Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase from Sp. Nov. JL3085

Overview

Journal Mar Drugs

Publisher MDPI

Specialties Biology
Pharmacology

Date 2020 May 10

PMID 32384803

Citations 2

Authors

Jianlong He

Le Liu

Xiaoyan Liu

Kai Tang

Affiliations

Soon will be listed here.

Abstract

We cloned a xylanase gene () from marine bacterium sp. nov. JL3085 and recombinantly expressed it in BL21. This gene encoded a polypeptide with 379 amino acid residues and a molecular weight of ~43 kDa. Its amino acid sequence shared 45.3% similarity with an endoxylanase from Cellvibrio mixtus that belongs to glycoside hydrolases family 10 (GH10). The XynT showed maximum activity at 40 °C and pH 7.0, and a maximum velocity of 62 μmoL min mg. The XynT retained its maximum activity by more than 69%, 51%, and 26% at 10 °C, 5 °C, and 0 °C, respectively. It also exhibited the highest activity of 135% in the presence of 4 M NaCl and retained 76% of its activity after 24 h incubation with 4 M NaCl. This novel xylanase, XynT, is a cold-active and halotolerant enzyme that may have promising applications in drug, food, feed, and bioremediation industries.

Citing Articles

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