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首页> 外文期刊>Bioprocess and Biosystems Engineering >Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate
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Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate

机译：通过共价固定化对Eco-Indancatic乙酸酶酶促分辨率的共价固定性对念珠菌抗野生菌特性的调节

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摘要

In this study, the modulation of enzymatic biocatalysts were developed by the use of lipase B fromCandida antarcticacovalently immobilized on an eco-friendly support, cashew apple bagasse, activated with 10% glycidol-ethylenediamine-glutaraldehyde (GEG) under different immobilization strategies (5 mM or 100 mM ionic strength and in absence or presence of 0.5% (v/v) Triton X-100). The biocatalysts were characterized for thermal and organic solvents stabilities and compared with the soluble enzyme. The biocatalysts were then applied to the hydrolysis of therac-indanyl acetate (2:1 ratio enzyme/substrate) at pH 7.0 and 30 degrees C for 24 h. For all the strategies evaluated, GEG promoted kinetic resolution ofrac-indanyl acetate with maximum conversion (50%) and led to (R)-indanol with excellent enantiomeric excess (97%), maintaining the maximum conversion for five consecutive cycles of hydrolysis. Therefore, the use of cashew apple bagasse has proved to be a promising eco-friendly support for enzyme immobilization, since it resulted in stable biocatalysts for enzymatic kinetic resolution. Graphic abstract
机译：在这项研究中，通过使用脂肪酶B从Candida抗野生动物的脂肪酶B.在Eco友好的支持下，用10％甘烷 - 乙二胺 - 戊二醛（GEG）在不同的固定策略下激活（5 mm或100mM离子强度，并且在不存在或存在下为0.5％（v / v）triton x-100）。生物催化剂的特征是热和有机溶剂稳定性，与可溶性酶相比。然后将生物催化剂施加到pH7.0和30℃下的Therac-茚（2：1比酶/底物）的水解24小时。对于所评估的所有策略，GEG促进了具有最大转化率（50％）的Rac-茚烷基乙酸酯的动力学分辨率，并导致（R） - 吲哚，具有优异的对映体过量（97％），保持最大转化5个连续的水解循环。因此，已证明使用腰果苹果Bagasse是对酶固定化的有希望的环保支持，因为它导致酶促催化剂稳定的生物催化剂。图形摘要

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