Portal de Periódicos da CAPES

The Relevance of Different Enzymes for the Hydrolysis of β-glucans in Malting and Mashing

2008; Wiley; Volume: 114; Issue: 3 Linguagem: Inglês

10.1002/j.2050-0416.2008.tb00332.x

2050-0416

Makoto Kanauchi, Charles W. Bamforth,

Biofuel production and bioconversion

Journal of the Institute of BrewingVolume 114, Issue 3 p. 224-229 Free Access The Relevance of Different Enzymes for the Hydrolysis of β-glucans in Malting and Mashing Makoto Kanauchi, Makoto Kanauchi Department of Food Management, Miyagi University, 2-2-1 Hatatate Taihaku-ku Sendai Miyagi, 982-0215 Japan.Search for more papers by this authorCharles W Bamforth, Corresponding Author Charles W Bamforth Department of Food Science & Technology, University of California, Davis, CA 95616-8598, USA.E-mail: [email protected]Search for more papers by this author Makoto Kanauchi, Makoto Kanauchi Department of Food Management, Miyagi University, 2-2-1 Hatatate Taihaku-ku Sendai Miyagi, 982-0215 Japan.Search for more papers by this authorCharles W Bamforth, Corresponding Author Charles W Bamforth Department of Food Science & Technology, University of California, Davis, CA 95616-8598, USA.E-mail: [email protected]Search for more papers by this author First published: 16 May 2012 https://doi.org/10.1002/j.2050-0416.2008.tb00332.xCitations: 25 AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat ABSTRACT: β-Glucosidase and to a lesser extent endo-β1–4-glucanase are present in significant quantity in raw barley. These enzymes, as well as endo-β1–3, 1–4-glucanase, endo-β1–3-glucanase and exo-β1–3-glucanase, increase in activity during steeping and germination. Exo-β1–3-glucanase stands apart through its very late development during germination and it may be a limiting enzyme in malts that have not received substantial modification. Three separate exo-glucanases were located in malt and each of them displayed a preference for β1–3 linkages. As the principle product of endo-β1–3, 1–4-glucanase is oligosaccharides with a β1–4 linkage at the non-reducing end (from which end exo enzymes approach the substrate), this is likely to be a second reason (alongside the late development of the enzyme) why such oligosaccharides survive in significant quantities into wort. A third contributing factor may be the sensitivity of the exo-glucanases to ions such as potassium, sodium and magnesium. REFERENCES 1 Bamforth, C. W., Barley β-glucans: their role in malting and brewing. Brew. Dig., 1982, 57 (6), 22–27, 35. 2 Bamforth, C. W., β-Glucan and β-glucanases in malting and brewing: practical aspects. Brew. Dig., 1994, 69 (5), 12–16, 21. 3 Bamforth, C. W., Beer: Health and Nutrition, 2004, Blackwell: Oxford. 4 Bamforth, C. W. and Gambill, S. C., Fiber and putative prebiotics in beer. J. Am. Soc. Brew. Chem., 2007, 65, 67–69. 5 Bamforth, C. W. and Kanauchi, M., A simple model for the cell wall of the starchy endosperm in barley. J. Inst. Brew., 2001, 107, 235–240. 6 Bamforth, C. W., Martin, H. L. and Wainwright, T., A role for carboxypeptidase in the solubilization of barley β-glucan? J. Inst. Brew. 1979, 85, 334–338. 7 Bamforth, C. W., Moore, J., McKillop, D., Williamson, G. and Kroon, P. A., Enzymes from barley which solubilize β-glucan. Proceedings of the European Brewery Convention Congress, Maastricht, IRL Press: Oxford, 1997, pp. 75–82. 8 Bathgate, G. N., Palmer, G. H. and Wilson, G., The action of endo-β-glucanases on barley and malt β-glucans? J. Inst. Brew. 1974, 80, 278–285. 9 Bathgate, G. N. and Dalgleish, C. E., The diversity of barley and malt β-glucans. Proceedings of the American Society of Brewing Chemists, 1974, pp. 32–36. 10 Bradford, M. M., A rapid and sensitive method for the quantitation or microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 1976, 72, 248–254. 11 Brenner, M. W., Brewing with barley. Tech. Q. Master Brew. Assoc. Am., 1972, 9, 12–17. 12 Fincher, G. B., Morphology and chemical composition of barley endosperm cell walls. J. Inst. Brew., 1975, 81, 116–122. 13 Fulcher, R. G., Setterfield, G., McCully, M. E. and Wood, P. J., Observations on the aleurone layer. II. Fluorescence microscopy of the aleurone-sub-aleurone junction with emphasis on possible β-1,3-glucan deposits in barley? Aust. J. Plant Physiol. 1977, 4, 917–928. 14 Hoy, J. L., Macauley, B. J. and Fincher, G. B., Cellulases of plant and microbial origin in germinating barley. J. Inst. Brew., 1981, 87, 77–80. 15 Hrmova, M. and Fincher, G. B., Barley β-D-glucan exohydrolases. Substrate specificity and kinetic properties. Carbohydrate Research, 1998, 305, 209–221. 16 Hrmova, M., Harvey, A. J., Wang, J., Shirley, N. J., Jones, G. P., Stone, B. A., Høj, P. B. and Fincher, G. B., Barley-β-D-glucan exohydrolases with β-glucosidase activity. Purification, characterization and determination of primary structure from a cDNA clone. J. Biol. Chem., 1996, 271, 5277–5286. 17 Hrmova, M., MacGregor, E. A., Biely, P., Stewart, R. J. and Fincher, G. B., Substrate binding and catalytic mechanism of a barley β-D-glucosidase/(1,4)-β-D-glucan exohydrolase. J. Biol. Chem., 1998, 273, 11134–11143. 18 Kanauchi, M. and Bamforth, C. W., Enzymic digestion of walls purified from the starchy endosperm of barley? J. Inst. Brew. 2002, 108, 73–77. 19 Luchsinger, W. W., English, H. and Kneen, E., Autolytic action of gumases in malting and brewing. Influence of malting and brewing on barley gums. Proceedings of the American Society of Brewing Chemists, 1958, pp. 40–46. 20 Martin, H. L. and Bamforth, C. W., An enzymic method for the measurement of total and water-soluble β-glucan in barley. J. Inst. Brew., 1981, 87, 88–91. 21 Martin, H. L. and Bamforth, C. W., Application of a radial diffusion assay for the measurement of β-glucanase in malt. J. Inst. Brew., 1983, 89, 34–37. 22 Somogyi, M., Notes on sugar determination? J. Biol. Chem. 1952, 195, 19–23. 23 Varghese, J. N., Garrett, T. P., Colman, P. M., Chen, L., Høj, P. B. and Fincher, G. B., Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities. Proc. Natl. Acad. Sci., 1994, 91, 2785–2789. 24 Woodward, J. R., Fincher, G. B. and Stone, B. A., Water soluble (1→3), (1→4)-β-D-glucans from barley (Hordeum vulgare) endosperm. II. Fine structure? Carb. Polym. 1983, 3, 207–225. 25 Yamashita, H., Uehara, H., Tsumura, Y., Hayase, F. and Kato, H., Precipitate forming reaction of β1-4-glucanase in malt? Agric. Biol. Chem. 1987, 51, 655–664. Citing Literature Volume114, Issue32008Pages 224-229 ReferencesRelatedInformation