Functional Gene Analysis And Structure Prediction Of Bacillus Cereus Collagenase
Keywords
Bacillus Cereus Mbl13-U, Collagenase, Cloning And Expression, Structure Prediction
Abstract
Abstract Taking Bacillus cereus MBL13-U, a strain of bone collagen-degrading bacteria, as the starting strain, the positioning and structure prediction of the collagenase functional gene were carried out through sequencing of the whole genome of the bacteria. The results show that the length of the functional gene sequence of collagenase obtained from the whole genome sequence is 2 916 bp; in this functional gene, ¦Á-helices account for 37.1% of the total amino acids, ¦Â-turns account for 12.8%, and random coils account for 26.0%, and the enzyme The three-dimensional structure of is predicted to be a tweezer-like structure. The collagenase gene was transferred into the Escherichia coli host strain BL21 to construct the engineering strain pET30a-ColM13/BL21. Analysis of the structure of type I collagen produced by the recombinant protease ColM13 produced by the engineered bacteria showed that the enzymatic hydrolysis of the collagen produced polypeptides and a large number of free amino acids, and its microstructure changed significantly, indicating that ColM13 has been used in the engineered bacteria. successful expression
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Original research was done by Dai Xiaoning, Meng Yuanyuan, Hao Weiming, Chen Ke, Liu Lili
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