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Mutant chitosanase with high temperature stability

A chitosanase and stability technology, applied in the field of mutant chitosanase, can solve problems such as temperature stability to be improved, achieve good application prospects, improve temperature stability, and improve temperature stability

Pending Publication Date: 2022-07-15
CHANGZHOU UNIV
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  • Abstract
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Problems solved by technology

However, there are few reports on the molecular modification of chitosanase enzymes of the Streptomyces avermitilis GH46 family. In the early stage of this study, a new chitosanase SaCsn46A was cloned by PCR technology. It was found that the enzyme has a wide range of Substrate spectrum, but temperature stability needs to be improved

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  • Mutant chitosanase with high temperature stability
  • Mutant chitosanase with high temperature stability
  • Mutant chitosanase with high temperature stability

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Embodiment Construction

[0020] The present invention is not limited to the following specific embodiments. Those skilled in the art can use other various specific embodiments to implement the present invention according to the content disclosed in the present invention, or use the design structure and thinking of the present invention, and make simple changes or Modifications fall within the protection scope of the present invention. It should be noted that the embodiments of the present invention and the features of the embodiments may be combined with each other under the condition of no conflict.

[0021] The present invention is described in further detail below in conjunction with embodiment:

[0022] 1. Confirmation of chitosanase mutation sites

[0023] The three-dimensional structure of chitosanase SaCsn46A was simulated by Swiss-Model using Streptomyces sp. N174 chitosanase (1CHK_A) as template, and the spatial structure of chitosanase SaCsn46A was obtained, which was calculated by PoPMuSiC...

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Abstract

The invention relates to gene cloning, site-specific mutagenesis and gene recombination technologies, and particularly discloses a novel mutant of a 46 family glycoside hydrolase chitosanase (SaCsn46A) cloned from streptomyces avermitilis, and the enzyme is composed of 271 amino acids which comprise 34 amino acid signal peptides. By analyzing a high-unfolding free energy site on a zymoprotein structure, a mutation site is selected for mutation, and a chitosanase mutant with improved temperature stability is screened out. According to the invention, glycine at the 237th position of an original enzyme SaCsn46A is mutated into alanine (G237A), and the mutant is expressed in escherichia coli Rosetta. Compared with the wild chitosanase, the temperature stability of the mutant enzyme is 4.8 times higher than that of the wild chitosanase. A thin-layer chromatographic analysis result shows that enzyme hydrolysates are mainly glucosamine GlcN and (GlcN) 2.

Description

technical field [0001] The invention relates to gene cloning, site-directed mutagenesis and gene recombination technology, and is specifically expressed as a mutant chitosanase with high temperature stability. Background technique [0002] Chitosan is a polysaccharide linked by glucosamine (GlcN) through β-1,4-glycosidic bonds. Chitosan is the product of deacetylation of chitin, widely present in the shell and cartilage of lower plant fungi, algae cells, shellfish, mollusks (such as salmon, squid), and is second only to cellulose on earth. The second largest natural polymer compound is a renewable biological resource. [0003] Some research reports show that chitosan has superior functions and excellent biological activities such as antibacterial, anti-tumor, and immunity enhancement. Therefore, it has a wide range of application prospects in the fields of food, medicine, agriculture and cosmetics. However, some research reports point out that many functional properties of...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C12N9/42C12N15/56C12N15/70C12N1/21C12P19/00C12P19/02C12P19/04C12P19/12C12P19/14C12R1/19
CPCC12N9/2442C12N15/70C12P19/02C12P19/00C12P19/12C12P19/14C12P19/04
Inventor 郭静高文君潘文鑫满在伟蔡志强
Owner CHANGZHOU UNIV
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