High-yield secretory production of stable, active trypsin through engineering of the N-terminal peptide and self-degradation sites in Pichia pastoris

Author:

Zhang Yunfeng,Huang Hao,Yao Xinhui,Du Guocheng,Chen Jian,Kang Zhen

Funder

National Natural Science Foundation of China

Central Universities

Natural Science Foundation of Jiangsu Province

Publisher

Elsevier BV

Subject

Waste Management and Disposal,Renewable Energy, Sustainability and the Environment,General Medicine,Environmental Engineering,Bioengineering

Reference48 articles.

1. Real-time PCR-based determination of gene copy numbers in Pichia pastoris;Abad;Biotechnol. J.,2010

2. Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production;Ahmad;Appl. Microbiol. Biotechnol.,2014

3. The amino-terminal 29 amino acids of cytochrome P450 2C1 are sufficient for retention in the endoplasmic reticulum;Ahn;J. Biol. Chem.,1993

4. A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae;Bae;Appl. Microbiol. Biotechnol.,2016

5. Interaction between trypsin and alginate: an ITC and DLS approach to the formation of insoluble complexes;Braia;Colloids Surf. B. Biointerfaces,2017

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