Whole-Cell Biocatalytic Synthesis of Cinnamyl Acetate with a Novel Esterase from the DNA Library of Acinetobacter hemolyticus

J Agric Food Chem. 2017 Mar 15;65(10):2120-2128. doi: 10.1021/acs.jafc.6b05799. Epub 2017 Feb 28.


Cinnamyl acetate has a wide application in the flavor and fragrance industry because of its sweet, balsamic, and floral odor. Up to now, lipases have been mainly used in enzyme-mediated synthesis of cinnamyl acetate, whereas esterases are used in only a few cases. Moreover, the use of purified enzymes is often a disadvantage, which leads to increases of the production costs. In this paper, a genomic DNA library of Acinetobacter hemolyticus was constructed, and a novel esterase (EstK1) was identified. After expression in Escherichia coli, the whole-cell catalyst of EstK1 displayed high transesterification activity to produce cinnamyl acetate in nonaqueous systems. Furthermore, under optimal conditions (vinyl acetate as acyl donor, isooctane as solvent, molar ratio 1:4, temperature 40 °C), the conversion ratio of cinnamyl alcohol could be up to 94.1% at 1 h, and it reached an even higher level (97.1%) at 2 h.

Keywords: acetic esters; cinnamyl acetate; esterase; genomic DNA library; transesterification; whole-cell biocatalyst.

MeSH terms

  • Acinetobacter / enzymology*
  • Acinetobacter / genetics
  • Acinetobacter / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Biocatalysis
  • Cinnamates / metabolism*
  • Esterases / chemistry
  • Esterases / genetics*
  • Esterases / metabolism*
  • Gene Library
  • Hydrogen-Ion Concentration
  • Kinetics
  • Substrate Specificity
  • Temperature


  • Bacterial Proteins
  • Cinnamates
  • Esterases
  • cinnamyl acetate