FA selectivity of lipases in acyl‐transfer reactions with acetate esters of polyols in organic media

• Published in: Journal of the American Oil Chemists' Society
• Main Authors: Lee, Chen‐Hsien, Parkin, Kirk L.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2003
• Subjects: Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1007/s11746-003-0682-4; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1007%2Fs11746-003-0682-4; https://onlinelibrary.wiley.com/doi/full/10.1007/s11746-003-0682-4

Abstract FA reaction selectivity of Burkholderia cepacia, Rhizomucor miehei , and Candida antarctica fraction B lipases was compared between acyl‐transfer and esterification reactions. Multicompetitive reaction mixtures containing a series of n ‐chain FA (a C 4 –C 18 series; and a C 18∶x series, where X=0‐3 double bonds) and a single acetate ester co‐substrate [triacetin, 1,2‐propanediol (1,2‐PD)diacetate, and 1,3‐PD diacetate] were studied in tert ‐butyl methyl ether at an a w of 0.69. For B. cepacia lipase, FA optima for C 8 , C 16 , and C 18∶2 were observed in all reactions with 1.0‐ to 5.9‐fold differences in FA selectivity. For R. miehei lipase, an optimum for C 8 FA was observed in all reactions with 1.2‐ to 6.7‐fold differences in FA selectivity. For C. antarctica lipase, FA optima for C 8 /C 10 were observed in all reactions with 1.0‐ to 2.8‐fold differences in FA selectivity. FA selectivities were broadly modulated upon changing from free polyol to acetate ester co‐substrates for B. cepacia and R miehei lipases, whereas FA selectivity modulations were more specific upon this change in reaction configuration for C. antarctica B lipase. For all lipases, reactivity toward unsaturated C 18∶x FA was enhanced in acyl‐transfer relative to esterification reactions with these polyol co‐substrates.