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从造纸厂污泥的宏基因组文库中分离出一个属于新家族的酯酶的表达和特性。

Expression and characterization of an esterase belonging to a new family via isolation from a metagenomic library of paper mill sludge.

机构信息

School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, PR China.

School of Life Science and Technology, Nanyang Normal University, Nanyang 473061, PR China.

出版信息

Int J Biol Macromol. 2019 Apr 1;126:1192-1200. doi: 10.1016/j.ijbiomac.2019.01.025. Epub 2019 Jan 6.

DOI:10.1016/j.ijbiomac.2019.01.025
PMID:30625356
Abstract

A new bacterial lipolytic enzyme Est903 was obtained from paper mill sludge via metagenomic approach. Est903 displayed moderate similarities to two lipolytic enzymes from Rhodopirellula islandica and contained a distinctive pentapeptide motif (GFSAG) that differed from those of all known fourteen families of bacterial lipolytic enzymes. Est903 was regarded as from a new bacterial lipolytic enzyme family through multiple sequence alignment and phylogenetic analysis. The recombinant Est903 showed the highest activity for ρ-nitrophenol butyrate. The pH optimum and temperature optimum of the recombinant enzyme was 9.0 and 51 °C, respectively. Also, this enzyme displayed moderate thermostability, high activity under alkaline conditions, and good tolerance against several organic solvents. In addition, the compatibility test and washing performance analysis revealed that Est903 had good compatibility with commercial laundry detergent and high cleaning ability of oil stains. These good properties make Est903 a potential candidate in organic synthesis or detergent industry.

摘要

通过宏基因组学方法,从造纸厂污泥中获得了一种新型细菌脂肪酶 Est903。Est903 与来自 Rhodopirellula islandica 的两种脂肪酶具有中等相似性,并且含有独特的五肽基序(GFSAG),与所有已知的 14 种细菌脂肪酶家族不同。通过多序列比对和系统发育分析,将 Est903 归类为一种新型细菌脂肪酶家族。重组 Est903 对 ρ-硝基苯酚丁酸显示出最高的活性。重组酶的最适 pH 值和最适温度分别为 9.0 和 51°C。此外,该酶显示出中等的热稳定性、在碱性条件下的高活性以及对几种有机溶剂的良好耐受性。此外,相容性测试和洗涤性能分析表明,Est903 与商业洗衣洗涤剂具有良好的相容性,并且对油斑具有高清洁能力。这些良好的特性使 Est903 成为有机合成或洗涤剂行业的潜在候选者。

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