2018 Volume 24 Issue 4 Pages 669-676
This study aimed to characterize the crude enzyme from Hericium erinaceum (H. erinaceum) as a substitute source of rennet and assess its proteolytic behavior on bovine caseins. The crude enzyme from H. erinaceum was active in the pH range from 3.7 to 6.5 and was inactivated completely by heating at 45 °C for 15 min. The use of specific inhibitors revealed that the crude enzyme from H. erinaceum contains an aspartic protease with an optimum temperature of 30–35 °C. The addition of CaCl2 enhanced the milk-clotting activity of the enzyme. A comparison of SDS-PAGE and kinetic properties of the crude enzyme from H. erinaceum with chymosin on bovine caseins showed that αs- and β-caseins were preferentially degraded relative to κ-casein.
The results indicate that crude enzyme from H. erinaceum can be used as an effective coagulant in cheesemaking.
