Catalytic rate improving keratinase mutants and preparation method thereof

A technology of keratinase mutation and keratinase, applied in biochemical equipment and methods, botanical equipment and methods, hydrolytic enzymes, etc. Detergent and other problems, to achieve the effect of enhancing the anti-detergent SDS ability and good application prospects
CN105002152AActive Publication Date: 2015-10-28JIANGNAN UNIV
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Patent Information

Authority / Receiving Office
CN · China
Current Assignee / Owner
JIANGNAN UNIV
Publication Date
2015-10-28

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Abstract

The present invention discloses catalytic rate improving keratinase mutants and a preparation method thereof, and belongs to the field of enzyme engineering. According to the present invention, the C terminal structure of keratinase KerSMD is sheared to obtain a series of keratinase mutants, wherein the catalytic rate of the keratinase mutants on the casein substrate is significantly improved and is increased by 33-103%, particularly the mutant V355 has effects of significantly improved catalytic rate, significantly improved enzyme activity, enhanced salt tolerance and enhanced detergent resistance, the characteristics of no collagenase activity and salt tolerance of the V355 can be used in the leather processing industry, the catalytic rate on the substrate is rapid, and the V355 has the characteristic of detergent resistance so as to be subjected to laundry additive production application.
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Description

technical field

[0001] The invention relates to a keratinase mutant with improved catalytic rate and a preparation method thereof, belonging to the field of enzyme engineering. Background technique

[0002] Keratinase is an enzyme that can specifically degrade keratin, which is produced by various microorganisms such as fungi, actinomycetes and bacteria. Keratinase is widely used in industries such as food, medicine, feed, refining and tanning. It has the functions of tenderizing meat, producing advanced nutrition, immune preparations and feed additives, as well as beautifying and softening leather. It can also cause mad cow disease and human Degradation of Prion in Creutzfeldt-Jakob disease. The keratinase gene reported so far mainly comes from the kerA gene of a foreign strain of Bacillus licheniformis. Although keratinase has great application and research value, the keratinase screened from wild bacteria has low catalytic efficiency, low substrate specificity, and cann...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
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