Characterization of a laccase-like multicopper oxidase from newly isolated Streptomyces sp C1 in agricultural waste compost and enzymatic decolorization of azo dyes
Characterization of a laccase-like multicopper oxidase from newly isolated Streptomyces sp C1 in agricultural waste compost and enzymatic decolorization of azo dyes
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新分离的链霉菌中漆酶样多铜氧化酶的表征。
DOI：
10.1016/j.bej.2013.01.004
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发表时间：
2013-03-15
影响因子：
3.9
通讯作者：
Jiang, Min
中科院分区：
文献类型：
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作者：
Lu, Lunhui;Zeng, Guangming;Jiang, Min
漆酶或漆酶样多铜氧化酶（LMCO）可以催化各种底物的氧化，并将氧还原为水。本研究从堆肥不同阶段的样品中分离到8株漆酶活性较高的菌株，其中从高温阶段样品中分离到的菌株C1漆酶活性最高。纯化的C1菌株LMCO在SDS-PAGE凝胶上显示单一的蛋白条带，分子量约为38 kDa。该漆酶具有一定的耐碱性和中等的热稳定性。在浓度为1 mM时，Cu ~（2+）、Co ~（2+）、Fe ~（3+）等金属离子对该酶有激活作用，而Hg ~（2+）对该酶有强烈的抑制作用。该LMCO对靛蓝胭脂红和钻石黑PV具有较好的脱色效果，在纺织工业中具有很好的应用前景。经鉴定，该菌株为链霉菌C1。本研究中新的漆酶产生菌链霉菌C1的发现也将有助于进一步解释放线菌在堆肥高温阶段的功能。(C)2013爱思唯尔有限公司版权所有。
Laccases or laccase-like multicopper oxidases (LMCOs) could catalyze the oxidation of various substrates coupled to the reduction of oxygen to water. In this study, eight strains with laccase activity were isolated from composting samples in different phases, among which strain C1 isolated from the thermophilic-phase sample presented the highest laccase activity. The purified LMCO of strain C1 showed a single protein band on SDS-PAGE gel with a molecular mass of about 38 kDa. The novel laccase showed alkaline resistance and moderate thermostability. The enzyme activity was activated by some metal ions such as Cu2+, Co2+ and Fe3+ at the concentration of 1 mM, while was strongly inhibited in the presence of Hg2+. The LMCO could efficiently decolorize the indigo carmine and diamond black PV with syringaldehyde as mediator, which suggested a great potential for dye decolorization in the textile industry. The novel strain was identified as Streptomyces sp. C1. The finding of new laccase-producing Streptomyces sp. C1 in this study will also contribute to the further explanation of the function of Actinomycetes in the thermophilic phase of composting. (C) 2013 Elsevier B.V. All rights reserved.