Cinnamyl acetate synthesis by lipase-catalyzed transesterification in a solvent-free system

被引:26
|
作者
Geng, Bo [1 ]
Wang, Mengfan [1 ]
Qi, Wei [1 ,2 ,3 ]
Su, Rongxin [1 ,2 ,3 ]
He, Zhimin [1 ,2 ]
机构
[1] Tianjin Univ, Chem Engn Res Ctr, Sch Chem Engn & Technol, Tianjin 300072, Peoples R China
[2] Tianjin Univ, State Key Lab Chem Engn, Tianjin 300072, Peoples R China
[3] Tianjin Univ, Tianjin Key Lab Membrane Sci & Desalinat Technol, Tianjin 300072, Peoples R China
关键词
flavor ester; Novozym; 435; transesterification; solvent-free system; kinetic model; CANDIDA-RUGOSA LIPASE; ISOAMYL ACETATE; IMMOBILIZED-LIPASE; ENZYMATIC-SYNTHESIS; VINYL-ACETATE; ESTERIFICATION; LAURATE; ESTERS; FLAVOR; BUTYRATE;
D O I
10.1002/bab.1023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cinnamyl acetate was synthesized using immobilized lipase through transesterification between ethyl acetate and cinnamyl alcohol. In the solvent-free system, ethyl acetate acted as not only the acyl donor but also as the solvent of cinnamyl alcohol. Conversion (90.06%) was achieved after 3 H when transesterification was carried out at ethyl acetate/cinnamyl alcohol 15:1, 2.67 g L of lipase (Novozym 435) loading, and 40 degrees C. Excellent stability and reusability of the enzyme resulted from the moderate reaction system. Kinetic studies showed that the Michaelis constants for ethyl acetate and cinnamyl alcohol and the inhibition constant of cinnamyl alcohol were 2.241, 206.82, and 0.461 mmol L-1, respectively, which indicated that the reaction complied with the PingPong BiBi mechanism, with the inhibition of cinnamyl alcohol on lipase.
引用
收藏
页码:270 / 275
页数:6
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