A new method for the extracellular production of recombinant thermolysin by co-expressing the mature sequence and pro-sequence in Escherichia coli

Protein Engineering, Design and Selection

Volumn 20, Issue 8, 2007, Pages 375-383

  Yasukawa, Kiyoshi ^a   Kusano, Masayuki ^a   Inouye, Kuniyo ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Autocatalytic digestion activity; Escherichia coli; Metalloproteinase; Pro sequence; Thermolysin

Indexed keywords

AUTOCATALYTIC DIGESTION ACTIVITY; METALLOPROTEINASE; PRO-SEQUENCES; THERMOLYSIN;

CATALYST ACTIVITY; CELL CULTURE; ESCHERICHIA COLI; GENE EXPRESSION; NUCLEIC ACID SEQUENCES;

ENZYMES;

ALANINE; AMIDE; ESTER DERIVATIVE; GLUTAMIC ACID; N [3 (2 FURYL)ACRYLOYL]GLYCYLLEUCINAMIDE; N CARBOBENZOXYASPARTYLPHENYLALANINE METHYL ESTER; POLYPEPTIDE; RECOMBINANT PROTEIN; THERMOLYSIN; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM CULTURE; CATALYSIS; CONTROLLED STUDY; CULTURE MEDIUM; ESCHERICHIA COLI; EXTRACELLULAR SPACE; GENE; GENE EXPRESSION; GENE SEQUENCE; HYDROLYSIS; MUTANT; NONHUMAN; NPR GENE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; SEQUENCE ANALYSIS; WILD TYPE;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACILLUS; CASEINS; ESCHERICHIA COLI; FERMENTATION; GENE EXPRESSION; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; MOLECULAR SEQUENCE DATA; PLASMIDS; RECOMBINANT PROTEINS; THERMOLYSIN;

BACILLUS THERMOPROTEOLYTICUS; ESCHERICHIA COLI;

EID: 34548801455     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzm031     Document Type: Article

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