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固定化突变脂肪酶合成富含共轭亚油酸的三酰基甘油,具有优异的性能和可重复使用性。

Synthesis of conjugated linoleic acid-rich triacylglycerols by immobilized mutant lipase with excellent capability and recyclability.

机构信息

School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.

College of Life Science, Tarim University, Alar 843300, China.

出版信息

Enzyme Microb Technol. 2018 Oct;117:56-63. doi: 10.1016/j.enzmictec.2018.06.007. Epub 2018 Jun 18.

Abstract

Conjugated linoleic acid (CLA)-rich triacylglycerols (TAG) have received significant attention owing to their health promoting properties. In this study, CLA-rich TAG were successfully synthesized by an immobilized mutant lipase (MAS1-H108A)-catalyzed esterification of CLA-rich fatty acids and glycerol under vacuum. MAS1-H108A was first immobilized onto ECR1030 resin. Results showed that the lipase/support ratio of 41 mg/g was suitable for the immobilization and the thermostability of immobilized MAS1-H108A was greatly enhanced. Subsequently, the immobilized MAS1-H108A was employed for the synthesis of CLA-rich TAG and 95.21% TAG with 69.19% CLA was obtained under the optimized conditions. The TAG content (95.21%) obtained by immobilized MAS1-H108A is the reported highest value thus far, which was significantly higher than that (9.26%) obtained by Novozym 435 under the same conditions. Although the TAG content comparable to the results obtained in this study could also be obtained by Novozym 435, the used enzyme amount is approximately 5-fold of the immobilized MAS1-H108A. Additionally, the immobilized MAS1-H108A exhibited excellent recyclability during esterification retaining 95.11% of its initial activity after 10 batches. Overall, such immobilized mutant lipase with superior esterification activity and recyclability has the potential to be used in oils and fats industry.

摘要

共轭亚油酸(CLA)丰富的三酰基甘油(TAG)因其具有促进健康的特性而受到广泛关注。在这项研究中,通过固定化突变脂肪酶(MAS1-H108A)催化 CLA 丰富的脂肪酸和甘油在真空下的酯化反应,成功合成了 CLA 丰富的 TAG。MAS1-H108A 首先固定在 ECR1030 树脂上。结果表明,脂肪酶/载体比为 41mg/g 适合固定化,固定化 MAS1-H108A 的热稳定性得到了极大提高。随后,将固定化 MAS1-H108A 用于合成 CLA 丰富的 TAG,在优化条件下可获得 95.21%的 TAG 和 69.19%的 CLA。固定化 MAS1-H108A 获得的 TAG 含量(95.21%)是迄今为止报道的最高值,明显高于相同条件下 Novozym 435 获得的 9.26%。尽管 Novozym 435 也可以获得与本研究结果相当的 TAG 含量,但所用酶量约为固定化 MAS1-H108A 的 5 倍。此外,MAS1-H108A 在酯化过程中表现出优异的可重复使用性,在 10 批后保留了其初始活性的 95.11%。总体而言,这种具有优越酯化活性和可重复使用性的固定化突变脂肪酶有可能在油脂工业中得到应用。

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