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《Guangxi Sciences》 2007-04
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The Extraction of Peroxidase from Momordica charantia and Its Property

LIU Jin-lei1,SU Tao2,LI Dian-peng1,LU Feng-lai1(1.Guangxi Institute of Botany,Guilin,Guangxi,541006,China;2.Guilin Yibai Lijiang Pharmaceutical Co.Ltd,Guilin,Guangxi,541006,China)  
Peroxidase was separated and purified from Momordica charantia.Its optimum pH value,optimum temperature,thermal stability and effect of substrate concentration on enzyme activity were determined.The results were showed as follows:With O-phenylenediamine as substrate,λmax=425nm,Km=4.6×103,Vmax=0.137unit/s,optimum pH value 4.6,optimum temperature at 50℃ with high enzyme activity.The inactivation rate of POD raised over 60℃,and the enzyme activity was almost lost above 70℃.Vitamin C and Cysteine had great inhabitation effect on POD activity,the inhibition rate reached 94%and 92% respectively.Al3+ was weaker,with inhibition rate of 69%.EDTA had no significant effect of inhibition,the inhibition rate was only 13%.
【CateGory Index】: Q946
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