Biochemical characterization of Aspergillus awamori exoinulinase: Substrate binding characteristics and regioselectivity of hydrolysis

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1650, Issue 1-2, 2003, Pages 22-29

  Kulminskaya, Anna A ^a   Arand, Michael ^b   Eneyskaya, Elena V ^a   Ivanen, Dina R ^a   Shabalin, Konstantin A ^a   Shishlyannikov, Sergei M ^a   Saveliev, Andrew N ^c   Korneeva, Olga S ^d   Neustroev, Kirill N ^a  

^a PETERSBURG NUCLEAR PHYSICS INSTITUTE   (Russian Federation)

^b UNIVERSITY OF WÜRZBURG   (Germany)

^c PETER THE GREAT ST PETERSBURG POLYTECHNIC UNIVERSITY   (Russian Federation)

^d VORONEZH STATE UNIVERSITY OF ENGINEERING TECHNOLOGIES   (Russian Federation)

Author keywords

Exoinulinase; Fructooligosaccharide; Fructosyl binding site; Multiple attack

Indexed keywords

EXOINULINASE; FRUCTOSE; FRUCTOSE OLIGOSACCHARIDE; FUNGAL ENZYME; HEXOSE; INULINASE; OLIGOSACCHARIDE; PENTOSE; UNCLASSIFIED DRUG; GLYCOSIDASE; INULIN;

ARTICLE; ASPERGILLUS AWAMORI; BINDING SITE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE COMPLEX; GLYCOSYLATION; HYDROLYSIS; NUCLEAR MAGNETIC RESONANCE; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; ASPERGILLUS; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; TIME;

ASPERGILLUS; ASPERGILLUS AWAMORI; FELIS CATUS;

ASPERGILLUS; BINDING SITES; GLYCOSIDE HYDROLASES; HYDROLYSIS; INULIN; MAGNETIC RESONANCE SPECTROSCOPY; TIME FACTORS;

EID: 0141976294     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00187-0     Document Type: Article

References (34)

1. Menne E., Guggenbuhl N., Roberfroid M. Fn-type chicory inulin hydrolysate has a prebiotic effect in humans. J. Nutr. 130:2000;1197-1199.
2. Carabin I.G., Flamm W.G. Evaluation of safety of inulin and oligofructose as dietary fiber. Regul. Toxicol. Pharmacol. 30:1999;268-282.
3. Hidaka H., Eida T., Saitoh Y. Industrial production of fructo-oligosaccharides and its application for human and animals. Nippon Nogeikagaku Kaishi (in Japanese). 61:1987;915-923.
4. Vijn I., Smeekens S. Fructans: more than a reserve carbohydrate? Plant Physiol. 120:1999;351-359.
5. Kaur N., Kaur M., Gupta A.K., Singh R. Properties of β-fructosidase (invertase and inulinase) of Fusarium oxysporum growth on an aqueous extract of Cichorium intybus roots. J. Chem. Technol. Biotechnol. 53:1992;279-284.
6. Pandey A., Soccol C.R., Selvakumar P., Soccol V.T., Krieger N., Fontana J.D. Recent developments in microbial inulinases. Its production, properties, and industrial applications. Appl. Biochem. Biotechnol. 81:1999;35-52.
7. Baumgartner S., Praznik W. Purification of exo- and endoinulinase from crude inulinase extract for the analysis of fructans. Int. J. Biol. Macromol. 17:1995;247-250.
8. Pessoni R.A.B., Figueredo-Ribeiro R.C.L., Braga M.R. Extracellular inulinase from Penicillium janczemskii, fungus isolated from the rhizosphere of Vernonia herbacea. J. Appl. Microbiol. 87:1999;141-147.
9. Arand M., Golubev A.M., Brandao Neto J.R., Polikarpov I., Wattiez R., Korneeva O.S., Eneyskaya E.V., Kulminskaya A.A., Shabalin K.A., Shishliannikov S.M., Chepurnaya O.V., Neustroev K.N. Purification, characterisation, gene cloning, and preliminary X-ray data of the exo-inulinase from Aspergillus awamori. Biochem. J. 362:2002;131-135.
10. Yanai K., Nakane A., Kawate A., Hirayama M. Molecular cloning and characterization of the fructooligosaccharide-producing beta-fructofuranosidase gene from Aspergillus niger ATCC 20611. Biosci. Biotechnol. Biochem. 65:2001;766-773.
11. Jung Kang E., Lee S.O., Lee J.D., Lee T.H. Purification and characterization of a levanbiose-producing levanase from Pseudomonas sp. No. 43. Biotechnol. Appl. Biochem. 29:1999;263-268.
12. Hiromi K., Nitta Y., Numata C., Ono S. Subsite affinities of glucoamylase: examination of the validity of the subsite theory. Biochim. Biophys. Acta. 302:1973;362-375.
13. Kulminskaya A.A., Thomsen K.K., Shabalin K.A., Sidorenko I.A., Eneyskaya E.V., Savel'ev A.N., Neustroev K.N. Isolation, enzymatic properties, and mode of action of an exo-1,3-beta-glucanase from Trichoderma viride. Eur. J. Biochem. 268:2001;6123-6131.
14. Rehm J., Willmitzer L., Heyer A.G. Production of 1-kestose in transgenic yeast expressing a fructosyltransferase from Aspergillus foetidus. J. Bacteriol. 180:1998;1305-1310.
15. Miasnikov A.N. Characterization of a novel endo-levanase and its gene from Bacillus sp. L7. FEMS Microbiol. Lett. 154:1997;23-28.
16. 13C NMR spectroscopy. Acta Chem. Scand. 44:1990;158-160.
17. Baumgartner S., Dax T.G., Praznik W., Falk H. Characterization of the high-molecular weight fructan isolated from garlic (Allium sativum L). Carbohydr. Res. 328:2000;177-183.
18. Bruss M.L., Black A.L. Enzymatic microdetermination of glycogen. Anal. Biochem. 84:1978;309-312.
19. Akino T., Nakamara N., Horikoshi K. Characterization of β-mannosidase of an alkalophilic Bacillus sp. Agric. Biol. Chem. 52:1988;1459-1464.
20. Somogyi M. Notes on sugar determination. J. Biol. Chem. 195:1952;19-23.
21. Leatherbarrow R.T. Enzifitter. A Non-Linear Regression Data Analysis Program for IBM-PC. 1987;Elsevier Biosoft, Cambridge.
22. Hiromi K. Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme. Biochem. Biophys. Res. Commun. 40:1970;1-6.
23. Davies G.J., Wilson K.S., Henrissat B. Nomenclature for sugar-binding subsites in glycoside hydrolases. Biochem. J. 321:1997;557-559.
24. Robyt J.F., French D. Multiple attack and polarity of action of porcine pancreatic alpha-amylase. Arch. Biochem. Biophys. 138:1970;662-670.
25. Kondo H., Nakatani H., Hiromi K., Matsuno R. Multiple attack in porcine pancreatic α-amylase-catalyzed hydrolysis of amylose studied with a fluorescence probe. J. Biochem. 84:1978;403-417.
26. Bailey J.M., Whelan W.J. The mechanism of carbohydrase action: 3. The action pattern of β-amylase. Biochem. J. 67:1957;540-547.
27. Suganuma T., Ohnishi M., Hiromi K., Morita Y. Evaluation of subsite affinities of soybean β-amylase by product analysis. Agric. Biol. Chem. 44:1980;1111-1117.
28. Kondo H., Nakatani H., Matsuno R., Hiromi K. Product distribution in amylase-catalyzed hydrolysis of amylose. Comparison of experimental results with theoretical predictions. J. Biochem. 87:1980;1053-1070.
29. Bailey J.M., French D. The significance of multiple reactions in enzyme-polymer systems. J. Biol. Chem. 226:1957;1-14.
30. Hrmova M., MacGregor E.A., Biely P., Stewart R.J., Fincher G.B. Substrate binding and catalytic mechanism of a barley β-D-glucosidase/(1,4) -β-D-glucan exohydrolase. J. Biol. Chem. 273:1998;11134-11143.
31. Yazaki T., Ohnishi M., Rokushika S., Okada G. Subsite structure of the β-glucosidase from Aspergillus niger, evaluated by steady-state kinetics with cello-oligosaccharides as substrates. Carbohydr. Res. 298:1997;51-57.
32. Warchol M., Perrin S., Grill J.P., Schneider F. Characterization of a purified beta-fructofuranosidase from Bifidobacterium infantis ATCC 15697. Lett. Appl. Microbiol. 35:2002;462-467.
33. Subbs H.J., Brasch D.J., Emerson G.W., Sullivan P.A. Hydrolase and transferase activities of the β-1,3-exoglucanase of Candida albicans. Eur. J. Biochem. 263:1999;889-895.
34. Siguskjold B.W., Christensen T., Payre N., Cottaz S., Driguez H., Svensson B. Thermodynamics of binding of heterobidentate ligans consisting of spacer-connected acarbose and β-cyclodextrin to the catalytic and starch-binding domains of glucoamylase from Aspergillus niger shows that the catalytic and starch-binding sites are in close proximity in space. Biochemistry. 37:1998;10446-10452.