Isolation, Purification And Degradation Kinetics Analysis Of Bacillus Cereus Mbl13-U Collagenase
Keywords
Collagen, Purification, Collagenase, Kinetics, Degradation
Abstract
Abstract Collagenase is an enzyme that specifically hydrolyzes natural collagen or gelatin. In order to prepare a new type of collagenase and explore its ability to degrade collagen, separation and purification steps such as ammonium sulfate fractionated precipitation, DEAE-Sepharose Fast Flow ion exchange chromatography, and Sephadex G-100 gel chromatography were used to purify Bacillus cereusMBL13- A collagenase (Bone-specific collagenase, BSC) that specifically degrades bovine bone collagen was isolated and purified from the crude enzyme solution of strain U, and the molecular weight, substrate specificity and degradation ability of the enzyme were analyzed, and A kinetic model of bovine collagen degradation was constructed. The results showed that the specific activity of the isolated and purified BSC was 5.57¡Á103U/mg, the purification factor reached 42.85 times, and the molecular weight was approximately 52.0 kDa. After specific analysis, the enzyme is collagenase and has significant ability to hydrolyze type I collagen. Its hydrolysis ability is superior to other commonly used proteases. The kinetic model of bovine collagen degradation by this enzyme was constructed as follows: the degradation rate and the inactivation constant K4 of the hydrolytic enzyme are 64.1157 h-1. This study provides a new protease source for the development of livestock and poultry bone collagen.
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Original research was done by 10.13995/j.cnki.11-1802/ts.015222
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