Martínez Irene, Markovits Alejandro, Chamy Rolando, Markovits Andrés
School of Biochemical Engineering, Catholic University of Valparaíso, Av. Brazil 2147, PO Box 4059, Valparaíso, Chile.
Appl Biochem Biotechnol. 2004 Jan;112(1):55-62. doi: 10.1385/abab:112:1:55.
Eighteen commercial lipase preparations, either immobilized or crude enzyme powders, were screened for the transesterification of wood sterols. The reactions were carried out in a solvent-free system, at the optimum temperature of the enzyme preparations as reported by the manufacturer and at the pressure of 2 mbar, with 5 or 10% in weight of the enzyme relative to the wood sterol content of the reacting mixture. Methyl esters of sunflower fatty acids were used as transesterifying agent. Of all the enzymes assayed, only Lipase TL from Pseudomonas stutzeri PL-836 (Meito Sangyo) exhibited any significant transesterifying capacity, 85 and 95% of conversion after 2 and 8 h of reaction, respectively, when 10% in weight of enzyme was used.
对18种商业脂肪酶制剂（固定化酶或粗酶粉）进行了木质甾醇酯交换反应的筛选。反应在无溶剂体系中进行，温度为制造商报告的酶制剂最佳温度，压力为2毫巴，酶的用量相对于反应混合物中木质甾醇含量为5%或10%（重量）。向日葵脂肪酸甲酯用作酯交换剂。在所有测试的酶中，只有来自施氏假单胞菌PL - 836（日本名东化学工业株式会社）的脂肪酶TL表现出显著的酯交换能力，当使用10%（重量）的酶时，反应2小时和8小时后的转化率分别为85%和95%。
