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首页> 外文期刊>Journal of Agricultural and Food Chemistry >PRELIMINARY KINETIC STUDIES ON THE ESTERATIC AND LIPOLYTIC COMPONENTS OF A COMMERCIAL WHEAT GERM LIPASE
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PRELIMINARY KINETIC STUDIES ON THE ESTERATIC AND LIPOLYTIC COMPONENTS OF A COMMERCIAL WHEAT GERM LIPASE

机译：商业小麦胚芽脂肪酶的脂肪和脂肪族成分的初步动力学研究

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摘要

Commercial wheat germ lipase was fractionated by gel filtration and ion-exchange chromatography. The activity of isolated fractions was tested with p-nitrophenyl acetate (PNPA) and dimercapto-propanol (DMP) tributyrate as substrate. Three active components were obtained: an esterase catalyzing only the hydrolysis of PNPA, a lipase catalyzing the hydrolysis of DMP tributyrate and a nonspecific esterase catalyzing the hydrolysis of both PNPA and DMP tributyrate. PNPA hydrolysis by the esterase fraction obeyed Michaelis-Menten kinetics. The nonspecific esterase fraction and the commercial enzyme preparation yielded nonlinear Lineweaver-Burk plots. The commercial preparation yielded a linear Lineweaver-Burk plot with DMP tributyrate as substrate, indicating that nonspecific esterase and lipase components had similar K-m values for the lipid substrate. However, the components had different heat stabilities as evidenced by nonlinear heat inactivation curves.
机译：通过凝胶过滤和离子交换色谱分离市售小麦胚芽脂肪酶。以乙酸对硝基苯酯（PNPA）和二巯基丙醇（DMP）三丁酸甘油酯为底物测试分离的级分的活性。获得了三个活性成分：仅催化PNPA水解的酯酶，催化DMP甘油三酸酯水解的脂肪酶和催化PNPA和DMP甘油三酸酯水解的非特异性酯酶。酯酶馏分水解PNPA符合Michaelis-Menten动力学。非特异性酯酶馏分和商业酶制剂产生非线性Lineweaver-Burk图。该商业制剂产生了以DMP三丁酸酯为底物的线性Lineweaver-Burk图，表明非特异性酯酶和脂肪酶组分对于脂质底物具有相似的K-m值。然而，非线性失活曲线证明了这些组分具有不同的热稳定性。

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