Chahinian H, Nini L, Boitard E, Dubès J P, Sarda L, Comeau L C
Laboratoire de Chimie Biologique Appliquée, Faculté des Sciences et Techniques, St-Jérôme, Marseille, France.
Lipids. 2000 Aug;35(8):919-25. doi: 10.1007/s11745-000-0601-3.
Penicillium cyclopium produces two lipases with different substrate specificities. Lipase I is predominantly active on triacylglycerols whereas lipase II hydrolyzes mono- and diacylglycerols but not triacylglycerols. In this study, we compared the kinetic properties of P. cyclopium lipases and human pancreatic lipase, a classical triacylglycerol lipase, by using vinyl esters as substrates. Results indicate that P. cyclopium lipases I and II and human pancreatic lipase hydrolyze solutions of vinyl propionate or vinyl butyrate at high relative rates compared with emulsions of the same esters, although, in all cases, maximal activity is reached in the presence of emulsified particles, at substrate concentrations above the solubility limit. It appears that partially water-soluble short-chain vinyl esters are suitable substrates for comparing the activity of lipolytic enzymes of different origin and specificity toward esters in solution and in emulsion.
环孢青霉产生两种具有不同底物特异性的脂肪酶。脂肪酶I主要对三酰甘油具有活性，而脂肪酶II水解单酰甘油和二酰甘油，但不水解三酰甘油。在本研究中，我们通过使用乙烯基酯作为底物，比较了环孢青霉脂肪酶与人胰腺脂肪酶（一种经典的三酰甘油脂肪酶）的动力学性质。结果表明，与相同酯类的乳液相比，环孢青霉脂肪酶I和II以及人胰腺脂肪酶以较高的相对速率水解丙酸乙烯酯或丁酸乙烯酯溶液，不过，在所有情况下，在底物浓度高于溶解度极限且存在乳化颗粒时达到最大活性。看来部分水溶性的短链乙烯基酯是比较不同来源和对溶液及乳液中酯类特异性的脂肪分解酶活性的合适底物。
