Collagenase
is a kind of enzymes thatspecificallyhydrolyze natural collagen or
gelatin. In order to prepare a new type of collagen protease and explore its
ability to degrade collagen,a novelbone
specific collagenase (BSC) was obtained fromBacillus cereuscrude enzyme liquid throughthe purification steps of ammonium sulfate
precipitation, DEAE-Sepharose Fast Flow ion exchange chromatography and
Sephadex G-100 gel chromatography. Furthermore, itsmolecular weight of the purified enzyme, substrate specificity and
degradation ability were analyzed. What’s more, we derived the kinetic
model of hydrolyzing bovine bone collagen. The results showed that the specific
activity of BSC was 5.57×103U/mg, the purification times was up to
42.85 times, and its molecular weight was about 52.0 kDa. The specificity analysis
showed that the substrate was a bone collagen enzyme, and its ability to
hydrolyze type I collagen was significant.The comparative test indicated that the hydrolysis
capacity of BSC was higher than that of other proteases.The dynamic model of the
enzymatic degradation of collagen was:the
degradation rate,degree of hydrolysis,Enzyme
inactivation constant K4=64.1157 h-1. Theresults provided a
novel collagenolytic protease for the development of animal bone collagen
industrial.
LIU Li-li et al
. Purifcation of Bacillus cereus MBL13-U collagenase and degradation kinetics of collagen[J]. Food and Fermentation Industries, 2017
, 43(12)
: 13
-19
.
DOI: 10.13995/j.cnki.11-1802/ts.015222