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Typoselectivity of Crude Geobacillus sp. T1 Lipase Fused with a Cellulose‐Binding Domain and Its Use in the Synthesis of Structured Lipids
Author(s) -
Qin XiaoLi,
Huang HuiHua,
Lan DongMing,
Wang YongHua,
Yang Bo
Publication year - 2014
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/s11746-013-2347-4
Subject(s) - lipase , tripalmitin , chemistry , soybean oil , hexane , cellulose , triacylglycerol lipase , chromatography , organic chemistry , enzyme , food science
Typoselectivity of crude CBD‐T1 lipase ( Geobacillus sp. T1 lipase fused with a cellulose binding domain) was investigated. Multi‐competitive reaction mixtures including a set of n ‐chain fatty acids (C8:0, C10:0, C12:0, C14:0, C18:1 n‐9, C18:2 n‐6 and C18:3 n‐3) and tripalmitin‐enriched triacylglycerols were studied in hexane. The crude CBD‐T1 lipase discriminated strongly against C18:1 n‐9 [competitive factor ( α ) = 0.23] and showed the highest preference for C8:0 ( α = 1). Utilizing the catalytic properties of crude CBD‐T1 lipase, acidolysis of soybean oil with C8:0 was selected as a model reaction to investigate the ability of the lipase to produce MLM‐type (medium‐long‐medium) structured lipids. Several reaction parameters (added water amount, reaction temperature, substrate molar ratio and reaction time) examined for incorporating C8:0 into soybean oil, the optimum conditions were: 1:3 (soybean oil/C8:0) of molar ratio, 3 mL of hexane, 50 °C of temperature, 48 h of reaction time, 20 % of crude CBD‐T1 lipase (w/w total substrates), and 7.5 % of water (w/w enzyme). Under these conditions, the incorporation of C8:0 was 29.6 mol%. The results suggest that crude CBD‐T1 lipase, which showed different fatty acid specificity profiles, is a potential biocatalyst for the modification of fats and oils.