一种具有磷脂酶和酰基转移酶活性的新型热稳定性酶的鉴定

IF 1.2 Q2 Biochemistry, Genetics and Molecular Biology Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-08-27 DOI:10.1159/000491698
Laura Emilce Navas, Mónica Florin-Christensen, Graciela Beatriz Benintende, Rubén Oreste Zandomeni, Marcelo Facundo Berretta
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引用次数: 1

摘要

磷脂酶根据它们在磷脂中切割的酯键被分为不同的酶家族。磷脂酶在工业过程中的应用促使人们寻找具有不同性质的新酶。在嗜热菌株Thermus sp. 2.9的基因组中发现了一个编码新磷脂酶(PLP_2.9)的基因。初级层序的分析揭示了一个类似图案的结构域。PLP_2.9的氨基酸序列与其他细菌patatin相关蛋白的比对表明,该类型磷脂酶的四个片段特征和代表催化二元体的氨基酸在该蛋白中是保守的。PLP_2.9在大肠杆菌中过表达,纯化酶经生化鉴定。PLP_2.9在碱性条件下(55-80℃)水解对硝基苯基棕榈酸酯,表现出较高的热稳定性。PLP_2.9对蛋黄磷脂酰胆碱具有磷酸化酶A和酰基转移酶活性。由于其高热稳定性,PLP_2.9在许多工业过程中作为催化剂具有潜在的应用前景。
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Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities.

Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain Thermus sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP_2.9 was overexpressed in Escherichia coli and the purified enzyme was characterized biochemically. PLP_2.9 hydrolyzed p-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55-80°C), showing high thermostability. PLP_2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP_2.9 has potential applications as a catalyst in several industrial processes.

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来源期刊
Journal of Molecular Microbiology and Biotechnology
Journal of Molecular Microbiology and Biotechnology 生物-生物工程与应用微生物
CiteScore
3.90
自引率
0.00%
发文量
0
审稿时长
>12 weeks
期刊介绍: We are entering a new and exciting era of microbiological study and application. Recent advances in the now established disciplines of genomics, proteomics and bioinformatics, together with extensive cooperation between academic and industrial concerns have brought about an integration of basic and applied microbiology as never before.
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Contents Front & Back Matter The Life Cycle of Dictyostelium discoideum Is Accelerated via MAP Kinase Cascade by a Culture Extract Produced by a Synthetic Microbial Consortium A Riboflavin Transporter in Bdellovibrio exovorous JSS Front & Back Matter
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