Novel lysyl endopeptidase and preparation method thereof

A specific, lysine-based technology, applied in the field of genetic engineering, can solve the problems of no obvious increase in yield, only reaching the μg level, and low expression level
CN109439643AActive Publication Date: 2019-03-08ZHUHAI JINBAIKANG BIOLOGICAL TECH CO LTD
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Patent Information

Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
ZHUHAI JINBAIKANG BIOLOGICAL TECH CO LTD
Publication Date
2019-03-08

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Abstract

The invention discloses novel lysyl endopeptidase. An enzyme core peptide is connected with histidine tags through an appropriate flexible linker peptide, so that nanogram residual enzyme in a samplecan be detected by an ELISA (enzyme-linked immunosorbent assay) method; and total activity of wild lysyl endopeptidase is ensured. At the same time, the invention further provides a preparation methodof the lysyl endopeptidase. Compared with a gene engineering modification and fermentation technology, the preparation method has the benefit of high yield; a recovery amount of 857mg novel lysyl endopeptidase can be obtained after purification of 1L fermentation liquid; and the method has an industrial potential.
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Description

technical field

[0001] The invention relates to the field of genetic engineering, in particular to a novel lysine-specific endonuclease and a preparation method thereof. Background technique

[0002] Lysyl endopeptidase (Lysyl endopeptidase, EC 3.4.21.50) is also known as lysyl endopeptidase, Achromobacter protease I, lysine endopeptidase, lysyl endopeptidase, lysine Acid C-terminal endonuclease, Lys-C endonuclease, is a serine protease originally discovered and isolated from soil bacteria by Masaki et al. Lysine-specific endonuclease is highly specific and can specifically cleave the peptide bond at the carboxy-terminal of lysine residues and S-aminoethylcysteine ​​residues in the peptide chain.

[0003] Lysine-specific endonuclease also has the following notable features: 1) 10 times higher activity than bovine trypsin; 2) wide pH tolerance (pH8.5-10.5); 3) stronger surface activity 4) It has higher substrate specificity than trypsin, which can recognize and cut lysine a...

Claims

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