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Properties of recombinant 4-?-glucanotransferase from Bifidobacterium longum subsp. longum JCM 1217 and its application.

ABSTRACT: To determine the physiochemical properties of the 4-?-glucanotransferase from Bifidobacterium sp., the bllj_0114 gene encoding 4-?-glucanotransferase was cloned from Bifidobacterium longum subsp. longum JCM 1217 and expressed in Escherichia coli. The amino acid sequence alignment indicated that the recombinant protein, named BL-?GTase, belongs to the glycoside hydrolase (GH) family 77. BL-?GTase was purified using nickel-nitrilotriacetic acid affinity chromatography and characterized using various substrates. The enzyme catalyzed the disproportionation activity, which transfers a glucosyl unit from oligosaccharides to acceptor molecules, and had the highest activity at 40 °C and pH 6.0. In the presence of 5 mM metal ions, in particular Cu2+, Zn2+, and Fe2+, BL-?GTase activity was reduced. To determine whether BL-?GTase can be used to generate thermoreversible gels, potato starch was treated with BL-?GTase for various reaction times. The BL-?GTase-treated starches showed sol-gel reversibility and melted at 59.6-75.7 °C.

SUBMITTER: Jeong DW 

PROVIDER: S-EPMC7221098 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Properties of recombinant 4-α-glucanotransferase from <i>Bifidobacterium longum</i> subsp. <i>longum</i> JCM 1217 and its application.

Jeong Da-Woon DW   Jeong Hyun-Mo HM   Shin Yu-Jeong YJ   Woo Seung-Hye SH   Shim Jae-Hoon JH  

Food science and biotechnology 20191223 5

To determine the physiochemical properties of the 4-α-glucanotransferase from <i>Bifidobacterium</i> sp., the <i>bllj</i>_0114 gene encoding 4-α-glucanotransferase was cloned from <i>Bifidobacterium longum</i> subsp. <i>longum</i> JCM 1217 and expressed in <i>Escherichia coli</i>. The amino acid sequence alignment indicated that the recombinant protein, named BL-αGTase, belongs to the glycoside hydrolase (GH) family 77. BL-αGTase was purified using nickel-nitrilotriacetic acid affinity chromatog  ...[more]

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