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酪氨酸酶对咖啡酸及其正壬酯的作用。催化和自杀失活。

Action of tyrosinase on caffeic acid and its n-nonyl ester. Catalysis and suicide inactivation.

机构信息

GENZ-Group of research on Enzymology, Department of Biochemistry and Molecular Biology-A, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, E-30100, Espinardo, Murcia, Spain(1).

Group of Molecular Interactions in Membranes, Department of Biochemistry and Molecular Biology-A, University of Murcia, E-30100, Espinardo, Murcia, Spain.

出版信息

Int J Biol Macromol. 2018 Feb;107(Pt B):2650-2659. doi: 10.1016/j.ijbiomac.2017.10.151. Epub 2017 Oct 31.

DOI:10.1016/j.ijbiomac.2017.10.151
PMID:29080822
Abstract

Different mechanisms for inhibiting tyrosinase can be designed to avoid postharvest quality losses of fruits and vegetables. The action of tyrosinase on caffeic acid and its n-nonyl ester (n-nonyl caffeate) was characterized kinetically in this work. The results lead us to propose that both compounds are suicide substrates of tyrosinase, for which we establish the catalytic and inactivation efficiencies. The ester is more potent as inactivator than the caffeic acid and the number of turnovers made by one molecule of the enzyme before its inactivation (r) is lower for the ester. We proposed that the anti-browning and antibacterial properties may be due to suicide inactivation processes.

摘要

可以设计出不同的抑制酪氨酸酶的机制来避免果蔬采后品质的损失。本工作从动力学上对酪氨酸酶对咖啡酸及其正壬基酯(正壬基咖啡酸酯)的作用进行了表征。结果表明,这两种化合物都是酪氨酸酶的自杀底物,我们建立了它们的催化和失活动力学效率。该酯作为抑制剂比咖啡酸更有效,并且在酶失活之前一个酶分子的转化数(r)也较低。我们提出,抗褐变和抗菌特性可能归因于自杀失活动力学过程。

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