the N-glycans were removed using site-directed mutagenesis and homologous expression in P. decumbens, the specific CBH activity of the recombinant CBHI without N-glycosylation increased by 65% compared with the wild-type CBHI with the highest specific activity. However, the activity was not stable. Only the N-glycosylation at Asn-137 can improve CBH activity by 40%. rCBHI with N-glycosylation only at Asn-470 exhibited no enzymatic activity. CBH activity was affected whether or not the protein was glycosylated, together with the N-glycosylation site and N-glycan structure. N-Glycosylation not only affects CBH activity but may also bring a new feature to a nonhydrolytic CBHI glycoform (CBHI-A). By supplementing CBHI-A to different commercial cellulase preparations, the glucose yield of lignocellulose hydrolysis increased by >20%. After treatment with a low dose (5 mg/g substrate) of CBHI-A at 50 °C for 7 days, the hydrogen-bond intensity and crystalline degree of cotton fibers decreased by 17 and 34%, respectively. These results may provide new guidelines for cellulase engineering.
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