Chemistry Department, Indian Institute of Technology Delhi, Hauz Khas, New Delhi 110 016, India.
Bioresour Technol. 2010 Apr;101(8):2877-9. doi: 10.1016/j.biortech.2009.09.088. Epub 2009 Oct 23.
An optimally prepared Candida rugosa lipase aggregate cross-linked with bovine serum albumin, was found to overcome acetaldehyde deactivation during transacetylation of a series of benzyl alcohols with vinyl acetate. The formulation, under the same reaction conditions, exhibited 4-30x enhancement in the reaction rate as compared to the celite immobilized lyophilized formulation and 25-133x enhancement as compared to the free lyophilized enzyme depending upon the alcohol chosen. The racemic 1-phenylethanol, taken as one of the alcohols, underwent a more efficient enantioselective transacetylation giving 80% enantiomeric excess of the product, (R)-1-phenylethyl acetate, at 38% conversion (E = 15) within 24h while the enzyme immobilized on celite gave 83% enantiomeric excess at 18% conversion (E = 13) during the same period of time.
经优化处理的 Candida rugosa 脂肪酶与牛血清白蛋白交联形成的聚集体，在一系列苄醇与醋酸乙烯酯的转酯化反应中，可克服乙醛的失活。与 Celite 固定化冻干制剂相比，在相同的反应条件下，该制剂的反应速率提高了 4-30 倍；与游离冻干酶相比，根据所选醇的不同，反应速率提高了 25-133 倍。作为醇之一的外消旋 1-苯乙醇，经过更有效的对映选择性转酯化反应，在 24 小时内转化率为 38%时，产物（R）-1-苯乙醇乙酸酯的对映体过量值达到 80%（E = 15），而 Celite 固定化的酶在相同时间内转化率为 18%时，对映体过量值达到 83%（E = 13）。
