Co-expression of chaperones from P. furiosus enhanced the soluble expression of the recombinant hyperthermophilic α-amylase in E. coli

Cell Stress and Chaperones

Volumn 21, Issue 3, 2016, Pages 477-484

  Peng, Shuaiying ^a   Chu, Zhongmei ^b,c   Lu, Jianfeng ^b,c   Li, Dongxiao ^b,c   Wang, Yonghong ^a   Yang, Shengli ^b,c   Zhang, Yi ^b,c  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b Chinese Academy of Sciences   (China)

^c INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Hyperthermophilic amylase; Molecular chaperones; Prefoldin; Pyrococcus furiosus; Soluble expression

Indexed keywords

AMYLASE; CHAPERONE; CHAPERONIN 60; PREFOLDIN; RECOMBINANT PROTEIN; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; CELL INCLUSION; CENTRIFUGATION; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE EXPRESSION SYSTEM; HYPERTHERMOPHILIC BACTERIUM; MOLECULAR CLONING; NONHUMAN; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PYROCOCCUS FURIOSUS; SUPERNATANT; BIOSYNTHESIS; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; HEAT;

ALPHA-AMYLASES; ENZYME STABILITY; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; HOT TEMPERATURE; MOLECULAR CHAPERONES; PYROCOCCUS FURIOSUS;

EID: 84957627048     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-016-0675-7     Document Type: Article

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