Efficient production by Escherichia coli of recombinant protein using salting-out effect protecting against proteolytic degradation.
To produce glucoamylase efficiently as a recombinant protein, E. coli was grown with 20 g (NH4)2SO4 l-1 which removed proteolytic activity but did not effect cell growth. Growth in M9 medium with 20 g (NH4)2SO4 l-1 produced 11 U glucoamylase ml-1 compared to 7 U ml-1 without addition. Furthermore, the glucoamylase activity was maintained at about 9 U ml-1.
Kobayashi
Fumihisa
F
Department of Chemistry and Chemical Engineering, Faculty of Engineering, Kanazawa University, 2-40-20 Kodatsuno, Kanazawa 920-8667, Japan.
Nakamura
Yoshitoshi
Y
D000645:Ammonium Sulfate / Q000494:pharmacology*; D002455:Cell Division / Q000187:drug effects; D003001:Cloning, Molecular; D003470:Culture Media / Q000494:pharmacology; D004926:Escherichia coli / Q000166:cytology / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005087:Glucan 1,4-alpha-Glucosidase / Q000096:biosynthesis* / Q000235:genetics; D010447:Peptide Hydrolases / Q000096:biosynthesis / Q000235:genetics; D011786:Quality Control; D011994:Recombinant Proteins / Q000096:biosynthesis; D012492:Salts / Q000378:metabolism; D013431:Sulfates / Q000494:pharmacology*; D014158:Transcription, Genetic
D003470:Culture Media; D011994:Recombinant Proteins; D012492:Salts; D013431:Sulfates; C012036:sodium sulfate; D005087:Glucan 1,4-alpha-Glucosidase; D010447:Peptide Hydrolases; D000645:Ammonium Sulfate