Characterization of a Glycoside Hydrolase Family 31 α-Glucosidase Involved in Starch Utilization in Podospora anserina
作者： Kyung-Mo SONG , Masayuki OKUYAMA , Kazuyuki KOBAYASHI , Haruhide MORI , Atsuo KIMURA
DOI: 10.1271/BBB.130545
关键词:
摘要: For Podospora anserina, several studies of cellulolytic enzymes have been established, but characteristics amylolytic are not well understood. When P. anserina grew in starch as carbon source, it accumulated glucose, nigerose, and maltose the culture supernatant. At same time, fungus secreted α-glucosidase (PAG). PAG was purified from supernatant, found to convert soluble nigerose maltose. The recombinant enzyme with C-terminal His-tag (rPAG) produced Pichia pastoris. Most rPAG under standard conditions lost its affinity for nickel-chelating resin, improved by use a buffered medium (pH 8.0) supplemented casamino acid reduction cultivation time. suffered limited proteolysis at site original PAG. A site-directed mutagenesis study indicated that had no effect on characteristics. kinetic possessed significant transglycosy...
sci-hub.se 参考文章(33)
Takeshi Yamamoto, Takehiro Unno, Yoshimi Watanabe, Mikio Yamamoto, Masayuki Okuyama, Haruhide Mori, Seiya Chiba, Atsuo Kimura, Purification and characterization of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage Biochimica et Biophysica Acta. ,vol. 1700, pp. 189- 198 ,(2004) , 10.1016/J.BBAPAP.2004.05.002
Nobuhisa Shimba, Mai Shinagawa, Wataru Hoshino, Hideyuki Yamaguchi, Naoyuki Yamada, Ei-ichiro Suzuki, Monitoring the hydrolysis and transglycosylation activity of α-glucosidase from Aspergillus niger by nuclear magnetic resonance spectroscopy and mass spectrometry Analytical Biochemistry. ,vol. 393, pp. 23- 28 ,(2009) , 10.1016/J.AB.2009.06.002
Joan Lin-Cereghino, William W. Wong, See Xiong, William Giang, Linda T. Luong, Jane Vu, Sabrina D. Johnson, Geoff P. Lin-Cereghino, Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris BioTechniques. ,vol. 38, pp. 44- 48 ,(2005) , 10.2144/05381BM04
K. L. Petersen, J. Lehmbeck, T. Christensen, A new transcriptional activator for amylase genes in Aspergillus. Molecular Genetics and Genomics. ,vol. 262, pp. 668- 676 ,(1999) , 10.1007/S004380051129
Takashi NAKAMURA, Yuki MAEDA, Nami TANOUE, Tomohiro MAKITA, Masashi KATO, Tetsuo KOBAYASHI, Expression profile of amylolytic genes in Aspergillus nidulans. Bioscience, Biotechnology, and Biochemistry. ,vol. 70, pp. 2363- 2370 ,(2006) , 10.1271/BBB.50694
Min-Sun Kang, Masayuki Okuyama, Haruhide Mori, Atsuo Kimura, The first α-1,3-glucosidase from bacterial origin belonging to glycoside hydrolase family 31 Biochimie. ,vol. 91, pp. 1434- 1442 ,(2009) , 10.1016/J.BIOCHI.2009.07.018
Rie Kawai, Kiyohiko Igarashi, Motomitsu Kitaoka, Tadashi Ishii, Masahiro Samejima, Kinetics of substrate transglycosylation by glycoside hydrolase family 3 glucan (1→3)-β-glucosidase from the white-rot fungus Phanerochaete chrysosporium Carbohydrate Research. ,vol. 339, pp. 2851- 2857 ,(2004) , 10.1016/J.CARRES.2004.09.019
Yoshio TANAKA, Tsunehiro AKI, Yûki HIDAKA, Yûji FURUYA, Seiji KAWAMOTO, Seiko SHIGETA, Kazuhisa ONO, Osamu SUZUKI, Purification and Characterization of a Novel Fungal α-Glucosidase from Mortierella alliacea with High Starch-hydrolytic Activity Bioscience, Biotechnology, and Biochemistry. ,vol. 66, pp. 2415- 2423 ,(2002) , 10.1271/BBB.66.2415
L. Poidevin, J. Feliu, A. Doan, J.-G. Berrin, M. Bey, P. M. Coutinho, B. Henrissat, E. Record, S. Heiss-Blanquet, Insights into Exo- and Endoglucanase Activities of Family 6 Glycoside Hydrolases from Podospora anserina Applied and Environmental Microbiology. ,vol. 79, pp. 4220- 4229 ,(2013) , 10.1128/AEM.00327-13
Katsuya GOMI, Terumi AKENO, Toshitaka MINETOKI, Kenji OZEKI, Chieko KUMAGAI, Naoto OKAZAKI, Yuzuru IIMURA, Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae Bioscience, Biotechnology, and Biochemistry. ,vol. 64, pp. 816- 827 ,(2000) , 10.1271/BBB.64.816