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Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities.
Microbial Physiology ( IF 1.2 ) Pub Date : 2018-08-28 , DOI: 10.1159/000491698
Laura Emilce Navas 1, 2 , Mónica Florin-Christensen 3, 4 , Graciela Beatriz Benintende 5 , Rubén Oreste Zandomeni 4, 5 , Marcelo Facundo Berretta 4, 5
Affiliation  

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.

中文翻译:

新型热稳定酶的表征。2.9具有磷脂酶和酰基转移酶活性。

磷脂酶根据它们在磷脂中裂解的酯键分为不同的酶家族。在工业过程中使用磷脂酶促使人们寻找具有不同特性的新酶。在嗜热菌株Thermus sp。的基因组中鉴定出编码新型磷脂酶(PLP_2.9)的基因。2.9。一级序列的分析揭示了patatin样结构域。PLP_2.9的氨基酸序列与其他细菌与patatin相关的蛋白的比对表明,这种磷脂酶的四个特征嵌段和代表催化二倍体的氨基酸均在该蛋白中保守。PLP_2.9在大肠杆菌中过表达,并对纯化的酶进行生化表征。PLP_2。9在较宽的温度范围(55-80°C)下,在碱性pH下水解了对硝基苯基棕榈酸酯,显示出很高的热稳定性。PLP_2.9在蛋黄磷脂酰胆碱上显示磷脂酶A和酰基转移酶活性。由于其高的热稳定性,PLP_2.9在许多工业过程中具有潜在的催化剂用途。
更新日期:2019-11-01
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