Swapping of pro-sequences between keratinases of Bacillus licheniformis and Bacillus pumilus: Altered substrate specificity and thermostability

Enzyme and Microbial Technology

Volumn 51, Issue 3, 2012, Pages 131-138

  Rajput, Rinky ^a   Tiwary, Ekta ^a   Sharma, Richa ^a   Gupta, Rani ^a  

^a UNIVERSITY OF DELHI   (India)

Author keywords

Bacillus licheniformis; Bacillus pumilus; Keratinase; Pro sequence

Indexed keywords

BACILLUS LICHENIFORMIS; BACILLUS PUMILUS; CLEAVAGE SITES; CONFORMATIONAL CHANGE; E. COLI; KERATINASE; PRO-SEQUENCE; SOLUBLE SUBSTRATES; SUBSTRATE SPECIFICITY; TEMPERATURE KINETICS;

ESCHERICHIA COLI; SUBSTRATES;

BACTERIOLOGY;

CASEIN; INSULIN; KERATIN; KERATINASE;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS LICHENIFORMIS; BACILLUS PUMILUS; BETA CHAIN; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STABILITY; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PH; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; STEADY STATE; TEMPERATURE;

AMINO ACID SEQUENCE; BACILLUS; BACTERIAL PROTEINS; CLONING, MOLECULAR; ENZYME PRECURSORS; ENZYME STABILITY; ESCHERICHIA COLI; GENETIC ENGINEERING; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; PEPTIDE HYDROLASES; PROTEIN FOLDING; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

BACILLUS LICHENIFORMIS; BACILLUS PUMILUS;

EID: 84863093129     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2012.04.010     Document Type: Article

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