The prufication and kinetics of wheat germ lipase
1989
Fadiloglu, S.
The commercial wheat germ lipase was purified by the methods of gel filtration and ion-exchange chromatography. The activity of isolated fractions was tested with p-nitrophenyl acetate and dimercaptopropanol tributyrate, as substrate. Three active enzymes were obtained. A lipase catalyzes the hydrolysis of both p-nitrophenyl acetate and dimercaptopropanol-tributyrate, a tributyrinase catalyzes the hydrolysis of dimercaptoprapanol-tributyrinase catalyzes the hydrolysis of p-nitrophenyl acetate, only. The hydrolysis of p-nitrophenyl acetate by commercial enzyme gives a nonlinear Lineweaver-Burk plot whereas a linear plot was obtained with DMP-tributyrate. However heat inactivation with DMP-tributyrate as substrate was nonlinear. p-Nitrophenyl acetate hydrolysis by isolated esterase fraction obeys Michealis-Menten kinetics. With lipase fraction, the hydrolysis of p-nitrophenyl acetate deviates from Michaelis-Menten kinetics
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