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Lipase‐catalyzed synthesis of kojic acid esters in organic solvents
Author(s) -
Liu KuanJu,
Shaw JeiFu
Publication year - 1998
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/s11746-998-0086-8
Subject(s) - kojic acid , lipase , chemistry , lauric acid , organic chemistry , penicillium , pseudomonas , biocatalysis , triacylglycerol lipase , oleic acid , tyrosinase , catalysis , fatty acid , enzyme , biochemistry , food science , bacteria , biology , ionic liquid , genetics
Kojic acid is an inhibitor of bacteria, viruses, and fungi. It is used for inhibiting the browning effect of tyrosinase in the food and cosmetic industries. To improve its lipophilic properties, Pseudomonas cepacia lipase and Penicillium camembertii lipase were used for catalyzing the esterification of kojic acid to synthesize kojic acid monolaurate and kojic acid monooleate. These products showed a 69.5% inhibitory effect on tyrosinase in hydrophobic organic solvent. The yields of kojic acid esters were affected by enzymes, substrates, organic solvent, and temperature. Lauric and oleic acids were the best substrates for esterification among various fatty acids tested. CaCl 2 and MnCl 2 stimulate Pseudomonas cepacia lipasecatalyzed esterification by 7.0%. On the contrary, MgCl 2 , SrCl 2 , and ZnCl 2 inhibited the reaction. The best pH of buffer for lipase pretreatment was pH 6.0. Pseudomonas and Penicillium lipases can be reused for the synthesis of kojic acid esters. After reaction at 40°C for 10 d, the Penicillium and Pseudomonas lipases still retained 57.0% and 92.0% of their initial activities, respectively.