热稳定性
酶
产量(工程)
戊二醛
生物催化
化学
共价键
可重用性
酪氨酸
蛋白质工程
组合化学
催化作用
催化效率
生物化学
有机化学
材料科学
计算机科学
冶金
程序设计语言
离子液体
软件
作者
Mingyu Jia,Zhiyuan Luo,Haomin Chen,Bianqin Ma,Qiao Li,Qinjie Xiao,Pengfei Zhang,Anming Wang
出处
期刊:Biomolecules
[MDPI AG]
日期:2022-07-18
卷期号:12 (7): 997-997
被引量:2
摘要
Ideal immobilization with enhanced biocatalyst activity and thermostability enables natural enzymes to serve as a powerful tool to yield synthetically useful chemicals in industry. Such an enzymatic method strategy becomes easier and more convenient with the use of genetic and protein engineering. Here, we developed a covalent programmable polyproteam of tyrosine ammonia lyases (TAL-CLEs) by fusing SpyTag and SpyCatcher peptides into the N-terminal and C-terminal of the TAL, respectively. The resulting circular enzymes were clear after the spontaneous isopeptide bonds formed between the SpyTag and SpyCatcher. Furthermore, the catalytic performance of the TAL-CLEs was measured via a synthesis sample of p-Coumaric acid. Our TAL-CLEs showed excellent catalytic efficiency, with 98.31 ± 1.14% yield of the target product—which is 4.15 ± 0.08 times higher than that of traditional glutaraldehyde-mediated enzyme aggregates. They also showed over four times as much enzyme-activity as wild-type TAL does and demonstrated good reusability, and so may become a good candidate for industrial enzymes.
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