N-Glycoform Diversity of Cellobiohydrolase I from Penicillium decumbens and Synergism of Nonhydrolytic Glycoform in Cellulose Degradation

Gao, Le; Gao, Feng; Wang, Lushan; Geng, Cunliang; Chi, Lianli; Zhao, Jian; Qu, Yinbo

doi:10.1074/jbc.m111.332890

Cited by 58 publications

(33 citation statements)

References 34 publications

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“…508 They found Man x GlcNAc y residues (where x = 2−5 and y = 1−2) attached at Asn137. The glycoform with the lowest amount of mannose in its glycosylation was shown to have zero detectable activity on pNPC, but it was only this glycoform that synergistically increased the glucose yield of an industrial enzyme cocktail (by a factor of 2).…”

Section: Pyroglutamatementioning

confidence: 98%

Fungal Cellulases

et al. 2015

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Section: Pyroglutamatementioning

confidence: 98%

Fungal Cellulases

et al. 2015

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“…However, because of the changes in the glycosylation extent, Tr-Cel7A native status with different molecular masses (from ~57 to ~70 kDa) were detected in T. reesei [12]. Same as in Penicillium decumbens, the native Pd-Cel7A also showed different molecular masses (from ~57 to ~74 kDa) [24]. For same reason, in S. cerevisiae, the secreted Tr-Cel7A with the same amino acid residues sequence also showed different molecular masses even over 100 kDa, which meant it was hypeglycosylated.…”

Section: Discussionmentioning

confidence: 99%

“…Glycosylation might affect the protein secondary structure such as folding, disulfide bonds formation and so on [23,24,26]. For Cel7A and other enzymes with similar function, N-glycan in the catalytic domain might also affect its binding with the cellulose substrate and its stability [27][28][29].…”

Section: Discussionmentioning

confidence: 99%

Promotion of Extracellular Activity of Cellobiohydrolase I from Trichoderma reesei by Protein Glycosylation Engineering in Saccharomyces cerevisiae

Shen²,

Hou³

et al. 2013

Curr Synthetic Sys Biol

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The N-glycosylation in Saccharomyces cerevisiae is of the high-mannose type, which affects the activity of the secreted heterologous glycoproteins. Cellobiohydrolase I (Tr-Cel7A) from Trichoderma reesei, is thus hyperglycosylated when expressed in S. cerevisiae. In the present work, three genes encoding the endogenous mannosyltransferases, Och1p, Mnn9p and Mnn1p, involved in glycoprotein processing in the S. cerevisiae Golgi apparatus, were individually or combinatorially disrupted to investigate the effect of the glycosylation extent on the activity of the secreted Tr-Cel7A. The glycosylation of the recombinant Tr-Cel7A was decreased and its extracellular activity was increased in all the deletion mutants. The simultaneous deletion of och1 and mnn1 has the most improvement on extracellular Tr-Cel7A activity. After expressed the α-1,2-mannosidase (Tr-Mds1p) from T. reesei in mnn1Δ/och1Δ strain, the Tr-Cel7A activity was further increased up to 320 ± 8% higher than that of the wild type strain. Such activity improvement was due not only to the higher secretion yield but also to the increased specific activity resulted from the changes in glycosylation. The results thus indicated that protein glycosylation engineering in S. cerevisiae was an effective approach to improve the extracellular activity of Tr-Cel7A.

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“…Currently, two classifications of synergism are widely accepted: synergism between EG and CBH and synergism between CBHs [15]. Previous studies have shown that CBH I added to exogenous commercial cellulase synergistically acts on cellulose [31] and that CBH I and CBH II synergistically act on MCC [13]. Unfortunately, synergism between CBH I and CBH II from Penicillium pinophilum has not been observed, but CBH and a trace of EG generate a very high synergistic cooperation [32].…”

Section: Synergism Of C-p16trmentioning

confidence: 99%

A Newly Isolated Penicillium oxalicum 16 Cellulase with High Efficient Synergism and High Tolerance of Monosaccharide

Zhao

Wang

Tong

et al. 2015

Appl Biochem Biotechnol

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Compared to Trichoderma reesei RUT-C30 cellulase (Trcel), Penicillium oxalicum 16 cellulase (P16cel) from the fermentation supernatant produced a 2-fold higher glucose yield when degrading microcrystalline cellulose (MCC), possessed a 10-fold higher β-glucosidase (BGL) activity, but obtained somewhat lower other cellulase component activities. The optimal temperature and pH of β-1,4-endoglucanase, cellobiohydrolase, and filter paperase from P16cel were 50-60 °C and 4-5, respectively, but those of BGL reached 70 °C and 5. The cellulase cocktail of P16cel and Trcel had a high synergism when solubilizing MCC and generated 1.7-fold and 6.2-fold higher glucose yields than P16cel and Trcel at the same filter paperase loading, respectively. Additional low concentration of fructose enhanced the glucose yield during enzymatic hydrolysis of MCC; however, additional high concentration of monosaccharide (especially glucose) reduced cellulase activities and gave a stronger monosaccharide inhibition on Trcel. These results indicate that P16cel is a more excellent cellulase than Trcel.

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N-Glycoform Diversity of Cellobiohydrolase I from Penicillium decumbens and Synergism of Nonhydrolytic Glycoform in Cellulose Degradation

Cited by 58 publications

References 34 publications

Fungal Cellulases

Fungal Cellulases

Promotion of Extracellular Activity of Cellobiohydrolase I from Trichoderma reesei by Protein Glycosylation Engineering in Saccharomyces cerevisiae

A Newly Isolated Penicillium oxalicum 16 Cellulase with High Efficient Synergism and High Tolerance of Monosaccharide

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