| Issue |
Korean Journal of Chemical Engineering,
Vol.28, No.1, 203-208, 2011
Vol.28, No.1, 203-208, 2011
Purification and properties of a milk-clotting enzyme produced by Bacillus amyloliquefaciens D4
The milk-clotting enzyme from Bacillus amyloliquefaciens D4 was purified to 17.2-fold with 20% recovery by precipitation in ammonium sulfate and ion-exchange chromatography. The molecular mass of the enzyme was 58.2 kDa as determined by SDS-PAGE, and it was proved to be a metalloprotease by EDTA inhibition. The enzyme was active in the pH range 5.5-7.0 and was inactivated completely by heating at 55 ℃ for 20 min. The highest level of enzyme activity was obtained at 65 ℃, pH 5.5, in the presence of 25mM CaCl2. The milk-clotting activity was inhibited only slightly by Na+ and K+ and significantly by Cu2+, Zn2+ and Sn2+. The Km value of this enzyme was 0.471 mg/mL. The high level of milk-clotting activity coupled with a low level of thermal stability suggested that the milk-clotting enzyme from B. amyloliquefaciens D4 should be considered as a potential substitute for calf rennet.
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