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T1脂肪酶的脂肪酸特异性及其在酰基甘油合成中的潜力。

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

作者信息

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

机构信息

College of Food Sciences, Southwest University, Chongqing, 400715, People's Republic of China; College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, 510640, People's Republic of China.

出版信息

J Sci Food Agric. 2014 Jun;94(8):1614-21. doi: 10.1002/jsfa.6468. Epub 2013 Dec 12.

DOI:10.1002/jsfa.6468
PMID:24338705
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 (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.

摘要

背景

T1脂肪酶因其热稳定性而备受关注。研究了T1脂肪酶(粗酶和纯化酶)的脂肪酸特异性,并评估了其在酰基甘油合成中的潜力。

结果

在脂肪酸(C6:0至C18:3)酯化反应中研究了T1脂肪酶(粗酶和纯化酶)的脂肪酸特异性,结果表明粗酶和纯化酶对C18:0的偏好最低[特异性常数(1/α)=0.08],其次是C18:1(1/α = 0.12),对C8:0的偏好最高(1/α = 1)。构建了一个结构模型以简要探究脂肪酶与其底物之间的相互作用。此外,研究了粗T1脂肪酶催化甘油与C18:1酯化合成二酰基甘油(DAGs)和单酰基甘油(MAGs),以评估其在酰基甘油合成中的潜力。最佳条件为甘油/油酸摩尔比5:1、脂肪酶浓度为底物的9.7 U g(-1))、水含量为底物的50 g kg(-1)以及温度50°C,在此条件下2小时时可产生42.25%的DAGs、26.34%的MAGs和9.18%的三酰基甘油。

结论

尽管使用了C18:1(一种较差的底物),但仍以较高产率合成了DAGs和MAGs。我们的工作表明,已发现具有1,3-区域选择性的T1脂肪酶是一种有前途的用于脂质修饰的生物催化剂。

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