Colletotrichum gloeosporioides lipase: Characterization and use in hydrolysis and esterifications

  • Denise S
  • Livia T
  • Jamil S
  • et al.
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Colletotrichum gloeosporioides was evaluated for its capacity to produce extracellular lipase. A crude enzyme preparation obtained after 48 h of fermentation reached 742 U/L of lipolytic activity. Estimated molecular weight of proteins responsible for this activity was about 18 kDa as determined by SDS-PAGE and zymogram analysis. Enzyme preparation showed optimum pH at 10 and stability at optimum temperature (37°C) for 5 h. It showed tolerance to a wide range of salts (NH 4 + , Mg +2 , Ca +2 , Mn +2 and Sn +2) and to some solvents (methanol, ethanol, isopropanol, 1-butanol, acetonitrile n-heptane and n-hexane) in different concentrations. The crude enzyme preparation was applied in hydrolysis reactions on different substrates (waste cooking soybean oil, cocoa butter and palm kernel oil) reaching high yields (87.6; 80.1; 74.9%, respectively). The preparation was lyophilized and it was applied in the synthesis of pineapple flavor, by esterification with butanol and butyric acid. C. gloeosporioides lipolytic enzymes synthesized butyl butyrate with 70% yield, in experiments carried out for 24 h using 1:1 acid/alcohol molar ratio in n-heptane medium. The lyophilized preparation was also able to perform transesterification of alcohols and p-nitrophenyl palmitate in organic medium (n-hexane), showing better activity when propanol was used (5.4.10-3 U/kg.min). This study pointed the potential of alkaline lipolytic enzyme produced by C. gloeosporioides in biotechnological industry.




Denise, S., Livia, T. A. S., Jamil, S. O., Marcelo, M. S., Inayara, C. A. L., Gecernir, C., & Jacqueline, A. T. (2015). Colletotrichum gloeosporioides lipase: Characterization and use in hydrolysis and esterifications. African Journal of Microbiology Research, 9(19), 1322–1330.

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