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首页> 外文期刊>Applied Microbiology and Biotechnology >A bacterial laccase from marine microbial metagenome exhibiting chloride tolerance and dye decolorization ability
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A bacterial laccase from marine microbial metagenome exhibiting chloride tolerance and dye decolorization ability

机译：来自海洋微生物基因组的细菌漆酶具有耐氯性和染料脱色能力

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摘要

Laccases are blue multicopper oxidases with potential applications in environmental and industrial biotechnology. In this study, a new bacterial laccase gene of 1.32 kb was obtained from a marine microbial metagenome of the South China Sea by using a sequence screening strategy. The protein (named as Lac15) of 439 amino acids encoded by the gene contains three conserved Cu2+-binding domains, but shares less than 40% of sequence identities with all of the bacterial multicopper oxidases characterized. Lac15, recombinantly expressed in Escherichia coli, showed high activity towards syringaldazine at pH 6.5–9.0 with an optimum pH of 7.5 and with the highest activity occurring at 45 °C. Lac15 was stable at pH ranging from 5.5 to 9.0 and at temperatures from 15 to 45 °C. Distinguished from fungal laccases, the activity of Lac15 was enhanced twofold by chloride at concentrations lower than 700 mM, and kept the original level even at 1,000 mM chloride. Furthermore, Lac15 showed an ability to decolorize several industrial dyes of reactive azo class under alkalescent conditions. The properties of alkalescence-dependent activity, high chloride tolerance, and dye decolorization ability make the new laccase Lac15 an alternative for specific industrial applications.
机译：漆酶是蓝色的多铜氧化酶，具有在环境和工业生物技术中的潜在应用。在这项研究中，使用序列筛选策略从南海的一个海洋微生物基因组中获得了一个新的1.32 kb细菌漆酶基因。该基因编码的439个氨基酸的蛋白质（称为Lac15）包含3个保守的Cu 2 + 结合域，但与所有细菌多铜氧化酶共享的序列同一性不到40％。在大肠杆菌中重组表达的Lac15在6.5–9.0的条件下对丁香嗪具有很高的活性，最适pH值为7.5，在45°C时活性最高。 Lac15在5.5至9.0的pH值和15至45°C的温度下稳定。与真菌漆酶不同，在低于700 mM的浓度下，氯化物将Lac15的活性提高了两倍，甚至在1000 mM的氯化物中也保持了原始水平。此外，Lac15具有在碱性条件下使几种活性偶氮类工业染料脱色的能力。依赖碱性的活性，高氯化物耐受性和染料脱色能力使新型漆酶Lac15成为特定工业应用的替代品。

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