一种新的韩国康氏菌苯丙氨酸解氨酶

IF 0.5 4区化学 Q4 CHEMISTRY, MULTIDISCIPLINARY Studia Universitatis Babes-bolyai Chemia Pub Date : 2017-01-01 DOI:10.24193/SUBBCHEM.2017.3.25

A. Varga, Z. Bata, Pál Csuka, Diana Monica Bordea, B. Vértessy, A. Marcovici, F. Irimie, L. Poppe, L. Bencze

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引用次数: 7

摘要

本研究将韩国康氏菌(Kangiella koreensis, KkPAL)苯丙氨酸解氨酶基因克隆到pET19b表达载体上。优化蛋白表达和纯化条件，从1升大肠杆菌培养物中获得纯可溶性蛋白15 mg。不同天然芳香族氨基酸的解氨酶活性测定证实该蛋白为苯丙氨酸解氨酶。分离得到的蛋白显示出非常高的熔融温度，达到81.7℃，使其特别适合生物催化应用。

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A novel phenylalanine ammonia-lyase from Kangiella koreensis

This study describes the cloning of the gene encoding a novel phenylalanine ammonia-lyase from Kangiella koreensis (KkPAL) into pET19b expression vector. Optimization of protein expression and purification conditions yielded 15 mg pure soluble protein from one liter of E. coli culture. Enzymatic activity measurements of the ammonia elimination reaction from different natural aromatic amino acids proved the protein to be a phenylalanine ammonia-lyase. The isolated protein showed remarkably high, 81.7 °C melting temperature, making it especially suitable for biocatalytic applications.

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来源期刊

Studia Universitatis Babes-bolyai Chemia 化学-化学综合

CiteScore

0.80

自引率

33.30%

发文量

审稿时长

>12 weeks

期刊介绍： Studia Universitatis Babes-Bolyai, Seria Chemia publishes fundamental studies in all areas of chemistry and chemical engineering. Coverage includes experimental and theoretical reports on quantitative studies of structure and thermodynamics, kinetics, mechanisms of reactions, inorganic, organic, organometallic chemistry, biochemistry, computational chemistry, solid-state phenomena, surface chemistry, chemical technology and environmental chemistry.