Method for improving thermal stability of GH10 xylanase through N-terminal replacement

A xylanase and heat-resistant technology, applied in the field of bioengineering, can solve the problems of difficult thermal stability, poor thermal stability, restricting the application of xylanase, etc., and achieve the effect of improving the optimum temperature and thermal stability
CN102994529AInactive Publication Date: 2013-03-27JIANGNAN UNIV
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Patent Information

Authority / Receiving Office
CN · China
Current Assignee / Owner
JIANGNAN UNIV
Publication Date
2013-03-27
Estimated Expiration
Not applicable · inactive patent

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Abstract

The invention aims at providing a method for thermal stability modification of GH10 xylanase Aus Xyn10A and efficient expression and purification of recombinant mutant enzyme. According to the protein sequence comparison result between Aus Xyn10A (from aspergillus usamii E001) and heat-resistant xylanase (from thermoascus aurantiacus 751K6A), the sequence of the N-terminal area of the heat-resistant enzyme is replaced by a corresponding sequence of Aus Xyn10A by a genetic engineering method. The obtained mutant enzyme is named ATx10AM. The experimental result indicates that the optimal temperature and thermal stability of the enzyme after mutation are obviously improved; and as a heat-resistant enzyme preparation, the xylanase has relatively great industrial production potential and economic value.
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Description

Technical field

[0001] The invention relates to a GH10 xylanase modification and a highly efficient expression method of a mutant enzyme, and belongs to the technical field of biological engineering. Background technique

[0002] Xylanase is a general term for a class of enzymes that can degrade xylan into xylo-oligosaccharides and xylose. In the narrow sense, xylanase specifically refers to β-1,4-xylanase (endo-β-1,4-xylanase, EC 3.2.1.8). β-1,4-endoxylanase can act on the xylosidic bond from the inside of the main chain and is one of the most important enzymes in the degradation of xylan. Most of the cloned xylanases currently belong to the F / 10 and G / 11 families. Compared with the 11th family, the 10th family of xylanase has low substrate specificity, fast hydrolysis rate, and low degree of polymerization of the hydrolysate. Great research and application value. Xylanase has broad application prospects in the fields of papermaking, food, energy, feed and environment, especi...

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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