Comparison of Diastatic Power Enzyme Release and Persistence during Modified Institute of Brewing 65°C and Congress Programmed Mashes

Literature Cited

• Arakawa, T., and Timasheff, S. N. Stabilization of protein structure by sugars. Biochemistry 21:6536–6544, 1982.
   PubMed Web of Science ®Google Scholar
• Back, J. F., Oakenfull, D., and Smith, M. B. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18:5191–5196, 1979.
   PubMed Web of Science ®Google Scholar
• Baks, T., Janssen, A. E. M., and Boom, R. M. A kinetic model to explain the maximum in α-amylase activity measurements in the presence of small carbohydrates. Biotechnol. Bioeng. 94:431–440, 2006.
   PubMed Web of Science ®Google Scholar
• Baks, T., Janssen, A. E. M., and Boom, R. M. The effect of carbohydrates on α-amylase activity measurements. Enzyme Microb. Technol. 39:114–119, 2006.
   Web of Science ®Google Scholar
• Bamforth, C. W., Barley and malt starch in brewing: A general review. Tech. Q. Master Brew. Assoc. Am. 40:89–97, 2003.
   Google Scholar
• Bathgate, G. N., and Bringhurst, T. A. Letter to the editor: Update on the knowledge regarding starch structure and degradation of malt enzymes (DP/DU and limit dextrinase). J. Inst. Brew. 117:33–38, 2011.
   Web of Science ®Google Scholar
• Bekkers, A., Vissenaekens, J., and Baks, T. Attenuation limit of malt as a function of gelatinisation characteristics of starch. In: Eur. Brew. Conv. Cong. Proc., Venice, presentation 19, 2007.
   Google Scholar
• Bendelow, V. M. Inheritance of free β-amylase in barley. Can. J. Plant Sci. 44:550–554, 1964.
   Web of Science ®Google Scholar
• Bertoft, B., Andtfolk, C., and Kulp, S.-E. Effect of pH, temperature, and calcium ions on barley malt α-amylase isoenzymes. J. Inst. Brew. 90:298–302, 1984.
   Web of Science ®Google Scholar
• Brandam, C., Meyer, X. M., Proth, J., Strehaiano, P., and Pingaud, H. An original kinetic model for the enzymatic hydrolysis of starch during mashing. Biochem. Eng. J. 13:43–52, 2003.
   Web of Science ®Google Scholar
• Briggs, D. E., Boulton, C. A., Brookes, P. A., and Stevens, R. Brewing: Science and Practice. CRC Press, Boca Raton, FL, 2004.
   Google Scholar
• Chu, S., Hasjim J., Hickey, L., Fox, G., and Gilbert, B. Structural changes of starch molecules during germination in barley grains. Cereal Chem. 91:431–437, 2014.
   Web of Science ®Google Scholar
• Cooper, C., Evans, D. E., Yousif, A., Metz, N., and Koutoulis, A. Comparison of the impact on performance of small-scale mashing with different proportions of unmalted barley, Ondea Pro®, malt and rice. J. Inst. Brew. 122:218–227, 2016.
   Web of Science ®Google Scholar
• Duke, S. H., and Henson, C. A. A comparison of barley malt proteomic enzyme activities as indicators of malt sugar concentrations. J. Am. Soc. Brew. Chem. 67:99–111, 2009.
   Web of Science ®Google Scholar
• Eglinton, J. K., Langridge, P., and Evans, D. E. Thermostability variation in alleles of barley beta-amylase. J. Cereal Sci. 28:301–309, 1998.
   Web of Science ®Google Scholar
• European Brewery Convention. Analytica–EBC. Verlag Hans Carl, Nurnberg, Germany, 1998.
   Google Scholar
• Evans, D. E. A more cost- and labor-efficient assay for the combined measurement of the diastatic power enzymes β-amylase, α-amylase, and limit dextrinase. J. Am. Soc. Brew. Chem. 66:215–222, 2008.
   Web of Science ®Google Scholar
• Evans, D. E. The impact of malt blending on lautering efficiency, extract yield, and wort fermentability. J. Am. Soc. Brew. Chem. 70:50–54, 2012.
   Web of Science ®Google Scholar
• Evans, D. E., Collins, H. M., Eglinton, J. K., and Wilhelmson, A. Assessing the impact of the level of diastatic power enzymes and their thermostability on the hydrolysis of starch during wort production to predict malt fermentability. J. Am. Soc. Brew. Chem. 63:185–198, 2005.
   Web of Science ®Google Scholar
• Evans, D. E., Dambergs, R., Ratkowsky, D., Li, C., Harasymow, S., Roumeliotis, S., and Eglinton, J. K. Refining the prediction of potential malt fermentability by including an assessment of limit dextrinase thermostability and additional measures of malt modification, using two different methods for multivariate model development. J. Inst. Brew. 116:86–97, 2010.
   Web of Science ®Google Scholar
• Evans, D. E., Goldsmith, M., Dambergs, R., and Nischwitz, R. A comprehensive revaluation of the small-scale Congress mash protocol parameters for determination of extract and fermentability. J. Am. Soc. Brew. Chem. 69:13–27, 2011.
   Web of Science ®Google Scholar
• Evans, D. E., Goldsmith, M., Redd, K. S., Nischwitz, R., and Lentini, A. Impact of mashing conditions on extract, its fermentability, and the levels of wort free amino nitrogen (FAN), β-glucan, and lipids. J. Am. Soc. Brew. Chem. 70:39–49, 2012.
   Web of Science ®Google Scholar
• Evans, D. E., Li, C., and Eglinton, J. K. A superior prediction of malt attenuation. In: Eur. Brew. Conv. Cong. Proc., Venice, presentation 4, 2007.
   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 Malting Quality. G. Zhang and C. Li, eds. Springer, New York, NY, 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., Li, C., Harasymow, S., Roumeliotis, S., and Eglinton, J. K. Improved prediction of malt fermentability by measurement of the diastatic power enzymes β-amylase, α-amylase, and limit dextrinase: II. Impact of barley genetics, growing environment, and gibberellin on levels of α-amylase and limit dextrinase in malt. J. Am. Soc. Brew. Chem. 67:14–22, 2009.
   Web of Science ®Google Scholar
• Evans, D. E., Redd, K., Harysamow, S., Elvig, N., and Koutoulis, A. Small scale comparison of the influence of malt quality on malt brewing with barley quality on barley brewing using Ondea Pro. J. Am. Soc. Brew. Chem. 72:192–207, 2014.
   Web of Science ®Google Scholar
• Evans, D. E., van Wegen, B., Ma, Y., and Eglinton, J. K., 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
• Evans, D. E., Wallace, W., Lance, R. C. M., and MacLeod, L. C. Measurement of beta-amylase in malting barley (Hordeum vulgare L.). Part 2: The effect of germination and kilning on beta-amylase. J. Cereal Sci. 26:241–250, 1997.
   Web of Science ®Google Scholar
• Fox, G. P., Visser, J., Skov, T., Meijering, I., and Manley, M. Effect of different analysis conditions of a rapid visco analyser malt visco-grams in relation to malt of varying fermentability. J. Inst. Brew. 120:183–192, 2014.
   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
• Gastl, M., Knofel, T., and Becker, T. Conversion of isothermal 65°C mash—Measurement of quality characteristics. Brauwelt 154:274–276, 2014.
   Google Scholar
• Gous, P., and Fox, G. P. Amylopectin synthesis and hydrolysis—Understanding isoamylase and limit dextrinase in barley (Hordeum vulgare) quality. Trends Food Sci. Technol. 62:23–32, 2017.
   Web of Science ®Google Scholar
• Hamilton, D. M., and Lewis, M. J. Factors affecting wort extract and attenuation. Tech. Q. Master Brew. Assoc. Am. 11:31–34, 1974.
   Google Scholar
• Henson, C. A., and Duke, S. H. Osmolyte concentrations 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
• Hu, S., Yu, J., Dong, J., Evans, D. E., Liu, J., Huang, S., Huang, S., Fan, W., Yin, H., and Li, M. Relationship between levels of diastatic power enzymes and wort sugar production from different barley cultivars during the commercial mashing process of brewing. Starch 66:615–623, 2014.
   Web of Science ®Google Scholar
• Huang, Y., Cai, S., Ye, L., Han, Y., Wu, D., Dai, F., Li, C., and Zhang, G. Genetic architecture of limit dextrinase inhibitor (LDI) activity in Tibetan wild barley. BMC Plant Biol. 14:117–125, 2014.
   Web of Science ®Google Scholar
• Huang, Y. Q., Cai, S. G., and Zhang, G. P. The relationship of limit dextrinase, limit dextrinase inhibitor and malt quality parameters in barley and their genetic analysis. J. Cereal Sci. 70:140–145, 2016.
   Web of Science ®Google Scholar
• Jin, X., Cai, S. G., Ye, L., Chen, Z., Zhou, M., and Zhang, G. P. Association of HvLDI with limit dextrinase activity and malt quality in barley. Biotechnol. Lett. 35:639–645, 2013.
   Web of Science ®Google Scholar
• Jones, B. L. Endo-proteinases of barley and malt. J. Cereal Sci. 42:139–56, 2005.
   Web of Science ®Google Scholar
• Jones, B. L., and Budde, A. D. How various malt endoproteinase classes affect wort soluble protein levels. J. Cereal Sci. 41:95–106, 2005.
   Web of Science ®Google Scholar
• Kadziola, A., Abe, J. I., Svensson, B., and Haser, R. Crystal and molecular structure of barley alpha-amylase. J. Mol. Biol. 239:104–121, 1994.
   PubMed Web of Science ®Google Scholar
• Kihara, M., Kaneko, T., and Ito, K. Genetic variation of β-amylase thermostability among varieties of barley, Hordeum vulgare L., and relation to malting quality. Plant Breed. 117:425–428, 1998.
   Web of Science ®Google Scholar
• Koljonen, T., Hamalainen, J. J., Sojholm, K., Kettunen, A., and Pietila, K. Stimulation of the degradation of starch and β-glucans during mashing. In: Eur. Brew. Conv. Cong. Proc., Oslo, pp. 525–532, 1993.
   Google Scholar
• Koljonen, T., Hamalainen, J. J., Sojholm, K., Kettunen, A., and Pietila, K. A model for the prediction of fermentable sugar concentrations during mashing. J. Food Eng. 26:329–350, 1995.
   Web of Science ®Google Scholar
• Kuhbeck, F., Back, W., and Krottenthaler, M. Influence of lauter turbidity on composition, fermentation performance and beer quality—A review. J. Inst. Brew. 112:215–221, 2006.
   Web of Science ®Google Scholar
• Kuhbeck, F., Back, W., and Krottenthaler, M. Influence of lauter turbidity on wort composition, fermentation, performance and beer quality in large-scale trials. J. Inst. Brew. 112:222–231, 2006.
   Web of Science ®Google Scholar
• Kuhbeck, F., Schutz, M., Thiele, F., Krottenthaler, M., and Back, W. Influence of lauter turbidity and hot trub on wort composition, fermentation, and beer quality. J. Am. Soc. Brew. Chem. 64:16–28, 2006.
   Web of Science ®Google Scholar
• Kunze, W. Technology Brewing and Malting. VLB, Berlin, Germany, 1999.
   Google Scholar
• Langstaff, S. A., and Lewis, M. J. The mouthfeel of beer—A review. J. Inst. Brew. 99:31–37, 1993.
   Web of Science ®Google Scholar
• Lee, W. J., and Pyler, R. E. Barley malt limit dextrinase: Varietal, environmental and malting effects. J. Am. Soc. Brew. Chem. 42:11–17, 1984.
   Google Scholar
• Lentini, A., Goldsmith, M., Tsolis, A., Rogers, P., Hawthorne, D., and Karanagh, T. The effect of mashing conditions using various Australian malting varieties and their impact on wort limit gravities and concentration of linoleic acid in wort. In: Proc. Inst. Brew. Conv., Singapore, pp. 184–185, 2000.
   Google Scholar
• Longstaff, M. A., and Bryce, J. H. Development of limit dextrinase in germinated barley (Hordeum vulgare L.). Plant Physiol. 101:881–889, 1993.
   Web of Science ®Google Scholar
• Ma, Y., Stewart, D. C., Eglinton, J. K., Logue, S. J., Langridge, P., and Evans, D. E. Comparative enzyme kinetics of two allelic forms of barley (Hordeum vulgare L.) beta-amylase. J. Cereal Sci. 31:335–344, 2000.
   Web of Science ®Google Scholar
• Ma, Y. F., Eglinton, J. K., Evans, D. E., Logue, S. J., and Langridge, P. Removal of the four C-terminal glycine rich repeats enhances the thermostability of barley β-amylase. Biochemistry 39:13350–13355, 2000.
   Web of Science ®Google Scholar
• Ma, Y. F., Langridge, P. Logue, S. J., and Evans, D. E. The amino acid substitutions of barley β-amylase allelic forms that improve thermostability and substrate-binding affinity. Mol. Gen. Genet. 266:345–352, 2001.
   Google Scholar
• MacGregor, A. W., Bazin, S. L., and Izydorczyk, M. S. Gelatinization characteristics and enzyme susceptibility of different types of barley starch in the temperature range 48–75 °C. J. Inst. Brew. 108:43–47, 2002.
   Web of Science ®Google Scholar
• MacGregor, A. W., Bazin, S. L., and 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. 35:17–28, 2002.
   Web of Science ®Google Scholar
• MacGregor, A. W., Bazin, S. L., Macri, L. J., and Babb, J. C. Modelling the contribution of alpha-amylase, beta-amylase and limit dextrinase to starch degradation during mashing. J. Cereal Sci. 29:161–169, 1999.
   Web of Science ®Google Scholar
• MacGregor, A. W., Macri, L. J., Schroeder, S. W., and Bazin, S. L. Limit dextrinase from malted barley: Extraction, purification and characterization. Cereal Chem. 71:610–617, 1994.
   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
• Mangan, D., McCleary, B. V., Cornaggia, C., Ivory, R., Rooney, E., and McKie, V. Colorimetic and fluorometric assay of limit dextrinase. J. Cereal Sci. 62:50–57, 2015.
   Web of Science ®Google Scholar
• McCafferty, C. A., Perch-Nielsen, N., and Bryce, J. H. Effects of aerobic and anaerobic germination on the debranching enzyme, limit dextrinase, in barley malt. J. Am. Soc. Brew. Chem. 58:47–50, 2000.
   Web of Science ®Google Scholar
• McCleary, B. V. Measurement of the content of limit-dextrinase in cereal flours. Carbohydr. Res. 227:257–268, 1992.
   Web of Science ®Google Scholar
• McCleary, B. V., and Codd, R. Measurement of β-amylase in cereal flours and commercial enzyme preparations. J. Cereal Sci. 9:17–33, 1989.
   Web of Science ®Google Scholar
• McCleary, B. V., and Sheehan, H. Measurement of cereal α-amylase: A new assay procedure. J. Cereal Sci., 6:237–251, 1987.
   Web of Science ®Google Scholar
• McCleary, B. V., Mangan, D., McKie, V., Cornaggia, C., Ivory, R., and Rooney, E. Colourimetric and fluorometric substrates for measurement of pullulanase activity. Carbohydr. Res. 393:60–69, 2014.
   PubMed Web of Science ®Google Scholar
• Moll, M., Flayeux, R., Lipus, G., and Marc, A. Biochemistry of mashing. Tech. Q. Master Brew. Assoc. Am. 18:166–173, 1981.
   Google Scholar
• Moonjai, N., Verstrepen, K. J., Shen, H.-Y., Derdelinckx, H., Verachtert, H., and Delvaux, F. R. Uptake of linoleic acid by croppedbrewers' yeast and its incorporation into cellular lipid fractions. J. Am. Soc. Brew. Chem. 61:161–168, 2003.
   Web of Science ®Google Scholar
• Munck, L., Mundy, J., and Vaag, P. Characterization of enzyme inhibitors in barley and their tentative role in malting and brewing. J. Am. Soc. Brew. Chem. 43:35–38, 1985.
   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
• Piendl, A. Malt modification and mashing conditions as influencing factors on the carbohydrates of wort. Brew. Dig. 48:58–84, 1973.
   Google Scholar
• Ragot, F., Guinard, J. X., Shoemaker, C. F., and Lewis, M. J. The contribution of dextrins to beer sensory properties. Part I. Mouthfeel. J. Inst. Brew. 95:427–430, 1989.
   Web of Science ®Google Scholar
• Rubsam, H., Gastl, M., and Becker, T. Influence of a range of molecular weight distribution of beer components on the intensity of palate fullness. Eur. Food Res. Technol. 236:65–75, 2013.
   Web of Science ®Google Scholar
• Sallans, H. R., and Anderson, J. A. Varietal differences in barley and malts. X. Correlations of carbohydrates with nitrogen fractions and with malt extract, steeping time and malting loss. Can. J. Res. 18:219–229, 1940.
   Google Scholar
• Sandegren, E., and Klang, N. On barley amylase and proteinase. J. Inst. Brew. 56:313–318, 1950.
   Google Scholar
• Sidenius, U., Olsen, K., Svensson, B., and Christensen, V. BASI-amylase complex occurs in a two step reaction. FEBS Lett. 361:250–254, 1995.
   Google Scholar
• Sissons, M. J. Studies on the activation and release of bound limit dextrinase in malted barley. J. Am. Soc. Brew. Chem. 54:19–25, 1996.
   Web of Science ®Google Scholar
• Sissons, M. J., Lance, R. C. M., and Wallace, W. Bound and free forms of barley limit dextrinase. Cereal Chem. 71:520–521, 1994.
   Web of Science ®Google Scholar
• Sissons, M. J., Taylor, M., and Proudlove, M. Barley malt limit dextrinase: Its extraction, heat stability and activity during malting and mashing. J. Am. Soc. Brew. Chem. 53:105–110, 1995.
   Web of Science ®Google Scholar
• Sjöholm, K., Macri, L. J., and MacGregor, A. W. Is there a role for limit dextrinase in mashing? In: Eur. Brew. Conv. Cong. Proc., Brussels, pp. 277–284, 1995.
   Google Scholar
• Stenholm, K., and Home, S. A new approach to limit dextrinase and its role in mashing. J. Inst. Brew. 105:205–210, 1999.
   Web of Science ®Google Scholar
• Stenholm, K., Home, S., Pietila, K., Jaakkola, N., and Leino, E. Are the days of congress mashing over? In: Proc. Barley Malt Wort Symp., Inst. Brew. (Central & South African Section), Zimbabwe, pp. 149–163, 1996.
   Google Scholar
• Stenholm, K., Home, S., Pietila, K., Macri, L. J., and MacGregor, A. W. Starch hydrolysis in mashing. In: Proc. Inst. Brew Conv. (Asia/Pacific), Singapore, pp. 142–145, 1996.
   Google Scholar
• Stenholm, K., Home, S., Pietila, K., Macri, L. J., and MacGregor, A. W. Starch hydrolysis in mashing. In: Eur. Brew. Conv. Cong. Proc., Maastricht, pp. 142–145, 1997.
   Google Scholar
• Stenholm, K., Wilhelmson, A., and Home, S. Starch gelatinization temperature as a malt quality characteristic. In: Proc. Aviemore Conf. Malt., Brew. Distill. Institute of Brewing, London, U.K., pp. 242–245, 1998.
   Google Scholar
• Stewart, G. G., Yonesawa, T., and Martin, S. A. Influence of mashing conditions on fermentation characteristics of all-malt wort used to produce beer or whiskey. Tech. Q. Master Brew. Assoc. Am. 44:256–263, 2007.
   Google Scholar
• Verstrepen, K. J., Derdelinckx, G., Winderickx, J., Thevelein, J. M., Pretorius, I. S., and Delvaux, F. R. Flavor-active esters: Adding fruitiness to beer. J. Biosci. Bioeng. 96:110–118, 2003.
   PubMed Web of Science ®Google Scholar
• Wang, X. L., Zhang, X. L., Cai, S. G., Ye, L. Z., Zhou, M. X. Chen, Z. H., Zhang, G. P., and Dai, F. Genetic diversity and QTL mapping of thermostability of limit dextrinase in barley. J. Agric. Food Chem. 63:3778–3783, 2015.
   Web of Science ®Google Scholar
• Yang, X., Westcott, S., Evans, D. E., Zhang, X.-Q., Lance, R. C. M., and Li, C. Alleles of limit dextrinase gene associated with the enzyme thermostability in barley. Mol. Breed. 23:61–64, 2009.
   Web of Science ®Google Scholar