Characterization of Serratia nematodiphila YM48 Lipase as a Biocatalyst in Fatty Acid Methyl Esters Production

Patcha BOONMAHOME, Pirom SUWANNASOM, Rattanaporn LEESING, Chalerm RUANGVIRIYACHAI, Wiyada MONGKOLTHANARUK

Abstract


Lipases are biocatalysts which have been used in transesterification for biodiesel production. The identification of a new lipase, Serratia nematodiphila YM48, necessitates exploration for its suitability in optimizing biodiesel production. Serratia nematodiphila YM48 is an obtained lipase gene similar to Serratia marcescens lipase. The properties of YM48 lipase included an optimal temperature and a pH of 40 °C and 8, respectively. The enzyme had increased stability compared with native enzyme when lyophilized with polyethylene glycol or α-cyclodextrin, and also when immobilized onto silica gel. It retained > 50 % activity after incubation at 40 °C, pH 8, for 48 h. Both lyophilized and immobilized lipase catalyzed reaction between palm oil and methanol (1: 6 molar ratio), resulting in an 84 - 88 % yield of fatty acid methyl esters (FAMEs). The approach of whole-cell culture immobilization resulted in the greatest amounts of FAME production, particularly fatty acids of methyl oleate, methyl linoleate, and methyl palmitate, and so has the potential for high quality biodiesel production.


Keywords


Immobilization, lipase, lyophilization, Serratia nematodiphila

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