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Mutant for improving thermal stability of heparinase I by enzyme flexibility analysis based on molecular dynamics and preparation method thereof

A technology of molecular dynamics and thermal stability, which is applied in the fields of genetic engineering and protein expression, can solve problems such as heavy workload, and achieve the effects of extending shelf life, reducing production costs, large industrial application potential and economic value

Active Publication Date: 2019-04-23
TIANJIN UNIVERSITY OF SCIENCE AND TECHNOLOGY +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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  • Mutant for improving thermal stability of heparinase I by enzyme flexibility analysis based on molecular dynamics and preparation method thereof
  • Mutant for improving thermal stability of heparinase I by enzyme flexibility analysis based on molecular dynamics and preparation method thereof
  • Mutant for improving thermal stability of heparinase I by enzyme flexibility analysis based on molecular dynamics and preparation method thereof

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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 for improving the thermal stability of heparinase I by enzyme flexibility analysis based on molecular dynamics, wherein the mutant is a mutant BtHepIQ198R and / or a mutant BtHepIK247W, and the amino acid sequence of the mutant BtHepIQ198R is SEQIDNO. 1, and the amino acid sequence of the mutant BtHepIK247W is SEQIDNO. 2. The mutant of the invention is a heparin enzyme I mutant strain with excellent thermal stability, has larger industrial application potential and economic value, and has important significance for prolonging the shelf period of the heparin enzyme I improveing the operation stability of the heparin enzyme I in a catalytic process and the reusing batches, reducing production cost and the like.

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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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 UNIVERSITY OF SCIENCE AND TECHNOLOGY
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