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Biogeneration of lipophenols by lipases using selected substrate models

McGill University
Publication Date
  • Lipase.
  • Esterification.
  • Lipids In Human Nutrition.
  • Phenols.
  • Food -- Biotechnology.


The objective of the research was to carry out the biogeneration of lipophenols by enzymatic esterification of tricaprylin and caprylic acid with catechin and catechol in a model hexane system. Commercial lipases, including Lipase N from Rhizopus niveus, Lipozyme IM from Mucor miehei and Novozym 435 from Candida antarctica were used throughout this study. The effects of reaction time, incubation temperatures and agitation speeds on enzymatic hydrolytic activity were investigated to determine the optimal conditions for biocatalysis. The optimal temperatures for biocatalysis were determined to be 37.5°C for Lipase N, and 55°C for Lipozyme IM and Novozym 435; the optimum agitation speed was 100 rpm. Using Lipase N, maximum hydrolysis of 1.66 mumol free fatty acids/mL was obtained after 1.5 days of incubation, while with Lipozyme IM, maximum hydrolysis of 8.1 and 8.5 mumol free fatty acids/mL was obtained after 1 and 4 days, respectively. With Novozym 435, the highest hydrolysis of 4.0 and 6.1 mumol free fatty acids/mL were found after 2 and 9 days, respectively.

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