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Updated: Dec 21, 2025
High Throughput Screening of Fungal Endoglucanase Activity in Escherichia coli
Published on: August 13, 2011
Properties of recombinant 4-α-glucanotransferase from Bifidobacterium longum subsp. longum JCM 1217 and its
Da-Woon Jeong1, Hyun-Mo Jeong1, Yu-Jeong Shin1
1Department of Food Science and Nutrition, and The Korean Institute of Nutrition, Hallym University, Chuncheon, 24252 Republic of Korea.
Abstract:
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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