NDLI: Overexpression of Candida rugosa lipase Lip1 via combined strategies in Pichia pastoris.

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Overexpression of Candida rugosa lipase Lip1 via combined strategies in Pichia pastoris.

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Overexpression of Candida rugosa lipase Lip1 via combined strategies in Pichia pastoris.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Li, Xu Liu, Zimin Wang, Guilong Pan, Dujie Jiao, Liangcheng Yan, Yunjun
Description	Author Affiliation: Li X ( Key Lab of Molecular Biophysics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, PR China. Electronic address: xuli@mail.hust.edu.cn.); Liu Z ( Key Lab of Molecular Biophysics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, PR China.); Wang G ( Key Lab of Molecular Biophysics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, PR China.); Pan D ( Key Lab of Molecular Biophysics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, PR China.); Jiao L ( Key Lab of Molecular Biophysics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, PR China.); Yan Y ( Key Lab of Molecular Biophysics of Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, PR China. Electronic address: yanyunjun@mail.hust.edu.cn.)
Abstract	In this study, combined strategies were employed to heterologously overexpress Candida rugosa lipase Lip1 (CRL1) in a Pichia pastoris system. The LIP1 gene was systematically codon-optimized and synthesized in vitro. The Lip1 activity of a recombinant strain harboring three copies of the codon-optimized LIP1 gene reached 1200 U/mL in a shake flask culture. Higher lipase activity, 1450 U/mL, was obtained using a five copy number construct. Co-expressing one copy of the ERO1p and BiP chaperones with Lip1p, the CRL1 lipase yield further reached 1758 U/mL, which was significantly higher than that achieved by expressing Lip1p alone or only co-expressing one molecular chaperone. When cultivated in a 3 L fermenter under optimal conditions, the recombinant strain GS115/87-ZA-ERO1p-BiP #7, expressing the molecular chaperones Ero1p and BiP, produced 13,490 U/mL of lipase activity at 130 h, which was greater than the 11,400 U/mL of activity for the recombinant strain GS115/pAO815- -mCRL1 #87, which did not express a molecular chaperone. This study indicates that a strategy of combining codon optimization with co-expression of molecular chaperones has great potential for the industrial-scale production of pure CRL1.
File Format	HTM / HTML
ISSN	01410229
Volume Number	82
e-ISSN	18790909
Journal	Enzyme and Microbial Technology
Language	English
Publisher	Elsevier
Publisher Date	2016-01-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Microbiology Discipline Biochemistry Discipline Biotechnology Candida Enzymology Carboxylic Ester Hydrolases Biosynthesis Cloning, Molecular Methods Fungal Proteins Pichia Metabolism Biocatalysis Bioreactors Isolation & Purification Codon Genetics Fermentation Gene Expression Regulation, Fungal Genes, Fungal Genetic Vectors Molecular Chaperones Plasmids Recombinant Fusion Proteins Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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