Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of Lipase from Trichosporon sp. Y-11and Its Use in Ester Synthesis of Unsaturated Fatty Acids and Alcohols

  • Song, Xin (State Key Laboratory of Microbial Technology, Shandong University) ;
  • Qu, Yinbo (State Key Laboratory of Microbial Technology, Shandong University) ;
  • Shin, Dong-Hoon (Graduate School of Biotechnology, Korea University) ;
  • Kim, Eun-Ki (Department of Biological Engineering, Inha University)
  • Published : 2001.12.01
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Abstract

A 28-kDa extracellular lipase (pI 8.7) was purified to homogeneity from the culture supernatant of Trichosporon sp. Y- 11 by mmonium sulfate precipitation, DEAE-Sephadex A-50, Bio-Gel P-30, CM- Sephadex C-50, and Bio-Gel P- 10 chromatographies. The purified enzyme exhibited a specific activity of $2,741{\;}{\mu}mol/min/mg$ based on the hydrolysis of triolein, and the optimal hydrolysis activity was dentified at pH 8.0 and $40^{\circ}C$. The enzyme activity was inhibited by $Ag^+$ and enhanced by $Fe^{2+}$, $Fe^{3+}$, $Mg^{2+}$, $Mn^{2+}$, and $Li^{+}$. The enzyme activity exhibited for the hydrolysis of both tributyrin and trilinolein. The ester synthesis of unsaturated fatty acids with various alcohols catalyzed by the purified lipase in a nonaqueous medium or microaqueous system was also investigated. The esterification activity of the lipase increased with an increase of the carbon chain length in the alcohol. The synthesis rate of linoleic acid and oleyl alcohol was the highest with an optimal temperature and pH of $40^{\circ}C$ and 8.0, respectively. The water content and agitation also affected the esterification activity of the lipase.

Keywords

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