Engineering School of Lorena, University of São Paulo, P.O. Box 116, Lorena, 12602-810 São Paulo, Brazil.
Appl Biochem Biotechnol. 2010 Feb;160(4):1146-56. doi: 10.1007/s12010-009-8578-z. Epub 2009 Mar 5.
Seven food grade commercially available lipases were immobilized by covalent binding on polysiloxane-polyvinyl alcohol (POS-PVA) hybrid composite and screened to mediate reactions of industrial interest. The synthesis of butyl butyrate and the interesterification of tripalmitin with triolein were chosen as model reactions. The highest esterification activity (240.63 microM/g min) was achieved by Candida rugosa lipase, while the highest interesterification yield (31%, in 72 h) was achieved by lipase from Rhizopus oryzae, with the production of about 15 mM of the triglycerides C(50) and C(52). This lipase also showed a good performance in butyl butyrate synthesis, with an esterification activity of 171.14 microM/g min. The results demonstrated the feasibility of using lipases from C. rugosa for esterification and R. oryzae lipase for both esterification and interesterification reactions.
七种食品级市售脂肪酶通过共价键固定在聚硅氧烷-聚乙烯醇（POS-PVA）杂化复合材料上，并进行筛选以介导工业感兴趣的反应。选择丁酸丁酯的合成和三棕榈酸甘油酯与三油酸甘油酯的酯交换反应作为模型反应。假丝酵母脂肪酶的酯化活性最高（240.63 μM/g min），而米根霉脂肪酶的酯交换产率最高（31%，72 h），产生约 15 mM 的甘油三酯 C（50）和 C（52）。该脂肪酶在丁酸丁酯合成中也表现出良好的性能，酯化活性为 171.14 μM/g min。结果表明，假丝酵母脂肪酶可用于酯化反应，米根霉脂肪酶可用于酯化和酯交换反应。
