Laccase activity tests and laccase inhibitors
Laccase activity tests and laccase inhibitors
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DOI：
10.1016/s0168-1656(00)00208-x
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发表时间：
2000-03-10
影响因子：
4.1
通讯作者：
Majcherczyk, A
中科院分区：
文献类型：
--
作者：
Johannes, C;Majcherczyk, A
以2，6-二甲氧基苯酚和2，2 ′-连氮基-双-（3-乙基苯并噻唑啉-6-磺酸）（ABTS）为底物，在不同的试验体系中，测定了巯基有机化合物（二硫苏糖醇、巯基乙酸、半胱氨酸、二乙基二硫代氨基甲酸和叠氮化钠）对变色栓菌漆酶的抑制活性。只有叠氮化钠作为一个真正的漆酶抑制剂，并没有表现出显着的干扰酶的测试。所有其他物质没有显着抑制漆酶活性和先前报道的抑制作用的结果从反应产物，如ABTS自由基阳离子和二醌或随后的非酶相互作用在底物氧化过程中的减少。后者显然与未反应的ABTS形成复合物，显示不同的光谱特征，导致低估酶活性。(C)2000 Elsevier Science B. V.保留所有权利。
Sulfhydryl organic compounds described as laccase inhibitors: dithiothreitol, thioglycolic acid, cysteine, diethyldithiocarbamic acid, and sodium azide were tested for their activity toward laccase of Trametes versicolor in different test systems utilising 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,6-dimethoxyphenol as enzyme substrates. Only sodium azide acted as a true laccase inhibitor and showed no significant interference with the enzyme tests. All other substances did not significantly inhibit the laccase activity and the previously reported inhibitory effects result from the reductions of the reaction products such as ABTS radical cation and diquinone or subsequent non-enzymatic interactions during substrate oxidation. The latter apparently forms a complex with unreacted ABTS displaying varied spectral characteristics and resulting in am underestimation of enzyme activity. (C) 2000 Elsevier Science B.V. All rights reserved.