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

Authors
  • Geng, Bo
  • Wang, Mengfan
  • Qi, Wei
  • Su, Rongxin
  • He, Zhimin
Type
Published Article
Journal
Biotechnology and applied biochemistry
Publication Date
Jan 01, 2012
Volume
59
Issue
4
Pages
270–275
Identifiers
DOI: 10.1002/bab.1023
PMID: 23586860
Source
Medline
License
Unknown

Abstract

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°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 Ping-Pong Bi-Bi mechanism, with the inhibition of cinnamyl alcohol on lipase.

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