Expression in Escherichia coli and Characterization of Arginase from Bacillus tequilensis

doi:10.7506/spkx1002-6630-201808013

Abstract

Abstract: Arginase is an alkaline hydrolases that catalyzes the production of urea and L-ornithine from arginine. An arginase gene encoding 297 amino acids was cloned from Bacillus tequilensis PanD37. By recombinant DNA technique, a genetically engineered strain of Escherichia coli was constructed for heterologous expression of the gene. Enzymatic assays indicated that the recombinant enzyme exhibited maximum activity at pH 10.0 and 45 ℃. Its activity was stable in the temperature range of 50–60 ℃ and in the pH range of 8.0–10.0. The enzymatic activity could be significantly activated by Mn2+, Ni2+, and Co2+. The activity of crude enzyme was 1 109.8 U/mL.

Key words: L-arginase, Bacillus tequilensis, L-ornithine, enzymatic properties

CLC Number:

Q812

ZHAO Qi, FENG Zhibin, QIN Xue, XU Qinxing, REN Mengyun, PAN Xiao, ZHANG Hongxia, ZHANG Juan. Expression in Escherichia coli and Characterization of Arginase from Bacillus tequilensis[J]. FOOD SCIENCE, 2018, 39(8): 77-82.

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Expression in Escherichia coli and Characterization of Arginase from Bacillus tequilensis

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