• REACTION KINETICS, CATALYSIS AND…… • 上一篇 下一篇
龚盛昭a,b; 程江a; 杨卓如a
GONG Shengzhaoa,b; CHENG Jianga; YANG Zhuorua
摘要: The inhibitory effect of ferulic acid on the diphenolase activity of mushroom tyrosinase and the kinetic behavior were studied with L-3,4-dihydroxyphenylalanine (L-DOPA) as substrate. The inhibitor concentration leading to 50% relative activity lost (IC50) was estimated to be 0.15 mmol·L^-1. The inhibition mechanism obtained from Lineweaver-Burk plots shows that ferulic acid is a competitive inhibitor and the inhibition of tyrosinase by ferulic acid is a reversible reaction. The equilibrium constant for ferulic acid binding with the tyrosinase was determined to be 0.25 mmol·L^-1 for diphenolaase.