Keratinase mutant with improved thermal stability and preparation method thereof

A kind of keratinase mutation and keratinase technology, which is applied in the direction of botany equipment and methods, microorganism-based methods, biochemical equipment and methods, etc., can solve the problem of reducing the development and application of keratinase, poor thermal stability of keratinase, and substrate specificity. One problem is not high, to achieve the effect of improved thermal stability, improved enzyme activity, and good application prospects
CN104017791AActive Publication Date: 2014-09-03JIANGNAN UNIV

Patent Information

Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
JIANGNAN UNIV
Publication Date
2014-09-03

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Abstract

The invention discloses a keratinase mutant with improved thermal stability and a preparation method thereof, and belongs to the field of enzyme engineering. Thermal stability and substrate specificity of the keratinase are improved by interchanging N ends or C ends of two different keratinases with higher homology from the same bacterial strain. The keratinase and the mutant thereof can effectively hydrolyze water-insoluble keratinase substrates such as feathers, wools, and the like, and can be used for leather spinning industry and feed industry.
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Description

technical field

[0001] The invention relates to a keratinase mutant with improved thermostability 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. Although keratinase has great application and research value, the keratinase screened from wild bacteria has poor thermal stability and low substrate specificity, which greatly reduces the development and application of keratinase. The keratinase gene reported so far mainly comes fro...

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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