Screening Of Collagenase-Producing Bacteria And Isolation And Purification Of Enzymes
Keywords
Collagenase, Screening, Purification, Properties
Abstract
The mbl13 strain with high collagenase production was screened from soil samples of accumulated bones and identified as Bacillus cereus. The collagenase bcc produced was isolated and purified, and the enzymatic properties were studied. The enzyme with a molecular weight of approximately 38.0 kdabcc was purified from the fermentation broth of the strain. The optimal temperature for the enzyme reaction is 40¡ãC, and the optimal pH is 8.0. Stable below 50¡æ, only 10% of the enzyme activity is retained after being incubated at 60¡æ for 1 hour; the activity is relatively stable at pH 7.0~8.5; metal ions ca2+, zn2+, mg2+ have an activating effect on the enzyme, and the metal ion cu2+ has a significant inhibitory effect on the enzyme . Edta and egta can inhibit this enzyme, indicating that bcc enzyme is a metalloprotease. The substrate specificity of the enzyme indicates that the enzyme is collagenase, and its ability to hydrolyze type ¢¡ collagen is significantly higher than that of type ¢¢ collagen and type ¢£ collagen. Applying the purified bcc enzyme to the hydrolysis of bone collagen can obtain polypeptides of different chain lengths, and its hydrolysis ability is higher than the standard collagenase type I. This study provides new strains and new collagenases for industrial enzymes, and provides an important theoretical basis for the development of collagenases.
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Original research was done by Liu Lili, Ma Meihu, Yu Xiufang, Wang Wentao
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