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KMID : 1007520200290050667
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Food Science and Biotechnology
2020 Volume.29 No. 5 p.667 ~ p.674
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Properties of recombinant 4-α-glucanotransferase from Bifidobacterium longum subsp. longum JCM 1217 and its application
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Jeong Da-Woon
Jeong Hyun-Mo
Shin Yu-Jeong
Woo Seung-Hye
Shim Jae-Hoon
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Abstract
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To determine the physiochemical properties of the 4-α-glucanotransferase from Bifidobacterium sp., the bllj_0114 gene encoding 4-α-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-αGTase, belongs to the glycoside hydrolase (GH) family 77. BL-αGTase 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-αGTase activity was reduced. To determine whether BL-αGTase can be used to generate thermoreversible gels, potato starch was treated with BL-αGTase for various reaction times. The BL-αGTase-treated starches showed sol?gel reversibility and melted at 59.6?75.7 °C.
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KEYWORD
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Bifidobacterium longum, 4-α-glucanotransferase, Thermoreversible gel, Transglycosylation
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