Immobilization of lipases by selective adsorption on hydrophobic supports

化学 吸附 脂肪酶 疏水效应 水解 酯酶 固定化酶 水溶液 有机化学 区域选择性 组合化学 催化作用
作者
Roberto Fernández‐Lafuente,Pilar Armisén,Pilar Sabuquillo,Gloria Fernández‐Lorente,José M. Guisán
出处
期刊:Chemistry and Physics of Lipids [Elsevier BV]
卷期号:93 (1-2): 185-197 被引量:448
标识
DOI:10.1016/s0009-3084(98)00042-5
摘要

The preparation of immobilized derivatives of lipases that may be useful to develop industrial processes of organic synthesis is an exciting field of research in which three main features have to be simultaneously considered: (a) immobilized derivatives have to be compatible with very different reaction requirements (e.g. continuos adjustment of pH with concentrated alkali, use of aqueous media or organic solvents, etc.); (b) Sometimes, some activity/stability properties of lipases should be improved during immobilization; and (c) because of a complex mechanism of action, lipases are poorly active in the absence of hydrophobic interfaces. In this paper, we will review different approaches for lipase immobilization mainly related to the further use of immobilized derivatives to carry out enantio and regioselective hydrolysis in high water-activity systems. Special emphasis is paid to the selective adsorption of lipases on tailor-made strongly hydrophobic support surfaces. This new immobilization procedure is based on the assumption that the large hydrophobic area that surrounds the active site of lipases is the one mainly involved in their adsorption on strongly hydrophobic solid surfaces. Thus, lipases recognize these surfaces similarly to those of their natural substrates and they suffer interfacial activation during immobilization. This immobilization method permits: (a) promote a dramatic hyper-activation of most of lipases after their immobilization. That is, adsorbed lipases show very enhanced esterase activity in the absence of additional hydrophobic interfaces; (b) promote highly selective adsorption of lipases, at very low ionic strength, from impure protein extracts. That is, we can associate immobilization and purification of lipases; (c) promote interesting improvements of enantioselectivity after immobilization; and (d) promote a strong but reversible immobilization that enables us to recover these expensive supports after inactivation of immobilized lipases.

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