The proteinaceous inhibitor of limit dextrinase in barley and malt

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1696, Issue 2, 2004, Pages 165-170

  MacGregor, E Ann ^a  

^a NONE   (United Kingdom)

Author keywords

Barley; Complex formation; Inhibitor specificity; Limit dextrinase; Limit dextrinase inhibitor

Indexed keywords

CYSTEINE; DEXTRINASE INHIBITOR; ENZYME INHIBITOR; GLUTATHIONE; OLIGOSACCHARIDE; POLYSACCHARIDE; PULLULANASE; STARCH; THIOL GROUP; UNCLASSIFIED DRUG;

BARLEY; CATALYSIS; CHEMICAL BOND; COMPLEX FORMATION; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME INHIBITOR INTERACTION; ENZYME ISOLATION; ENZYME SPECIFICITY; GERMINATION; HYDROLYSIS; INHIBITION KINETICS; MALT; PRIORITY JOURNAL; REVIEW; SEED KERNEL; SEQUENCE HOMOLOGY; THREE DIMENSIONAL IMAGING;

HORDEUM VULGARE SUBSP. VULGARE;

EID: 1042266306     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.09.018     Document Type: Review

References (42)

1. MacGregor E.A. Limit dextrinase/pullulanase. Whitaker J.R., Voragen A.G.J., Wong D.W.S. Handbook of Food Enzymology. 2003;739-749 Marcel Dekker, New York.
2. Bryce J.H. Limit dextrinase. Whitaker J.R., Voragen A.G.J., Wong D.W.S. Handbook of Food Enzymology. 2003;751-759 Marcel Dekker, New York.
3. Yamada J. Purification of oat debranching enzyme and occurrence of inactive debranching enzyme in cereals. Agric. Biol. Chem. 45:1981;1013-1015.
4. Lenoir P., MacGregor A.W., Moll M., Daussant J. Identification de la R-enzyme de l'orge et du malt par focalisation isoelectrique. C. R. Acad. Sci., Paris. 298(III):1984;243-248.
5. Lauriere C., Mayer C., Renard H., MacGregor A., Daussant J. Maturation du caryopse d'orge: evolution des isoformes des α- et β-amylases, de l'enzyme debranchante, de l'inhibiteur d'α-amylases chez plusieurs varieties. Proceedings of the 20th Congress. 1985;675-682 European Brewery Convention, Helsinki, Finland.
6. Longstaff M.A., Bryce J.H. Levels of limit dextrinase activity in malting barley. Proceedings of the 23rd Congress. 1991;593-600 European Brewery Convention, Lisbon, Portugal.
7. Sissons M.J., Lance R.C.M., Wallace W. Bound and free forms of barley limit dextrinase. Cereal Chem. 71:1994;520-521.
8. Longstaff M.A., Bryce J.H. Development of limit dextrinase in germinated barley (Hordeum vulgare L.). Plant Physiol. 101:1993;881-889.
9. Sissons M.J. Studies on the activation and release of bound limit dextrinase in malted barley. J. Am. Soc. Brew. Chem. 54:1996;19-25.
10. Macri L.J., Macgregor A.W., Schroeder S.W., Bazin S.L. Detection of a limit dextrinase inhibitor in barley. J. Cereal Sci. 18:1993;103-106.
11. MacGregor A.W., Macri L.J., Schroeder S.W., Bazin S.L. Purification and characterisation of limit dextrinase inhibitors from barley. J. Cereal Sci. 20:1994;33-41.
12. Wong J.H., Jiao J.-A., Kobrehel K., Buchanan B.B. Thioredoxin-dependent deinhibition of pullulanase of barley malt by inactivation of a specific inhibitor protein. Plant Physiol. 108:1995;67. (abstr. no. 292).
13. McCleary B.V. Measurement of the content of limit-dextrinase in cereal flours. Carbohydr. Res. 227:1992;257-268.
14. MacGregor A.W., Bazin S.L., Schroeder S.W. Effect of starch hydrolysis products on the determination of limit dextrinase and limit dextrinase inhibitors in barley and malt. J. Cereal Sci. 35:2002;17-28.
15. Macgregor A.W., Macri L.J., Schroeder S.W., Bazin S.L. Limit dextrinase from malted barley: extraction, purification and characterization. Cereal Chem. 71:1994;610-617.
16. MacGregor E.A., Bazin S.L., Ens E.W., Lahnstein J., Macri L.J., Shirley N.J., MacGregor A.W. Structural models of limit dextrinase inhibitors from barley. J. Cereal Sci. 31:2000;79-90.
17. Lazaro A., Rodriguez-Palenzuela P., Marana C., Carbonero P., Garcia-Olmedo F. Signal peptide homology between sweet potato thaumatin II and unrelated cereal α-amylase/trypsin inhibitors. FEBS Lett. 239:1988;147-150.
18. Campos F.A.P., Richardson M. The complete amino acid sequence of the bifunctional alpha-amylase/trypsin inhibitor from seeds of ragi (Indian finger millet Eleusine coracana Gaertn.). FEBS Lett. 152:1983;300-304.
19. C.A. Behnke, V.C. Yee, I. Le Trong, L.C. Pedersen, R.E. Stenkamp, S.-S. Kim, G.R. Reeck, D.C. Teller, X-ray crystallographic structure determination at 1.9 Å resolution of the 14 kDa bifunctional protease and amylase inhibitor from corn, Direct submission to Protein Data Bank at URL: http://www.rcsb.org/pdb/ ; structure 1BEA (1998).
20. Maeda K., Wakabayashi S., Matsubara H. Complete amino acid sequence of an alpha-amylase inhibitor in wheat kernel (0.19-inhibitor). Biochim. Biophys. Acta. 828:1985;213-221.
21. Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Ruth F.X., Glockshuber R. A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the ragi bifunctional inhibitor at 2.5 Å resolution. Structure. 6:1998;911-921.
22. MacGregor A.W., Donald L.J., MacGregor E.A., Duckworth H.W. Stoichiometry of the complex formed by barley limit dextrinase with its endogenous inhibitor. Determination by electrospray time-of-flight mass spectrometry. J. Cereal Sci. 37:2003;357-362.
23. Strobl S., Muhlhahn P., Bernstein R., Wiltschek R., Maskos K., Wunderlich M., Huber R., Glockshuber R., Holak T.A. Determination of the three-dimensional structure of the bifunctional α-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy. Biochemistry. 34:1995;8281-8293.
24. Gourinath S., Alam N., Srinivasan A., Betzel C., Singh T.P. Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 Å resolution. Acta Crystallogr. D56:2000;287-293.
25. Oda Y., Matsunaga T., Fukuyama K., Miyazaki T., Morimoto T. Tertiary and quaternary structures of 0.19 α-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 Å resolution. Biochemistry. 36:1997;13503-13511.
26. Kristensen M., Planchot V., Abe J., Svensson B. Large-scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family. Cereal Chem. 75:1998;473-479.
27. Kristensen M., Lok F., Planchot V., Svendsen I., Leah R., Svensson B. Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley. Biochim. Biophys. Acta. 1431:1999;538-546.
28. Burton R.A., Zhang X.-Q., Hrmova M., Fincher G.B. A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol. 119:1999;859-871.
29. Coutinho P.M., Henrissat B. Carbohydrate-active enzymes: an integrated database approach. Gilbert H.J., Davies G.J., Henrissat B., Svensson B. Recent Advances in Carbohydrate Bioengineering. 1999;3-12 The Royal Society, Cambridge. The server can be found at URL: http://afmb.cnrs-mrs.fr/CAZY/.
30. Bryce J.H., Kim N.J., Zammit R., McCafferty C.A., Pinheiro M.G.M., Kendall G.L. Branched dextrins in wort - is their presence inevitable? Proceedings of the 25th Congress. 1995;285-292 European Brewery Convention, Brussels, Belgium.
31. 8-barrel domain and evolutionary relationship to other amylolytic enzymes. J. Protein Chem. 12:1993;791-805.
32. MacGregor E.A., Janecek S., Svensson B. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta. 1546:2001;1-20.
33. Alam N., Gourinath S., Dey S., Srinivasan A., Singh T.P. Substrate-inhibitor interactions in the kinetics of α-amylase inhibition by ragi α-amylase/trypsin inhibitor (RATI) and its various N-terminal fragments. Biochemistry. 40:2001;4229-4233.
34. Sissons M.J., Lance R.C.M., Sparrow D.H.B. Studies on limit dextrinase in barley: 3. Limit dextrinase in developing kernels. J. Cereal Sci. 17:1993;19-24.
35. MacGregor A.W., Macri L.J., Bazin S.L., Sadler G.W. Limit dextrinase inhibitor in barley and malt and its possible role in malting and brewing. Proceedings of the 25th Congress. 1995;185-192 European Brewery Convention, Brussels, Belgium.
36. Burton R.A., van Wegen S.M., Macgregor A.W., Fincher G.B. The limit dextrinase enzyme and its inhibitor in barley. Proceedings of the 8th Barley Genetics Symposium. 2000;223-224 Department of Plant Science, University of Adelaide, Glen Osmond, Adelaide, Australia.
37. Schroeder S.W., MacGregor A.W. Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues. J. Am. Soc. Brew. Chem. 56:1998;32-37.
38. McCafferty C.A., Perch-Nielsen N., Bryce J.H. Effects of aerobic and anaerobic germination on the debranching enzyme, limit dextrinase, in barley malt. J. Am. Soc. Brew. Chem. 58:2000;47-50.
39. Enevoldsen B.S. Degradation of starch by amylases in beer brewing. J. Jpn. Soc. Starch Sci. 25:1978;89-99.
40. Sissons M., Taylor M., Proudlove M. Barley malt limit dextrinase: its extraction, heat stability, and activity during malting and mashing. J. Am. Soc. Brew. Chem. 53:1995;104-110.
41. Walker J.W., Bringhurst T.A., Broadhead A.L., Brosnan J.M., Pearson S.Y. The survival of limit dextrinase during fermentation in the production of Scotch whisky. J. Inst. Brew. 107:2001;99-106.
42. Bringhurst T.A., Broadhead A.L., Brosnan J.M., Pearson S.Y., Walker J.W. The identification and behaviour of branched dextrins in the production of Scotch whisky. J. Inst. Brew. 107:2001;137-149.