Screening Of Collagenase-Producing Strain And Purification Of Bacillus Cereus Collagenase Screening Of Collagenase-Producing Strain And Purification Of Bacillus Cereus Collagenase
Keywords
Collagenase,Screening,Purification,Property Collagenase, Screening, Purification, Property
Abstract
We isolated the strain MBL13 with high collagenase productivity from the soil of piled up animal bones.It was identified as Bacillus cereus.We purified and characterized Bacillus cereus collagenase(BCC).The molecular weight of BCC Was 38.0 kDa and the optimum temperature and pH for the enzyme activity were 40¡æ and 8.0 respectively.The enzyme was stable when the temperature was below 50¡æ,but only retained 10%activity when kept at 60¡æ for 1 h.The enzyme activity was stable between pH 7.0-8.5.Some metal ions such as Ca~(2+),Zn~(2+),Mg~(2+) enhanced the enzyme activity, and Cu~(2+) brought the obvious inhibition. In addition, EDTA and EGTA could inhibit the enzyme activity.We suggested that the purified enzyme was a member of the metalloproteases.Based on the experiment of substrate specificity,WC found that the purified enzyme was bone collagenolytic protease,and had a much stronger capacity of hydrolysis fortype ¢ñ collagen than that fortype ¢ò collagen and type ¢ó collagen.By BCC hydrolyzing bone collagen, we obtained polypeptides with different chain lengths.The comparative test indicated that the hydrolysis capacity of BBC was higher than that of standard type ¢ñ collagenase.The results introduced a new swain and a novel collagenolytic protease for industrial enzvme.
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Original research was done by Lili Liu, Meihu M, Xiufang Yu, Wentao Wang, Lili Liu, Ma Meihu, Yu Xiufang, Wang Wentao
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