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首页> 外文期刊>Biotechnology Progress >Kinetic Resolution of Drug Intermediates Catalyzed by Lipase B from Candida Antarctica Immobilized on Immobead-350
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Kinetic Resolution of Drug Intermediates Catalyzed by Lipase B from Candida Antarctica Immobilized on Immobead-350

机译：通过脂肪酶B催化的药物中间体的动力学分辨率从Candida南极洲固定在Immobead-350上

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Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica (CALB), has been proven to be inadequate for the kinetic resolution of rac-indanyl acetate. As it has been previously described that different immobilization protocols may greatly alter lipase features, in this work, CALB was covalently immobilized on epoxy Immobead-350 (IB-350) and on glyoxyl-agarose to ascertain if better kinetic resolution would result. Afterwards, all CALB biocatalysts were utilized in the hydrolytic resolution of rac-indanyl acetate and rac-(chloromethyl)-2-(o-methoxyphenoxy) ethyl acetate. After optimization of the immobilization protocol on IB-350, its loading capacity was 150 mg protein/g dried support. Furthermore, the CALB-IB-350 thermal and solvent stabilities were higher than that of the soluble enzyme (e.g., by a 14-fold factor at pH 5-70 degrees C and by a 11-fold factor in dioxane 30%-65 degrees C) and that of the glyoxyl-agarose-CALB (e.g., by a 12-fold factor at pH 10-50 degrees C and by a 21-fold factor in dioxane 30%-65 degrees C). The CALB-IB-350 preparation (with 98% immobilization yield and activity versus p-nitrophenyl butyrate of 6.26 +/- 0.2 U/g) was used in the hydrolysis of rac-indanyl acetate using a biocatalyst/substrate ratio of 2:1 and a pH value of 7.0 at 30 degrees C for 24 h. The conversion obtained was 48% and the enantiomeric excess of the product (e.e.(p)) was 97%. These values were much higher than the ones obtained with Novozyme 435, 13% and 26% of conversion and e.e.p, respectively. (C) 2018 American Institute of Chemical Engineers
机译：诺酶435，其是来自Candida南极（CALB）的商业固定化脂肪酶B，已被证明对于乙酸RAC-茚体酰基的动力学分辨率是不充分的。如前所述，不同的固定方案可以大大改变脂肪酶特征，在这项工作中，CALB在环氧免疫树脂-350（IB-350）上并在乙醛酸上共价固定，以确定是否会导致更好的动力学分辨率。然后，所有CALB生物催化剂用于RAC-茚满乙酸乙酯和RAC-（氯甲基）-2-（O-甲氧基苯氧基）乙酸乙酯的水解分辨率。在IB-350上的固定方案优化后，其负载能力为150mg蛋白质/ G干燥载体。此外，CALB-IB-350热量和溶剂稳定性高于可溶性酶的热量和溶剂稳定性（例如，在pH5-70℃下的14倍，并在二恶烷中的11倍因子30％-65度C）和乙醛琼脂糖-CALB（例如，在pH10-50℃下的12倍，二恶烷30％-65℃下的21倍因子）。使用生物催化剂/基材比为2：1，使用CALB-IB-350制备（具有98％的固定产率和6.26 +/- 0.2u / g的对硝基苯丁酸乙酯）的乙酸乙酯水解并且在30摄氏度下为7.0的pH值为24小时。得到的转化率为48％，对映体过量的产物（例如（P））为97％。这些值远高于用诺酶435,13％和26％的转化率和22％获得的值。 （c）2018美国化学工程研究所

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