Maltose Effects on Barley Malt Diastatic Power Enzyme Activity and Thermostability at High Isothermal Mashing Temperatures: II. α-AmylaseFootnote¹

1 Mention of a proprietary product does not constitute a guarantee or warranty of the product by the U.S. Department of Agriculture and does not imply its approval to the exclusion of other suitable products.

Literature Cited

• Ajandouz, E. H., Abe, J., Svensson, B., and Marchis-Mouren, G. Barley malt-α-amylase: Purification, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substrates. Biochem. Biophys. Acta 1159:193–202, 1992.
   PubMed Web of Science ®Google Scholar
• Al Kazaz, M., Desseaux, V., Marchis-Mouren, G., Prodanov, E., and Santimone, M. The mechanism of porcine pancreatic α-amylase inhibition of maltopentaose hydrolysis by acarbose, maltose, and maltotriose. Eur. J. Biochem. 252:100–107, 1998.
   Google Scholar
• Alves Jr., S. L., Herberts, R. A., Hollatz, C., Miletti, L. C., and Stambuk, B. Maltose and maltotriose active transport and fermentation by Saccharomyces cerevisiae. J. Am. Soc. Brew. Chem. 65:99–104, 2007.
   Web of Science ®Google Scholar
• American Society of Brewing Chemists. Methods of Analysis, 8th ed. Malt-4 Extract; −6A Diastatic power. ASBC, St. Paul, MN, 1992.
   Google Scholar
• Arakawa, T., and Timasheff, S. N. The stabilization of proteins by osmolytes. Biophys. J. 47:411–414, 1985.
   PubMed Web of Science ®Google Scholar
• Arakawa, T., and Timasheff, S. N. Stabilization of protein structure by sugars. Biochemistry 21:6536–6544, 1982.
   PubMed Web of Science ®Google Scholar
• Bamforth, C. W. Barley and malting. In: Scientific Principles of Malting and Brewing. American Society of Brewing Chemists, St. Paul, MN, pp. 21–44, 2006.
   Google Scholar
• Bamforth, C. W. The components of barley and their degradation during malting and mashing. In: Scientific Principles of Malting and Brewing. American Society of Brewing Chemists, St. Paul, MN, pp. 45–57, 2006.
   Google Scholar
• Bamforth, C. W. Current perspectives on the role of enzymes in brewing. J. Cereal Sci. 50:353–357, 2009.
   Web of Science ®Google Scholar
• Beers, E. P., and Duke, S. H. Characterization of α-amylase from shoots and cotyledons of pea (Pisum sativum L.) seedlings. Plant Physiol. 92:1154–1163, 1990.
   PubMed Web of Science ®Google Scholar
• Bertoft, B., Andtfolk, C., and Kulp, S. E. Effect of pH, temperature, and calcium ions on barley malt isoenzymes. J. Inst. Brew. 90:298–302, 1984.
   Web of Science ®Google Scholar
• Briggs, D. E. The biochemistry of malting. In: Malts and Malting. Blackie Academic & Professional, London, pp. 133–228, 1998.
   Google Scholar
• Carninci, P., Nishiyama, Y., Westover, A., Itoh, M., Nagaoka, S., Sasaki, N., Okazaki, Y., Muamatsu, M., and Hayashizaki, Y. Thermostabilization and thermoactivation of thermolabile enzymes by trehalose and its application for the synthesis of full length cDNA. Proc. Natl. Acad. Sci. U.S.A. 95:520–524, 1998.
   PubMed Web of Science ®Google Scholar
• Commuri, P. D, and Duke, S. H. Apoplastic α-amylase in pea is enhanced by heat stress. Plant Cell Physiol. 38:625–630, 1997.
   Web of Science ®Google Scholar
• Coventry, S. J., Collins, H. M., Barr, A. R., Jefferies, S. P., Chalmers, K. J., Logue, S. J., and Langridge, P. Use of putative QTLs and structural genes in marker assisted selection for diastatic power in malting barley (Hordeum vulgare L.). Aust. J. Agric. Res. 54:1241–1250, 2003.
   Google Scholar
• Delcour, J. A., and Verschaeve, S. G. Malt diastatic activity. II. A modified EBC-diastatic power assay for the selective estimation of β-amylase activity: Time and temperature dependence of the release of reducing sugars. J. Inst. Brew. 93:296–301, 1987.
   Web of Science ®Google Scholar
• Doehlert, D. C., and Duke, S. H. Specific determination of α-amylase activity crude plant extracts containing β-amylase. Plant Physiol. 71:229–234, 1983.
   PubMed Web of Science ®Google Scholar
• Doyle, E. A., Lane, A. M., Sides, J. M., Mudgett, M. B., and Monroe, J. D. An alpha-amylase (At4g25000) in Arabidopsis leaves is secreted and induced by biotic and abiotic stress. Plant Cell Environ. 30:388–398, 2007.
   PubMed Web of Science ®Google Scholar
• Duke, S. H., and Duke, S. O. In vitro nitrate reductase activity and in vivo phytochrome measurements of maize seedlings as affected by various light treatments. Plant Cell Physiol. 19:481–489, 1978.
   Web of Science ®Google Scholar
• Duke, S. H., and Henson, C. A. Green malt osmolyte concentration as an early indicator of finished malt quality. J. Am. Soc. Brew. Chem. 65:145–150, 2007.
   Web of Science ®Google Scholar
• Duke, S. H., and Henson, C. A. A comparison of barley malt quality measurements and malt sugar concentrations. J. Am. Soc. Brew. Chem. 66:151–161, 2008.
   Web of Science ®Google Scholar
• Duke, S. H., and Henson, C. A. A comparison of barley malt amylolytic enzyme activities as indicators of malt sugar concentrations. J. Am. Soc. Brew. Chem. 67:99–111, 2009.
   Web of Science ®Google Scholar
• Duke, S. H., and Henson, C. A. A comparison of barley malt osmolyte concentrations and standard malt quality measurements as indicators of barley malt amylolytic enzyme activities. J. Am. Soc. Brew. Chem. 67:206–216, 2009.
   Web of Science ®Google Scholar
• Duke, S. H., and Henson, C. A. Tracking the progress of wort sugar production during Congress mashing with North American barley cultivars and comparisons to wort osmolyte concentrations and malt extract. J. Am. Soc. Brew. Chem. 69:200–213, 2011.
   Web of Science ®Google Scholar
• Duke, S. H., Henson, C. A., and Vinje, M. A. Comparisons of barley malt amylolytic enzyme thermostabilities to wort osmolyte concentrations, malt extract, ASBC measures of malt quality, and initial enzyme activities. J. Am. Soc. Brew. Chem. 72:271–284, 2014.
   Web of Science ®Google Scholar
• Duke, S. H., Schrader, L. E., and Miller, M. G. Low temperature effects on soybean (Glycine max [L.] Merr. cv. Wells) mitochondrial respiration and several dehydrogenases during imbibition and germination. Plant Physiol. 60:716–722, 1977.
   PubMed Web of Science ®Google Scholar
• Duke, S. H., Vinje, M. A., and Henson, C. A. Tracking amylolytic enzyme activities during Congress mashing with North American barley cultivars: Comparisons of patterns of activity and β-amylases with differing Bmy1 intron III alleles and correlations of amylolytic enzyme activities. J. Am. Soc. Brew. Chem. 70:10–28, 2012.
   Web of Science ®Google Scholar
• Duke, S. H., Vinje, M. A., and Henson, C. A. Comparisons of amylolytic enzyme activities and β-amylases with differing Bmy1 intron III alleles to sugar production during Congress mashing with North American barley cultivars. J. Am. Soc. Brew. Chem. 70:230–248, 2012.
   Web of Science ®Google Scholar
• Duke, S. H., Vinje, M. A., and Henson, C. A. Comparisons of amylolytic enzyme activities and β-amylases with differing Bmy1 intron III alleles to osmolyte concentration and malt extract during Congress mashing with North American barley cultivars. J. Am. Soc. Brew. Chem. 71:193–207, 2013.
   Web of Science ®Google Scholar
• Ekberg, J., Rautio, J., Mattinen, L., Vidgren, V., Londesborough, J., and Gibson, B. R. Adaptive evolution of the lager brewing yeast Saccharomyces pastorianus for improved growth under hyperosmotic conditions and its influence on fermentation performance. Fed. Eur. Microbiol. Soc. Yeast Res. 13:335–349, 2013.
   Google Scholar
• Ellis, R. J. Macromolecular crowding: Obvious but underappreciated. Trends Biochem. Sci. 26:597–604, 2001.
   PubMed Web of Science ®Google Scholar
• European Brewery Convention. Analytica–EBC. Fachverlag Hans Carl, Nürnberg, Germany, 2010.
   Google Scholar
• Evans, D. E., Li, C., and Eglinton, J. K. The properties and genetics of barley malt starch degrading enzymes. In: Genetics and Improvement of Barley Malt Quality, G. Zhang and C. Li, eds. Springer-Verlag, Berlin, and Zhejiang University Press, Hangzhou, China, pp. 143–189, 2009.
   Google Scholar
• Evans, D. E., Li, C., and Eglinton, J. K. Improved prediction of malt fermentability by measurement of the diastatic power enzymes β-amylase, α-amylase, and limit dextrinase: I. Survey of the levels of diastatic power enzymes in commercial malts. J. Am. Soc. Brew. Chem. 66:223–232, 2008.
   Web of Science ®Google Scholar
• Evans, D. E., Wallace, W., Lance, R. C. M., and MacLeod, L. C. Measurement of beta-amylase in malting barley (Hordeum vulgare L.). II. The effect of germination and kilning. J. Cereal Sci. 26:241–1250, 1997.
   Web of Science ®Google Scholar
• Evans, D. E., van Wegen, B., Ma, Y., and Eglinton, J. The impact of the thermostability of α-amylase, β-amylase, and limit dextrinase on potential wort fermentability. J. Am. Soc. Brew. Chem. 61:210–218, 2003.
   Web of Science ®Google Scholar
• Filichkin T. P., Vinje, M. A., Budde A. D., Corey A. E., Duke S. H., Gallagher, L. W., Helgesson, J., Henson, C. A., Obert, D. E., Ohm, J. B., Petrie, S. E., Ross, A. S., and Hayes, P. M. Phenotypic variation for diastatic power, β-amylase activity, and thermostability vs. Bmy1 allelic variation in North American barley. Crop Sci. 50:826–834, 2010.
   Web of Science ®Google Scholar
• Frigon, R. P., and Lee, J. C. The stabilization of calf-brain microtubule protein by sucrose. Arch. Biochem. Biophys. 153:587–589, 1972.
   PubMed Web of Science ®Google Scholar
• Gibson, T. S., Solah, V., Holmes, M. R. G. and Taylor, H. R. Diastatic power in malted barley—Contributions of malt parameters to its development and the potential of barley grain β-amylase to predict malt diastatic power. J. Inst. Brew. 101:277–280, 1995.
   Web of Science ®Google Scholar
• Henson, C. A., and Duke, S. H. Osmolyte concentration as an indicator of malt quality. J. Am. Soc. Brew. Chem. 65:59–62, 2007.
   Web of Science ®Google Scholar
• Henson, C. A., and Duke, S. H. A comparison of standard and non-standard measures of malt quality. J. Am. Soc. Brew. Chem. 66:11–19, 2008.
   Web of Science ®Google Scholar
• Henson, C. A., and Duke, S. H. Maltose effects on barley malt diastatic power enzyme activity and thermostability at high isothermal mashing temperatures: I. β-Amylase. J. Am. Soc. Brew. Chem. 74:100–112, 2016.
   Web of Science ®Google Scholar
• Henson, C. A., Duke, S. H., and Vinje, M. A. A comparison of barley malt amylolytic enzyme thermostabilities and wort sugars produced during mashing. J. Am. Soc. Brew. Chem. 72:51–65, 2014.
   Web of Science ®Google Scholar
• Huuskonen, A., Markkula, T., Vidgren, V., Lima, L., Mulder, L., Geurts, W., Walsh, V., and Londesborough, J. Selection from industrial lager yeast strains of variants with improved fermentation performance in very-high gravity worts. Appl. Environ. Microbiol. 76:1563–1573, 2010.
   PubMed Web of Science ®Google Scholar
• Kaplan, F., and Guy, C. L. β-Amylase induction and the protective role of maltose during temperature shock. Plant Physiol. 135:l674–1684, 2004.
   Web of Science ®Google Scholar
• Kuntz, R. J., and Bamforth, C. W. Time course for the development of enzymes in barley. J. Inst. Brew. 113:196–205, 2007.
   Web of Science ®Google Scholar
• Kuo, T.-M., Warner, R. L., and Kleinhofs, A. In vitro stability of nitrate reductase from barley leaves. Phytochemistry 21:531–533, 1982.
   Web of Science ®Google Scholar
• Lizotte, P. A., Henson, C. A., and Duke, S. H. Purification and characterization of pea epicotyl β-amylase. Plant Physiol. 92:615–621, 1990.
   PubMed Web of Science ®Google Scholar
• MacGregor, A. W. α-Amylase I from malted barley—Physical properties and action pattern on amylose. Cereal Chem. 55:754–765, 1978.
   Web of Science ®Google Scholar
• MacGregor, A. W., Marchylo, B. A., and Kruger, J. E. Multiple α-amylase components in germinated cereal grains determined by isoelectric focusing and chromatofocusing. Cereal Chem. 65:326–333, 1988.
   Web of Science ®Google Scholar
• MacGregor, A. W., Morgan, J. E., and MacGregor, E. A. The action of germinated barley alpha-amylases on linear maltodextrins. Carbohydr. Res. 227:301–313, 1992.
   Web of Science ®Google Scholar
• MacGregor, E. A., MacGregor, A. W., Macri, L. J., and Morgan, J. E. Models for the action of alpha-amylase isozymes on linear substrates. Carbohydr. Res. 257:249–268, 1994.
   PubMed Web of Science ®Google Scholar
• Minton, A. P. Effects of concentrated “inert” macromolecular cosolute on the stability of globular protein with respect to denaturation by heat and by chaotropes; a statistical-thermodynamic model. Biophys. J. 78:101–109, 2000.
   PubMed Web of Science ®Google Scholar
• Moreira, F. G., Lenartovicz, V., and Peralta, R. M. A thermostable maltose-tolerant α-amylase from Aspergillus tamari. J. Basic Microbiol. 44:29–35, 2004.
   PubMed Web of Science ®Google Scholar
• Muller, R. The effects of mashing temperature and mash thickness on wort carbohydrate composition. J. Inst. Brew. 97:85–92, 1991.
   Web of Science ®Google Scholar
• Muslin, E. H., Karpelenia, C. B., and Henson, C. A. The impact of thermostable α-glucosidase on the production of fermentable sugars during mashing. J. Am. Soc. Brew. Chem. 61:142–145, 2003.
   Web of Science ®Google Scholar
• Neucere, N. J., and St. Angelo, A. J. Physicochemical properties of peanut proteins in sucrose. Anal. Biochem. 47:80–89, 1972.
   PubMed Web of Science ®Google Scholar
• Phiarais, B. P. N., Wijngaard, H. H., and Arendt, E. K. The impact of kilning on enzymatic activity of buckwheat malt. J. Inst. Brew. 111:290–298, 2005.
   Web of Science ®Google Scholar
• Rogers, J. C. Two barley α-amylase gene families are regulated differently in aleurone cells. J. Biol. Chem. 260:3731–3738, 1985.
   PubMed Web of Science ®Google Scholar
• Santos, M. M. M., and Riis, P. Optimized McCleary method for measurement of total β-amylase in barley and its applicability. J. Inst. Brew. 102:271–275, 1996.
   Web of Science ®Google Scholar
• Schrader, L. E., Cataldo, D. A., and Peterson, D. M. Use of protein in extraction and stabilization of nitrate reductase. Plant Physiol. 53:688–690, 1974.
   PubMed Web of Science ®Google Scholar
• Sola-Penna, M., and Meyer-Fernandes, J. R. Stabilization against thermal inactivation promoted by sugars on enzyme structure and function: Why is trehalose more effective than other sugars? Arch. Biochem. Biophys. 360:10–14, 1998.
   PubMed Web of Science ®Google Scholar
• Stewart, G. G. High-gravity brewing and distilling—Past experiences and future prospects. J. Am. Soc. Brew. Chem. 68:1–9, 2010.
   Web of Science ®Google Scholar
• Sun, Z., and Henson, C. A. A quantitative assessment of the importance of barley seed α-amylase, β-amylase, debranching enzyme, and α-glucosidase in starch degradation. Arch. Biochem. Biophys. 284:298–305, 1991.
   PubMed Web of Science ®Google Scholar
• Vinje, M. A., Duke, S. H., and Henson, C. A. Comparison of factors involved in starch degradation in barley germination under laboratory and malting conditions. J. Am. Soc. Brew. Chem. 73:195–205, 2015.
   Web of Science ®Google Scholar
• Yamasaki, Y. β-Amylase in germinating millet. Phytochemistry 64:935–939, 2003.
   PubMed Web of Science ®Google Scholar
• Yancey, P. H., Clark, M. E., Hand, S. C., Bowlus, R. D., and Somero, G. N. Living in a water system: Evolution of osmolyte systems. Science 217:1214–1222, 1982.
   PubMed Web of Science ®Google Scholar
• Young, R. A., and Briggs, D. E. Stability of α-amylase in model brewery mashes. J. Sci. Food Agric. 20:272–275, 1969.
   Web of Science ®Google Scholar
• Yu, Z., Zhao, M., Li, H., Zhao, H., Zhang, Q., Wan, Q., and Li, H. A comparative study on physiological activities of lager and ale brewing yeasts under different gravity conditions. Biotechnol. Bioprocess Eng. 17:818–826, 2012.
   Web of Science ®Google Scholar
• Zancan, P., and Sola-Pena, M. Trehalose and glycerol stabilize and renature yeast inorganic pyrophosphatase inactivated by very high temperatures. Arch. Biochem. Biophys. 444:52–60, 2005.
   PubMed Web of Science ®Google Scholar