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脂肪酶杂化纳米花的自组装具有双功能 Ca,可提高活性和稳定性。

Self-assembly of lipase hybrid nanoflowers with bifunctional Ca for improved activity and stability.

机构信息

School of Bioengineering, Dalian University of Technology, Dalian, 116024, China.

School of Food and Environmental Science and Technology, Dalian University of Technology, Panjin, 12421, China.

出版信息

Enzyme Microb Technol. 2020 Jan;132:109408. doi: 10.1016/j.enzmictec.2019.109408. Epub 2019 Aug 17.

DOI:10.1016/j.enzmictec.2019.109408
PMID:31731973
Abstract

Lipase ZC12, a cold-adapted lipase derived from Psychrobacter sp. ZY124, can be effectively activated by Ca. Inspired by this significant property, we developed a novel immobilized lipase ZC12/Ca(PO) hybrid nanoflowers (LHNs). The LHNs have been characterized as a regular hierarchical flowerlike structure nanoflowers by scanning electron microscopy (SEM). Compared with free lipase ZC12, the LHNs exerted enhanced enzymatic activity of 206% and 2.31-fold in k/K value, especially high specific activity at low temperature. After 7 successive cycles, the LHNs could still maintain its initial activity, demonstrating superior durability than the free lipase ZC12. Meanwhile, its stability basically kept unchanged in a wide range of temperature and pH. Finally, fructose laurate was transformed by the LHNs with 57.39% conversion rate which is twice as much as the free lipase. To sum up, these results validated that LHNs could emerge as an efficient immobilized lipase and possess the promising potential for practical applications.

摘要

脂肪酶 ZC12 是一种源自Psychrobacter sp. ZY124 的耐冷脂肪酶,能够被 Ca 有效激活。受此显著特性的启发,我们开发了一种新型固定化脂肪酶 ZC12/Ca(PO)杂化纳米花(LHNs)。通过扫描电子显微镜(SEM)对 LHNs 进行了表征,结果表明其具有规则的分级花状纳米花结构。与游离脂肪酶 ZC12 相比,LHNs 的酶活提高了 206%,k/K 值提高了 2.31 倍,低温下的比酶活更高。经过 7 次连续循环后,LHNs 仍能保持其初始活性,其耐用性优于游离脂肪酶 ZC12。同时,其在较宽的温度和 pH 范围内基本保持稳定。最后,LHNs 可将月桂酸果糖酯转化为 57.39%的转化率,是游离脂肪酶 ZC12 的两倍。综上所述,这些结果验证了 LHNs 可以作为一种高效的固定化脂肪酶,并具有实际应用的巨大潜力。

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