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首页> 外文期刊>BMC Biotechnology >Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum
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Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum

机译：短小芽孢杆菌漆酶：具有广泛底物谱的热稳定酶

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Background Laccases are multi-copper oxidases that catalyze the one electron oxidation of a broad range of compounds. Laccase substrates include substituted phenols, arylamines and aromatic thiols. Such compounds are activated by the enzyme to the corresponding radicals. Owing to their broad substrate range laccases are considered to be versatile biocatalysts which are capable of oxidizing natural and non-natural industrial compounds, with water as sole by-product. Results A novel CotA-type laccase from Bacillus pumilus was cloned, expressed and purified and its biochemical characteristics are presented here. The molecular weight of the purified laccase was estimated to be 58 kDa and the enzyme was found to be associated with four copper atoms. Its catalytic activity towards 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS), 2,6-dimethoxyphenol (2,6-DMP) and syringaldazine (SGZ) was investigated. The kinetic parameters K M and k cat for ABTS were 80 ± 4 μM and 291 ± 2.7 s-1, for 2,6-DMP 680 ± 27 μM and 11 ± 0.1 s-1 and for SGZ only k cat could be estimated to be 66 ± 1.5 s-1. The pH optimum for ABTS was 4, for 2,6-DMP 7 and for SGZ 6.5 and temperature optima for ABTS and 2,6-DMP were found to be around 70°C. The screening of 37 natural and non-natural compounds as substrates for B. pumilus laccase revealed 18 suitable compounds. Three of them served as redox mediators in the laccase-catalyzed decolorization of the dye indigocarmine (IC), thus assessing the new enzyme's biotechnological potential. Conclusions The fully copper loaded, thermostable CotA laccase from Bacillus pumilus is a versatile laccase with potential applications as an industrial biocatalyst.
机译：背景技术漆酶是多铜氧化酶，可催化多种化合物的单电子氧化。漆酶底物包括取代的酚，芳基胺和芳族硫醇。这类化合物被酶激活成相应的基团。由于漆酶具有广泛的底物范围，因此被认为是通用的生物催化剂，它们能够氧化天然和非天然的工业化合物，而水是唯一的副产物。结果克隆，表达和纯化了一种新的短小芽孢杆菌CotA型漆酶，并提出了其生化特性。纯化的漆酶的分子量估计为58 kDa，发现该酶与四个铜原子缔合。研究了其对2,2'-叠氮基双（3-乙基苯并噻唑啉-6-磺酸）（ABTS），2,6-二甲氧基苯酚（2,6-DMP）和丁香嗪（SGZ）的催化活性。 ABTS的动力学参数K M 和k cat 为80±4μM和291± 2.7 s -1 ，对于2,6-DMP 680±27μM和11±0.1 s -1 ，对于SGZ，仅k cat 估计为66±1.5 s -1 < / sup>。对于ABTS而言，最适的pH为4，对于2,6-DMP 7而言，对于SGZ 6.5而言，最适pH为70°C左右。筛选作为短小芽孢杆菌漆酶底物的37种天然和非天然化合物发现了18种合适的化合物。其中三个在漆酶催化的染料靛蓝胭脂红（IC）的脱色中充当氧化还原介体，从而评估了这种新酶的生物技术潜力。结论来自短小芽孢杆菌的全铜负载的热稳定的CotA漆酶是一种通用的漆酶，具有作为工业生物催化剂的潜在用途。

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