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Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase from Echinicola rosea sp. Nov. JL3085T.


ABSTRACT: We cloned a xylanase gene (xynT) from marine bacterium Echinicola rosea sp. nov. JL3085T and recombinantly expressed it in Escherichia coli 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 ?moL min-1 mg-1. 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.

SUBMITTER: He J 

PROVIDER: S-EPMC7281462 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase from <i>Echinicola rosea</i> sp. Nov. JL3085<sup>T</sup>.

He Jianlong J   Liu Le L   Liu Xiaoyan X   Tang Kai K  

Marine drugs 20200506 5


We cloned a xylanase gene (<i>xynT</i>) from marine bacterium <i>Echinicola rosea</i> sp. nov. JL3085<sup>T</sup> and recombinantly expressed it in <i>Escherichia coli</i> 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  ...[more]

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