Substrate affinity and catalytic efficiency are improved by decreasing glycosylation sites in Trichoderma reesei cellobiohydrolase I expressed in Pichia pastoris-Reference-Cited by-同舟云学术

Substrate affinity and catalytic efficiency are improved by decreasing glycosylation sites in Trichoderma reesei cellobiohydrolase I expressed in Pichia pastoris

Published:2015-11-23 Issue:3 Volume:38 Page:483-488
ISSN:0141-5492
Container-title:Biotechnology Letters
language:en
Short-container-title:Biotechnol Lett

Author:

Ranaei Siadat Seyed Omid^ORCID,Mollasalehi Hamidreza,Heydarzadeh Narjes

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biotechnology,Bioengineering,Applied Microbiology and Biotechnology

Link

http://link.springer.com/content/pdf/10.1007/s10529-015-1997-8.pdf

Reference16 articles.

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2. Ghose TK (1987) Measurement of cellulase activities. Pure Appl Chem 59:257–268

3. Godbole S et al (1999) Cloning and expression of Trichoderma reesei cellobiohydrolase I in Pichia pastoris. Biotechnol Progr 15:828–833

4. Guedon E, Desvaux M, Petitdemange H (2002) Improvement of cellulolytic properties of Clostridium cellulolyticum by metabolic engineering. Appl Environ Microbiol 68:53–58

5. Harrison MJ, Nouwens AS, Jardine DR, Zachara NE, Gooley AA, Nevalainen H, Packer NH (1998) Modified glycosylation of cellobiohydrolase I from a high cellulase-producing mutant strain of Trichoderma reesei. Eur J Biochem 256:119–127

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