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T1脂肪酶
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY · 2013 ·Vol. 91 ·期 1 ·55-62 · IF 1.592

Typoselectivity of Crude Geobacillus sp. T1 Lipase Fused with a Cellulose-Binding Domain and Its Use in the Synthesis of Structured Lipids

Qin Xiao-Li,Huang Hui-Hua,Lan Dong-Ming,Wang Yong-Hua,Yang Bo

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.

研究领域: 生物化学 · 食品科学
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JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE · 2013 ·Vol. 94 ·期 8 ·1614-1621 · IF 1.759

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

Xiao-Li Qin,Dong-Ming Lan,Jin-Feng Zhong,Lu Liu,Yong-Hua Wang,Bo Yang

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 (C6:0 to C18:3), suggesting that crude and purified T1 lipase had the lowest preference for C18:0 [specificity constant (1/ α ) = 0.08] followed by C18:1 (1/ α = 0.12) and showed the highest preference for C8:0 (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 C18:1 was studied for evaluating its potential in acylglycerols synthesis. The optimal conditions were glycerol/oleic acid molar ratio 5:1, 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 C18:1 (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. © 2013 Society of Chemical Industry

研究领域: 生物化学 · 酶工程
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