Takahashi K, Yoshimoto T, Tamaura Y, Saito Y, Inada Y
Biochem Int. 1985 Apr;10(4):627-31.
The lipoprotein lipase from Pseudomonas fluorescens was modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine. The modified lipase in which 55% of the amino groups in the enzyme molecule were coupled with polyethylene glycol was found to be soluble in benzene and catalyzed the reactions of ester synthesis, ester exchange, aminolysis and ester hydrolysis in benzene. The modified lipase had an extraordinary temperature-dependency: enzymic activity for methyl laurate synthesis from methyl alcohol and lauric acid increased with decreasing temperature and attained the maximum at the extremely low temperature of -3 degrees C. The optimum temperature for hydrolysis of methyl laurate was as low as -4 degrees C.
用2,4-双（O-甲氧基聚乙二醇）-6-氯-s-三嗪对荧光假单胞菌的脂蛋白脂肪酶进行修饰。发现酶分子中55%的氨基与聚乙二醇偶联的修饰脂肪酶可溶于苯，并能催化苯中的酯合成、酯交换、氨解和酯水解反应。修饰脂肪酶具有非凡的温度依赖性：由甲醇和月桂酸合成月桂酸甲酯的酶活性随温度降低而增加，并在极低的-3℃达到最大值。月桂酸甲酯水解的最适温度低至-4℃。
