Fatty acid specificity of T1 lipase and its potential in acylglycerol synthesis.

ABSTRACT

BACKGROUND: T1 lipase has received considerable attention due to its thermostability. Fatty acid specificity of T1 lipase (crude and purified) was investigated, and its potential in the synthesis of acylglycerols was also evaluated. RESULTS: Fatty acid specificity of T1 lipase (crude and purified) was investigated in the esterification of fatty acids (C60 to C183), suggesting that crude and purified T1 lipase had the lowest preference for C180 [specificity constant (1/α) = 0.08] followed by C181 (1/α = 0.12) and showed the highest preference for C80 (1/α = 1). A structural model was constructed to briefly explore interactions between the lipase and its substrate. Furthermore, crude T1 lipase-catalysed synthesis of diacylglycerols (DAGs) and monoacylglycerols (MAGs) by esterification of glycerol with C181 was studied for evaluating its potential in acylglycerols synthesis. The optimal conditions were glycerol/oleic acid molar ratio 51, the lipase concentration 9.7 U g(-1) of substrates, water content 50 g kg(-1) of substrates and temperature 50 °C, which yielded 42.25% DAGs, 26.34% MAGs and 9.18% triacylglycerols at 2 h. CONCLUSION: DAGs and MAGs were synthesised in good yields although C181 (a much poorer substrate) was used. Our work demonstrates that T1 lipase, which was discovered to show 1,3-regio-selectivity, is a promising biocatalyst for lipids modification.