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A mutant that improves the thermal stability of heparanase I based on molecular dynamics analysis of enzyme flexibility and its preparation method

A thermostability and mutant technology, applied in the fields of genetic engineering and protein expression, can solve the problems of heavy workload and achieve the effects of extending shelf life, reducing production costs, and reducing screening workload

Active Publication Date: 2021-03-05
TIANJIN UNIV OF SCI & TECH +1
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Problems solved by technology

The workload of traditional qualitative evolution methods is too large to obtain mutants with good effects in a short period of time

Method used

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  • A mutant that improves the thermal stability of heparanase I based on molecular dynamics analysis of enzyme flexibility and its preparation method
  • A mutant that improves the thermal stability of heparanase I based on molecular dynamics analysis of enzyme flexibility and its preparation method
  • A mutant that improves the thermal stability of heparanase I based on molecular dynamics analysis of enzyme flexibility and its preparation method

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Embodiment Construction

[0038] The present invention will be described in further detail below in conjunction with specific examples. The following examples are only descriptive, not restrictive, and cannot limit the protection scope of the present invention.

[0039] The raw materials used in the present invention, unless otherwise specified, are conventional commercially available products; the methods used in the present invention, unless otherwise specified, are conventional methods in the art.

[0040] A mutant that improves the thermal stability of heparanase I based on molecular dynamics analysis of enzyme flexibility, the mutant is mutant BtHepI Q198R and / or mutant BtHepI K247W , the mutant BtHepI Q198R The amino acid sequence is SEQID NO.1, the mutant BtHepI K247W The amino acid sequence of is SEQ ID NO.2.

[0041] An encoding gene of a mutant that improves the thermostability of heparanase I based on molecular dynamics analysis of enzyme flexibility as described above, the mutant BtHepI ...

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Abstract

The invention relates to a mutant that improves the thermal stability of heparanase I based on molecular dynamics analysis of enzyme flexibility, and the mutant is mutant BtHepI Q198R and / or mutant BtHepI K247W , the mutant BtHepI Q198R The amino acid sequence is SEQ ID NO.1, the mutant BtHepI K247W The amino acid sequence of is SEQ ID NO.2. The mutant of the present invention is a heparanase I mutant strain with excellent thermal stability, which has great potential for industrial application and economic value. Operational stability and batch reuse in catalytic processes, reducing production costs, etc., are of great importance.

Description

technical field [0001] The invention belongs to the technical field of genetic engineering and protein expression, in particular to a mutant capable of improving the thermal stability of heparanase I based on molecular dynamics analysis of enzyme flexibility and a preparation method thereof. Background technique [0002] Heparanase I (GenBank: AAO79780.1) is a kind of polysaccharide lyase that can crack heparin-like structural substances and prepare low-molecular-weight heparin. Bacillus, etc. Heparanase I was first discovered in Flavobacter heparinus (Pedobacter heparinus), which can selectively cleave the α(1-4) glycosidic bond between glucosamine and uronic acid in sulfated heparin glycans. According to the amino acid sequence and protein structure characteristics of various sources of heparanase I, heparanase I is divided into 13 families of glycoside hydrolases PLs. At present, heparinase I is mainly used in the preparation of low-molecular-weight heparin, the elimina...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C12N9/88C12N15/60C12N15/70C12N1/21C12Q1/527C12R1/19
CPCC12N9/88C12N15/70C12Q1/527C12Y402/02007
Inventor 罗学刚张川张同存刘耀天
Owner TIANJIN UNIV OF SCI & TECH
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