INFLUENCE OF THE HYDROPHOBICITY OF LIPASE ISOENZYMES FROM CANDIDA-RUGOSA ON ITS HYDROLYTIC ACTIVITY IN REVERSE MICELLES
INFLUENCE OF THE HYDROPHOBICITY OF LIPASE ISOENZYMES FROM CANDIDA-RUGOSA ON ITS HYDROLYTIC ACTIVITY IN REVERSE MICELLES
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DOI：
10.1016/0014-5793(95)00104-h
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发表时间：
1995-02-27
期刊：
影响因子：
3.5
通讯作者：
ROBLEDO, L
中科院分区：
文献类型：
--
作者：
OTERO, C;RUA, ML;ROBLEDO, L
皱褶假丝酵母脂肪酶的两种同工酶，具有相同的分子量，大小和相似的氨基酸序列，仅仅在AOT的反胶束中研究。结果表明，脂肪酶的疏水性与反胶束体系中的反应有关，这是减轻荷电胶束抑制作用的关键因素，疏水性越强的脂肪酶A在反胶束体系中对水解过程的催化作用越好，其α-螺旋含量从反胶束体系中总结构的31%增加到49%。荧光研究表明，对于更疏水的异脂肪酶A来说，更非极性的环境。在AOT体系中，该酶的发射光谱发生蓝移，在各酶活性最高的ω（0）值处，Trp的发射强度下降，最佳ω（0）值存在酶和底物依赖性，异脂肪酶A和B与胶束体系的不同相互作用产生与其稳定性相反的ω（0）依赖性。更疏水的脂肪酶A在更大的液滴尺寸下具有更高的稳定性。
Two isoenzymes of Candida rugosa lipase, having the same mol.wt., size and similar aminoacid sequence, mere studied in reverse micelles of AOT. The results demonstrated the relevance of lipase hydrophobicity in reactions in anionic micelles, This is a key factor in mitigating the inhibition effect of charged micelles, The more hydrophobic isolipase A was a better biocatalyst for hydrolytic processes in these systems, Its alpha-helix content increased from 31% to 49% of the total structure in reverse micelles. A fluorescence study indicated a more apolar environment for the more hydrophobic isolipase A. Emission spectra of this isolipase in the AOT systems were blue shifted, At omega(0) values where each isolipase presented its maximum activity, a decrease of the emission intensity of Trp was found. An enzyme and substrate dependence of optimal omega(0) is reported, The different interaction of isolipases A and B with the micellar system produced an opposite omega(0) dependence to their stabilities. The more hydrophobic lipase A had higher stability at higher droplet sizes.