Monitoring the hydrolysis and transglycosylation activity of α-glucosidase from Aspergillus niger by nuclear magnetic resonance spectroscopy and mass spectrometry

Analytical Biochemistry

Volumn 393, Issue 1, 2009, Pages 23-28

  Shimba, Nobuhisa ^a   Shinagawa, Mai ^a   Hoshino, Wataru ^a   Yamaguchi, Hideyuki ^a   Yamada, Naoyuki ^a   Suzuki, Ei ichiro ^a  

^a AJINOMOTO CO INC   (Japan)

Author keywords

Glucose; Glucosidase; HSQC; Mass spectrometry; NMR; Oligosaccharide; 1,4 Linkage; 1,6 Linkage

Indexed keywords

ASPERGILLUS; GLUCOSE; HYDROLYSIS; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE; OLIGOSACCHARIDES;

ANALYTICAL METHOD; ASPERGILLUS NIGER; GLUCOSIDASE; HSQC; NUCLEAR MAGNETIC RESONANCE(NMR); QUANTITATIVE ESTIMATION; TRANS GLYCOSYLATION ACTIVITY; TRANSGLUCOSYLATION;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

ALPHA GLUCOSIDASE; DEXTRANASE; OLIGOSACCHARIDE; SUGAR;

ANALYTIC METHOD; ARTICLE; ASPERGILLUS NIGER; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME GLYCOSYLATION; ENZYME MECHANISM; FRACTIONATION; MASS SPECTROMETRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; QUANTITATIVE ANALYSIS;

ASPERGILLUS NIGER;

EID: 67650944994     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.06.002     Document Type: Article

References (24)

1. Kato K., Sasakawa H., Kamiya Y., Utsumi M., Nakano M., Takahashi N., and Yamaguchi Y. 920 MHz ultra-high field NMR approaches to structural glycobiology. Biochim. Biophys. Acta 1780 (2008) 619-625
2. 13C NMR data. Carbohydr. Res. 335 (2001) 101-114
3. Jansson P.-E., Kenne L., and Widmalm G. CASPER: a computerized approach to structure determination of polysaccharides using information from NMR spectroscopy and simple chemical analyses. Carbohydr. Res. 168 (1987) 67-77
4. Jansson P.-E., Kenne L., and Widmalm G. Computer assisted structural analysis of oligosaccharides using CASPER. Anal. Biochem. 199 (1991) 11-17
5. Ao Z., Simsek S., Zhang G., Venkatachalam M., Reuhs B.L., and Hamaker B.R. Starch with a slow digestion property produced by altering its chain length, branch density, and crystalline structure. J. Agric. Food Chem. 55 (2007) 4540-4547
6. Miyano H., and Suzuki E. Nondestructive analysis of residue types in β-d-glucan derivatives by two-dimensional homonuclear Hartmann-Hahn spectroscopy. Anal. Sci. 8 (1992) 561-564
7. Miyano H., Nakagawa R., Suzuki E., and Uryu T. Analysis of residue types in curdlan sulfate by nuclear magnetic resonance. Carbohydr. Res. 235 (1992) 29-39
8. Chakraborty I., Mondal S., Pramanik M., Rout D., and Islam S.S. Structural investigation of a water-soluble glucan from an edible mushroom, Astraeus hygrometricus. Carbohydr. Res. 339 (2004) 2249-2254
9. Mansson M., Hood D.W., Moxon R., and Schweda E.K.H. Structural characterization of a novel branching pattern in the lipopolysaccharide from nontypeable Heamophilus influenzae. Eur. J. Biochem. 270 (2003) 2979-2991
10. Kjellberg A., Weintraub A., Albert M.J., and Widmalm G. Structural analysis of the O-antigenic polysaccharide from Vibrio cholerae O10. Eur. J. Biochem. 249 (1997) 758-761
11. Morelle W., and Srecker G. Structural analysis of oligosaccharide-alditols released by reductive β-elimination from oviducal mucins of Bufo fufo: characterization of the carbohydrate sequence Gal(α1-3)GalNAc(α1-3)[Fuc(α1-2)]Gal. Glycobiology 7 (1997) 777-790
12. 1H NMR. Carbohydr. Res. 266 (1995) 37-52
13. Kita A., Matsui H., Somoto A., Kimura A., Takata M., and Chiba S. Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger. Agric. Biol. Chem. 55 (1991) 2327-2335
14. Nakamura A., Nishimura I., Yokoyama A., Lee D.-G., Hidaka M., Masaki H., Kimura A., Chiba S., and Uozumi T. Cloning and sequencing of an α-glucosidase gene from Aspergillus niger and its expression in A. nidulans. J. Biotechnol. 53 (1997) 75-84
15. Chiba S. Molecular mechanism in α-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem. 61 (1997) 1233-1239
16. Pazur J.H., Cepure A., Okada S., and Forsberg L.S. Comparison of the action of glucoamylase and glucosyltransferase on d-glucose, maltose, and malto-oligosaccharides. Carbohydr. Res. 58 (1977) 193-202
17. 13C]maltose. Carbohydr. Res. 344 (2009) 460-465
18. M. Ota, T. Okamoto, W. Hoshino, H. Wakabayashi, Action of α-d-glucosidase from Aspergillus niger towards dextrin and starch, Carb. Pol. (2009), in press.
19. Shimba N., Yamada N., Yokoyama K., and Suzuki E. Enzymatic labeling of arbitrary proteins. Anal. Biochem. 301 (2002) 123-127
20. Shimba N., Yokoyama K., and Suzuki E. NMR-based screening method for transglutaminases: rapid analysis of their substrate specificities and reaction rates. J. Agric. Food Chem. 50 (2002) 1330-1334
21. Shimba N., Shinohara M., Yokoyama K., Kashiwagi T., Ishikawa K., Ejima D., and Suzuki E. Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Lett. 517 (2002) 175-179
22. Balaban R.S., and Ferretti J.A. Rates of enzyme-catalyzed exchange determined by two-dimensional NMR: a study of glucose 6-phosphate anomerization and isomerization. Proc. Natl. Acad. Sci. USA 80 (1983) 1241-1245
23. Bodenhausen G., and Ruben D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69 (1980) 185-189
24. Wang J., Jiang G., Vasanthan T., and Sporns P. MALDI-MS characterization of maltooligo/polysaccharides from debranched starch amylopectin of corn and barley. Starch 51 (1999) 243-248