Characterization of an Alkaline GH49 Dextranase from Marine Bacterium <i>Arthrobacter</i> <i>oxydans</i> KQ11 and Its Application in the Preparation of Isomalto-Oligosaccharide

A GH49 dextranase gene DexKQ was cloned from marine bacteria <i>Arthrobacter oxydans</i> KQ11. It was recombinantly expressed using an <i>Escherichia coli</i> system. Recombinant DexKQ dextranase of 66 kDa exhibited the highest catalytic activity at pH 9.0 and 55 &#176;C....

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Bibliographic Details
Published in:Marine Drugs
Main Authors: Hongfei Liu, Wei Ren, Mingsheng Ly, Haifeng Li, Shujun Wang
Format: Article
Language:English
Published: MDPI AG 2019-08-01
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Online Access:https://www.mdpi.com/1660-3397/17/8/479
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Summary:A GH49 dextranase gene DexKQ was cloned from marine bacteria <i>Arthrobacter oxydans</i> KQ11. It was recombinantly expressed using an <i>Escherichia coli</i> system. Recombinant DexKQ dextranase of 66 kDa exhibited the highest catalytic activity at pH 9.0 and 55 &#176;C. kcat/Km of recombinant DexKQ at the optimum condition reached 3.03 s<sup>&#8722;1</sup> &#956;M<sup>&#8722;1</sup>, which was six times that of commercial dextranase (0.5 s<sup>&#8722;1</sup> &#956;M<sup>&#8722;1</sup>). DexKQ possessed a <i>K</i>m value of 67.99 &#181;M against dextran T70 substrate with 70 kDa molecular weight. Thin-layer chromatography (TLC) analysis showed that main hydrolysis end products were isomalto-oligosaccharide (IMO) including isomaltotetraose, isomaltopantose, and isomaltohexaose. When compared with glucose, IMO could significantly improve growth of <i>Bifidobacterium longum</i> and <i>Lactobacillus rhamnosus</i> and inhibit growth of <i>Escherichia coli</i> and <i>Staphylococcus aureus</i>. This is the first report of dextranase from marine bacteria concerning recombinant expression and application in isomalto-oligosaccharide preparation.
ISSN:1660-3397