Analysis Of Enzymatic And Structural Properties Of Recombinant Collagenase Bacillus Cereus Colm13
Keywords
Engineering Bacteria Pet30A-Colm13/Bl21, Recombinant Collagenase Colm13, Collagen, Enzymology, Structural Properties
Abstract
Abstract Taking pET30a-ColM13/BL21, an engineered strain that degrades collagen that was successfully constructed in the early stage, as the starting strain, the enzymatic properties of the recombinant collagenase (ColM13) expressed and purified by the engineered strain were analyzed. By studying the effects of temperature, pH, and inhibitors, it was concluded that the optimal reaction temperature of ColM13 is 50 ¡æ, and the optimal reaction pH is 8.0; it has good stability in the range of 20 to 55 ¡æ and pH 6.0 to 9.0 ; The metalloproteinase inhibitors ethylenediaminetetraacetic acid (EDTA) and ethylenebis(oxyethylenenitrilo tetraacetic acid, EGTA) have significant inhibitory effects on ColM13. Using UV Use ultraviolet and visible spectrum (UV), differential scanning calorimeter (DSC), fluorescence spectrum (FS), and Fourier transform infrared spectroscopy (FT-IR) to structure the collagen and its enzymatic hydrolysis products. Characteristic analysis shows that enzymatic hydrolysis destroys the triple helical structure of collagen and releases a large amount of free amino acids. After enzymatic hydrolysis, the mutual repulsion of the peptide chains of collagen is weakened, and the effect of hydrophobic amino acid residues is enhanced, resulting in higher Thermal stability. Compared with collagenase (BSC) isolated and purified from B. cereus MBL13-U, the degradation effect of ColM13-treated collagen is more obvious
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Original research was done by 10.13995/j.cnki.11-1802/ts.016065
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