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Volumn 66, Issue 4, 2008, Pages 223-232

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

Author keywords

amylase; amylase; Limit dextrinase; Malt fermentability

Indexed keywords

HORDEUM;

EID: 57049125659     PISSN: 03610470     EISSN: None     Source Type: Journal    
DOI: 10.1094/ASBCJ-2008-0909-02     Document Type: Conference Paper
Times cited : (50)

References (51)
  • 1
    • 34249321291 scopus 로고    scopus 로고
    • Influence of corn size distribution on the diastatic power of malted barley and its impact on other malt quality parameters
    • Agu, R. C., Brosnan, J. M., Bringhurst, T. A., Palmer, G. H., and Jack, F. R. Influence of corn size distribution on the diastatic power of malted barley and its impact on other malt quality parameters. J. Agric. Food Chem. 55:3702-3707, 2007.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 3702-3707
    • Agu, R.C.1    Brosnan, J.M.2    Bringhurst, T.A.3    Palmer, G.H.4    Jack, F.R.5
  • 2
    • 0041754246 scopus 로고
    • American Society of Brewing Chemists, 8th ed. The Society, St. Paul, MN
    • American Society of Brewing Chemists. ASBC Methods of Analysis, 8th ed. The Society, St. Paul, MN, 1992.
    • (1992) ASBC Methods of Analysis
  • 3
    • 50049119059 scopus 로고
    • Diastatic activity (Lintner value)
    • Anonymous
    • Anonymous. Diastatic activity (Lintner value). J. Inst. Brew. 12:1-10, 1906.
    • (1906) J. Inst. Brew , vol.12 , pp. 1-10
  • 4
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa, T., and Timasheff, S. N. Stabilization of protein structure by sugars. Biochemistry 21:6536-6544, 1982.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 5
    • 0029141870 scopus 로고
    • Genetic and environmental variation in the diastatic power of Australian barley
    • Arends, A. M., Fox, G. P., Henry, R. J., Marschke, R. J., and Symons, M. H. Genetic and environmental variation in the diastatic power of Australian barley. J. Cereal Sci. 21:63-70, 1995.
    • (1995) J. Cereal Sci , vol.21 , pp. 63-70
    • Arends, A.M.1    Fox, G.P.2    Henry, R.J.3    Marschke, R.J.4    Symons, M.H.5
  • 6
    • 1642537891 scopus 로고    scopus 로고
    • Malt analysis - Prediction or predicament
    • Axcell, B. C. Malt analysis - Prediction or predicament Tech. Q. Master Brew. Assoc. Am. 35:28-30, 1998.
    • (1998) Tech. Q. Master Brew. Assoc. Am , vol.35 , pp. 28-30
    • Axcell, B.C.1
  • 7
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • 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.
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 8
    • 84987277559 scopus 로고
    • Malt diastatic activity. Part 2: A modified EBC diastatic power assay for the selective estimation of β-amylase activity. Time and temperature dependence of the release of reducing sugars
    • Delcour, J. A., and Verschaeve, S. G. Malt diastatic activity. Part 2: 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.
    • (1987) J. Inst. Brew , vol.93 , pp. 296-301
    • Delcour, J.A.1    Verschaeve, S.G.2
  • 9
    • 27444433567 scopus 로고    scopus 로고
    • Strains and handling techniques
    • J. T. McCabe, ed. Master Brewers Association of the Americas, St. Paul, MN. Pp
    • Dowhanick, T. M. Yeast - Strains and handling techniques. In: The Practical Brewer. J. T. McCabe, ed. Master Brewers Association of the Americas, St. Paul, MN. Pp. 263-298, 1999.
    • (1999) The Practical Brewer , pp. 263-298
    • Dowhanick, T.M.Y.1
  • 11
    • 57049175936 scopus 로고    scopus 로고
    • Effects of the high heat stable beta-amylase allele on fermentability of malts with low vs. high diastatic power
    • Edney, M. J., Eglinton, J. K., Collins, H. M., Barr, A. R., Legg, W. G., and Rossnagel, B. G. Effects of the high heat stable beta-amylase allele on fermentability of malts with low vs. high diastatic power. Proc. Congr. Eur. Brew. Conv. 31:475-482, 2007.
    • (2007) Proc. Congr. Eur. Brew. Conv , vol.31 , pp. 475-482
    • Edney, M.J.1    Eglinton, J.K.2    Collins, H.M.3    Barr, A.R.4    Legg, W.G.5    Rossnagel, B.G.6
  • 12
    • 0000704990 scopus 로고    scopus 로고
    • Thermostability variation in alleles of barley beta-amylase
    • Eglinton, J. K., Langridge, P., and Evans, D. E. Thermostability variation in alleles of barley beta-amylase. J. Cereal Sci. 28:301-309, 1998.
    • (1998) J. Cereal Sci , vol.28 , pp. 301-309
    • Eglinton, J.K.1    Langridge, P.2    Evans, D.E.3
  • 13
    • 0002809805 scopus 로고
    • Total β-amylase in barley used as a screening criteria for combined amylolytic activity in malt
    • Erdal, K., Jensen, M. O., Kristensen, M., Krough, J. J., Riis, P., and Vaag, P. Total β-amylase in barley used as a screening criteria for combined amylolytic activity in malt. Proc. Congr. Eur. Brew. Conv. 24:147-154, 1993.
    • (1993) Proc. Congr. Eur. Brew. Conv , vol.24 , pp. 147-154
    • Erdal, K.1    Jensen, M.O.2    Kristensen, M.3    Krough, J.J.4    Riis, P.5    Vaag, P.6
  • 14
    • 57049182466 scopus 로고    scopus 로고
    • European Brewery Convention, Verlag Hans Carl Getranke-Fachverlag, Nürnberg, Germany
    • European Brewery Convention. Analytica - EBC. Verlag Hans Carl Getranke-Fachverlag, Nürnberg, Germany, 1998.
    • (1998) Analytica - EBC
  • 15
    • 57049179580 scopus 로고    scopus 로고
    • A more cost- and labor-efficient assay for the combined measurement of the diastatic power enzymes β-amylase, α-amylase, and limit dextrinase
    • 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.
    • (2008) J. Am. Soc. Brew. Chem , vol.66 , pp. 215-222
    • Evans, D.E.1
  • 16
    • 27444431733 scopus 로고    scopus 로고
    • 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
    • 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.
    • (2005) J. Am. Soc. Brew. Chem , vol.63 , pp. 185-198
    • Evans, D.E.1    Collins, H.M.2    Eglinton, J.K.3    Wilhelmson, A.4
  • 17
    • 27444431754 scopus 로고    scopus 로고
    • The selection of a dried yeast strain for use in the apparent attenuation limit malt analysis (AAL) procedure
    • Evans, D. E., and Hamet, M. A. G. The selection of a dried yeast strain for use in the apparent attenuation limit malt analysis (AAL) procedure. J. Inst. Brew. 111:209-214, 2005.
    • (2005) J. Inst. Brew , vol.111 , pp. 209-214
    • Evans, D.E.1    Hamet, M.A.G.2
  • 19
    • 62149102966 scopus 로고    scopus 로고
    • Improved prediction of malt fermentability by the 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
    • In press
    • Evans, D. E., Li, C., Harasymow, S., Roumeliotis, S., and Eglinton, J. K. Improved prediction of malt fermentability by the 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. In press.
    • J. Am. Soc. Brew. Chem
    • Evans, D.E.1    Li, C.2    Harasymow, S.3    Roumeliotis, S.4    Eglinton, J.K.5
  • 20
  • 21
    • 84987278682 scopus 로고
    • 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
    • Gibson, T. S., Solah, V., Glennie Holmes, M. R., 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.
    • (1995) J. Inst. Brew , vol.101 , pp. 277-280
    • Gibson, T.S.1    Solah, V.2    Glennie Holmes, M.R.3    Taylor, H.R.4
  • 22
    • 0001599901 scopus 로고
    • Synthesis of salt-soluble proteins in barley: Pulse labelling study of grain filling in liquid-cultured detached spikes
    • Giese, H., and Hejgaard, J. Synthesis of salt-soluble proteins in barley: Pulse labelling study of grain filling in liquid-cultured detached spikes. Planta 161:172-177, 1984.
    • (1984) Planta , vol.161 , pp. 172-177
    • Giese, H.1    Hejgaard, J.2
  • 23
    • 0001110037 scopus 로고
    • Influence of nitrogen on the amount of hordein, protein Z and β-amylase messenger RNA in developing endosperms of barley
    • Giese, H., and Hopp, H. E. Influence of nitrogen on the amount of hordein, protein Z and β-amylase messenger RNA in developing endosperms of barley. Carlsberg Res. Commun. 49:365-383, 1984.
    • (1984) Carlsberg Res. Commun , vol.49 , pp. 365-383
    • Giese, H.1    Hopp, H.E.2
  • 24
    • 57049186610 scopus 로고    scopus 로고
    • Malt attenuation - An Australian brewer's perspective
    • Goldsmith, M. R. Malt attenuation - An Australian brewer's perspective. Aust. Barley Tech. Symp. 13:107-115, 2007.
    • (2007) Aust. Barley Tech. Symp , vol.13 , pp. 107-115
    • Goldsmith, M.R.1
  • 25
    • 0004681026 scopus 로고
    • Control of carbohydrate formation by gibberellic acid in barley endosperm
    • Hardie, D. G. Control of carbohydrate formation by gibberellic acid in barley endosperm. Phytochemistry 14:1719-1722, 1975.
    • (1975) Phytochemistry , vol.14 , pp. 1719-1722
    • Hardie, D.G.1
  • 26
    • 0011068506 scopus 로고
    • Effects of environment, variety and season on barley quality
    • Harris, G., and Banasik, O. J. Effects of environment, variety and season on barley quality. Cereal Chem. 29:148-155, 1952.
    • (1952) Cereal Chem , vol.29 , pp. 148-155
    • Harris, G.1    Banasik, O.J.2
  • 27
    • 84974324397 scopus 로고
    • Environmental and varietal differences in diastatic power and four associated characteristics of spring barley
    • Hayter, A. M., and Riggs, T. J. Environmental and varietal differences in diastatic power and four associated characteristics of spring barley. J. Agric. Sci. 80:297-302, 1973.
    • (1973) J. Agric. Sci , vol.80 , pp. 297-302
    • Hayter, A.M.1    Riggs, T.J.2
  • 28
    • 38949206389 scopus 로고    scopus 로고
    • A comparison of standard and non-standard measures of malt quality
    • 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.
    • (2008) J. Am. Soc. Brew. Chem , vol.66 , pp. 11-19
    • Henson, C.A.1    Duke, S.H.2
  • 29
    • 33847155727 scopus 로고    scopus 로고
    • Institute of Brewing, Analysis Committee of the IoB, IoB, London
    • Institute of Brewing, Analysis Committee of the IoB. Recommended Methods of Analysis. IoB, London, 1998.
    • (1998) Recommended Methods of Analysis
  • 30
    • 0031735767 scopus 로고    scopus 로고
    • Genetic variation of β-amylase thermostability among varieties of barley, Hordeum vulgare L., and relation to malting quality
    • 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.
    • (1998) Plant Breed , vol.117 , pp. 425-428
    • Kihara, M.1    Kaneko, T.2    Ito, K.3
  • 32
    • 0021260351 scopus 로고
    • Identification de la R-enzyme de'orge et du malt par focalisation isoelectrique.
    • Lenoir, P., MacGregor, A. W., Moll, M., and Daussant, J. Identification de la R-enzyme de'orge et du malt par focalisation isoelectrique. C. R. Acad. Sci. Paris 298:243-248, 1984.
    • (1984) C. R. Acad. Sci. Paris , vol.298 , pp. 243-248
    • Lenoir, P.1    MacGregor, A.W.2    Moll, M.3    Daussant, J.4
  • 33
    • 2442479244 scopus 로고    scopus 로고
    • Aspen Publishers Inc, Gaithersberg, MD
    • Lewis, M. J., and Young, T. W. Brewing. Aspen Publishers Inc., Gaithersberg, MD, 2001.
    • (2001) Brewing
    • Lewis, M.J.1    Young, T.W.2
  • 34
    • 57049157695 scopus 로고
    • The nature and properties of diastase
    • Lintner, C. J. The nature and properties of diastase. Wochenschr. Brau. 3:733-736, 753-755, 1886.
    • (1886) Wochenschr. Brau , vol.3 , Issue.733-736 , pp. 753-755
    • Lintner, C.J.1
  • 35
    • 0000687121 scopus 로고
    • Development of limit dextrinase in germinated barley (Hordeum vulgare L)
    • Longstaff, M. A., and Bryce, J. H. Development of limit dextrinase in germinated barley (Hordeum vulgare L). Plant Physiol. 101:881-889, 1993.
    • (1993) Plant Physiol , vol.101 , pp. 881-889
    • Longstaff, M.A.1    Bryce, J.H.2
  • 36
    • 84978584849 scopus 로고
    • Studies on debranching enzymes. Part 1: The limit dextrinase activity of extracts of certain higher plants and commercial malts
    • Manners, D. J., and Yellowlees, D. Studies on debranching enzymes. Part 1: The limit dextrinase activity of extracts of certain higher plants and commercial malts. J. Inst. Brew. 79:377-385, 1973.
    • (1973) J. Inst. Brew , vol.79 , pp. 377-385
    • Manners, D.J.1    Yellowlees, D.2
  • 37
    • 0027113459 scopus 로고
    • Measurement of the content of limit-dextrinase in cereal flours
    • McCleary, B. V. Measurement of the content of limit-dextrinase in cereal flours. Carbohydr. Res. 227:257-268, 1992.
    • (1992) Carbohydr. Res , vol.227 , pp. 257-268
    • McCleary, B.V.1
  • 38
    • 84987346517 scopus 로고
    • Measurement of β-amylase in cereal flours and commercial enzyme preparations
    • McCleary, B. V., and Codd, R. Measurement of β-amylase in cereal flours and commercial enzyme preparations. J. Cereal Sci. 9:17-33, 1989.
    • (1989) J. Cereal Sci , vol.9 , pp. 17-33
    • McCleary, B.V.1    Codd, R.2
  • 39
    • 0011817910 scopus 로고
    • Measurement of cereal α-amylase: A new assay procedure
    • McCleary, B. V., and Sheehan, H. Measurement of cereal α-amylase: A new assay procedure. J. Cereal Sci. 6:237-251, 1987.
    • (1987) J. Cereal Sci , vol.6 , pp. 237-251
    • McCleary, B.V.1    Sheehan, H.2
  • 40
    • 4344690835 scopus 로고    scopus 로고
    • The effect of milling parameters on starch hydrolysis of milled malt in the brewing process
    • Mousia, Z., Balkin, R. C., Pandiella, S. S., and Webb, C. The effect of milling parameters on starch hydrolysis of milled malt in the brewing process. Process Biochem. 39:2213-2219, 2004.
    • (2004) Process Biochem , vol.39 , pp. 2213-2219
    • Mousia, Z.1    Balkin, R.C.2    Pandiella, S.S.3    Webb, C.4
  • 41
    • 0005791934 scopus 로고
    • Memoire sur la diastase, les principaux produits de ses reactions, et leurs applications aux arts industriels.
    • Payen, A., and Persoz, J. F. Memoire sur la diastase, les principaux produits de ses reactions, et leurs applications aux arts industriels. Ann. Chim. 53:73, 1833.
    • (1833) Ann. Chim , vol.53 , pp. 73
    • Payen, A.1    Persoz, J.F.2
  • 42
    • 28444444154 scopus 로고    scopus 로고
    • Protein and hordein content in barley seeds as affected by nitrogen level and their relationship to beta-amylase activity
    • Qi, J.-C., Zhang, G.-P., and Zhou, M.-X. Protein and hordein content in barley seeds as affected by nitrogen level and their relationship to beta-amylase activity. J. Cereal Sci. 43:102-107, 2006.
    • (2006) J. Cereal Sci , vol.43 , pp. 102-107
    • Qi, J.-C.1    Zhang, G.-P.2    Zhou, M.-X.3
  • 43
    • 0011118636 scopus 로고
    • Variation and covariation in agronomic and malt quality characteristics of barley. II. Interrelationships of characters
    • Rutger, J. N., Schaller, C. W., and Dickson, A. D. Variation and covariation in agronomic and malt quality characteristics of barley. II. Interrelationships of characters. Crop Sci. 7:325-326, 1967.
    • (1967) Crop Sci , vol.7 , pp. 325-326
    • Rutger, J.N.1    Schaller, C.W.2    Dickson, A.D.3
  • 44
    • 0001258513 scopus 로고    scopus 로고
    • Optimized McCleary method for measurement of total β-amylase in barley and its applicability
    • 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.
    • (1996) J. Inst. Brew , vol.102 , pp. 271-275
    • Santos, M.M.M.1    Riis, P.2
  • 45
    • 0002440434 scopus 로고    scopus 로고
    • Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues
    • Schroeder, S. W., and MacGregor, A. W. Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues. J. Am. Soc. Brew. Chem. 56:32-37, 1998.
    • (1998) J. Am. Soc. Brew. Chem , vol.56 , pp. 32-37
    • Schroeder, S.W.1    MacGregor, A.W.2
  • 46
    • 0010980673 scopus 로고
    • Studies on limit dextinase in barley. 3. Limit dextrinase in developing kernels
    • Sissons, M. J., Lance, R. C. M., and Sparrow, D. H. B. Studies on limit dextinase in barley. 3. Limit dextrinase in developing kernels. J. Cereal Sci. 17:19-24, 1993.
    • (1993) J. Cereal Sci , vol.17 , pp. 19-24
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 47
    • 84979434229 scopus 로고
    • The use of electrophoresis in testing for high diastatic power in barley
    • Swanston, J. S. The use of electrophoresis in testing for high diastatic power in barley. J. Inst. Brew. 86:81-83, 1980.
    • (1980) J. Inst. Brew , vol.86 , pp. 81-83
    • Swanston, J.S.1
  • 48
    • 0042121144 scopus 로고    scopus 로고
    • Genotypic and environmental variation in barley beta-amylase activity and its relation to protein content
    • Wang, J., Zhang, G., Chen, J., Shen, Q., and Wu, F. Genotypic and environmental variation in barley beta-amylase activity and its relation to protein content. Food Chem. 83:163-165, 2003.
    • (2003) Food Chem , vol.83 , pp. 163-165
    • Wang, J.1    Zhang, G.2    Chen, J.3    Shen, Q.4    Wu, F.5
  • 49
    • 0036839762 scopus 로고    scopus 로고
    • Variation of beta- amylase activity in barley as affected by cultivar and environment and its relation to protein content and grain weight
    • Yin, C., Zhang, G. P., Wang, J. M., and Chen, J.-X. Variation of beta- amylase activity in barley as affected by cultivar and environment and its relation to protein content and grain weight. J. Cereal Sci. 36:307-312, 2002.
    • (2002) J. Cereal Sci , vol.36 , pp. 307-312
    • Yin, C.1    Zhang, G.P.2    Wang, J.M.3    Chen, J.-X.4
  • 50
    • 33645123587 scopus 로고    scopus 로고
    • The effect of cultivar and environment on β-amylase activity is associated with the change of protein content in barley grains
    • Zhang, G. P., Chen, J. X., Dai, F., Wang, J. M., and Wu, F. B. The effect of cultivar and environment on β-amylase activity is associated with the change of protein content in barley grains. J. Agron. Crop Sci. 192:43-49, 2006.
    • (2006) J. Agron. Crop Sci , vol.192 , pp. 43-49
    • Zhang, G.P.1    Chen, J.X.2    Dai, F.3    Wang, J.M.4    Wu, F.B.5


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