化学
月桂酸
戊二醛
脂肪酶
酒
溶剂
酶
乙醇
有机化学
动力学
固定化酶
色谱法
脂肪酸
物理
量子力学
作者
Sumbita Gogoi,Swapnali Hazarika,Paruchuri G. Rao,Narendra Nath Dutta
标识
DOI:10.1080/10242420600997495
摘要
In this paper, we report a comprehensive kinetic study on esterification of lauric acid with lauryl alcohol catalysed by commercial porcine pancreatic lipase (PPL) in the form of cross-linked enzyme crystals (CLEC) using glutaraldehyde as the cross linker. The stability of the CLEC was better than the immobilized enzyme for practical applications. Comparative studies using six different solvents having hydrophobicity (log p) values ranging from 0.70 to 3.50 revealed that the esterification reaction was favoured in hydrophobic solvents. The kinetics of the esterification reaction conformed with the so-called Ping-Pong–Bi-Bi mechanism with alcohol inhibition.
科研通智能强力驱动
Strongly Powered by AbleSci AI