Journal of Applied Glycoscience

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ISSN / EISSN : 13447882 / 18807291
Total articles ≅ 703
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Naoki Shirasaka, Koichi Harazono, Ryota Nakahigashi, Keigo Mitsui, Jun Tanaka, Sayaka Tanazawa, Masaru Mitsutomi, Takayuki Ohnuma
Journal of Applied Glycoscience; doi:10.5458/jag.jag.jag-2019_0001

Abstract:We characterized SaHEX, which is a glycoside hydrolase (GH) family 20 exo-β-N-acetylhexosaminidase found in Streptomyces avermitilis. SaHEX exolytically hydrolyzed chitin oligosaccharides from their non-reducing ends, and yielded N-acetylglucosamine (GlcNAc) as the end product. According to the initial rate of substrate hydrolysis, the rates of (GlcNAc)3 and (GlcNAc)5 hydrolysis were greater than the rates for the other oligosaccharides. The enzyme exhibited antifungal activity against Aspergillus niger, which was probably due to hydrolytic activity with regard to chitin in the hyphal tips. Therefore, SaHEX has potential for use in GlcNAc production and food preservation.
Atsushi Kawano, Yuji Matsumoto, Nozomi Nikaido, Akihiro Tominaga, Takashi Tonozuka, Kazuhide Totani, Nozomu Yasutake
Journal of Applied Glycoscience; doi:10.5458/jag.jag.jag-2018_0012

Abstract:We characterized an α-glucosidase belonging to the glycoside hydrolase family 31 from Aspergillus sojae. The α-glucosidase gene was cloned using the whole genome sequence of A. sojae, and the recombinant enzyme was expressed in Aspergillus nidulans. The enzyme was purified using affinity chromatography. The enzyme showed an optimum pH of 5.5 and was stable between pH 6.0 and 10.0. The optimum temperature was approximately 55 °C. The enzyme was stable up to 50 °C, but lost its activity at 70 °C. The enzyme acted on a broad range of maltooligosaccharides and isomaltooligosaccharides, soluble starch, and dextran, and released glucose from these substrates. When maltose was used as substrate, the enzyme catalyzed transglucosylation to produce oligosaccharides consisting of α-1,6-glucosidic linkages as the major products. The transglucosylation pattern with maltopentaose was also analyzed, indicating that the enzyme mainly produced oligosaccharides with molecular weights higher than that of maltopentaose and containing continuous α-1,6-glucosidic linkages. These results demonstrate that the enzyme is a novel α-glucosidase that acts on both maltooligosaccharides and isomaltooligosaccharides, and efficiently produces oligosaccharides containing continuous α-1,6-glucosidic linkages.
Di Guan, Rui Zhao, Yuan Li, Yoshikiyo Sakakibara, Masakazu Ike, Ken Tokuyasu
Journal of Applied Glycoscience, Volume 66, pp 21-28; doi:10.5458/jag.jag.jag-2018_0006

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Naoko Crofts, Ayaka Itoh, Misato Abe, Satoko Miura, Naoko F. Oitome, Jinsong Bao, Naoko Fujita
Journal of Applied Glycoscience, Volume 66, pp 37-46; doi:10.5458/jag.jag.jag-2018_005

Hideyuki Takahashi, Chiharu Yoshida, Takumi Takeda
Journal of Applied Glycoscience, Volume 66, pp 47-50; doi:10.5458/jag.jag.jag-2018_0007

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Haruka Yagi, Ryo Takehara, Aika Tamaki, Koji Teramoto, Sosyu Tsutsui, Satoshi Kaneko
Journal of Applied Glycoscience, Volume 66, pp 29-35; doi:10.5458/jag.jag.jag-2018_0008

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Shigekazu Yano, Yukari Hori, Tatsuro Kijima, Hiroyuki Konno, Wasana Suyotha, Kazuyoshi Takagi, Mamoru Wakayama
Journal of Applied Glycoscience; doi:10.5458/jag.jag.jag-2018_0011

Abstract:The cellulose binding domain (CBD) of cellulosome-integrating protein A from Clostridium thermocellum NBRC 103400 was genetically fused to FMN-dependent NADH-azoreductase (AZR) and glucose 1-dehydrogenase (GDH) from Bacillus subtilis. The fusion enzymes, AZR-CBD and CBD-GDH, were expressed in Escherichia coli Rosetta-gami B (DE3). The enzymes were purified from cell-free extracts, and the specific activity of AZR-CBD was 15.1 U/mg and that of CBD-GDH was 22.6 U/mg. AZR-CBD and CBD-GDH bound strongly to 0.5 % swollen cellulose at approximately 95 % and 98 % of the initial protein amounts, respectively. After immobilization onto the swollen cellulose, AZR-CBD and CBD-GDH retained their catalytic activity. Both enzymes bound weakly to 0.5 % microcrystalline cellulose, but the addition of a high concentration of microcrystalline cellulose (10 %) improved the binding rate of both enzymes. A reactor for flow injection analysis was filled with microcrystalline cellulose-immobilized AZR-CBD and CBD-GDH. This flow injection analysis system was successfully applied for the determination of glucose, and a linear calibration curve was observed in the range of approximately 0.16–2.5 mM glucose, with a correlation coefficient, r, of 0.998.
Kazuhiro Chiku, Mami Wada, Haruka Atsuji, Arisa Hosonuma, Mitsuru Yoshida, Hiroshi Ono, Motomitsu Kitaoka
Journal of Applied Glycoscience, Volume 66, pp 1-9; doi:10.5458/jag.jag.jag-2018_0002

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Kenji Yamagishi, Masakazu Ike, Di Guan, Ken Tokuyasu
Journal of Applied Glycoscience, Volume 66, pp 11-19; doi:10.5458/jag.jag.jag-2018_0003

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Taisuke Watanabe, Masashi Nasukawa, Yuki Yoshida, Takashi Kogo, Jun Ogihara, Takafumi Kasumi
Journal of Applied Glycoscience; doi:10.5458/jag.jag.jag-2018_0004

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