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Volumn , Issue 323, 1997, Pages

Malt limit dextrinase and its importance in brewing

Author keywords

Dextrins; Fermentability; Limit dextrinase; Malting, brewing; Mashing

Indexed keywords


EID: 7444225823     PISSN: 12350621     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article
Times cited : (3)

References (165)
  • 1
    • 0013490668 scopus 로고
    • The mechanism of carbohydrase action: 11. Pullulanase, an enzyme specific for the hydrolysis of alpha-1,6-bonds in amylaceous oligoand polysaccharides
    • Abdullah, M., Catley, B.J., Lee, E.Y.C., Robyt, J., Wallenfels, K. & Whealan, W.J. The mechanism of carbohydrase action: 11. Pullulanase, an enzyme specific for the hydrolysis of alpha-1,6-bonds in amylaceous oligoand polysaccharides. Cer. Chem., 1966. Vol. 43, pp. 111-118.
    • (1966) Cer. Chem. , vol.43 , pp. 111-118
    • Abdullah, M.1    Catley, B.J.2    Lee, E.Y.C.3    Robyt, J.4    Wallenfels, K.5    Whealan, W.J.6
  • 2
    • 0026203847 scopus 로고
    • High performance anion-exchange chromatography with pulsed amperometric detection of linear and branched glucose oligosaccharides
    • Ammeraal, R.N., Delgado, G.A., Tenbarge, F.L. & Friedman, R.B. High performance anion-exchange chromatography with pulsed amperometric detection of linear and branched glucose oligosaccharides. Carbohydr. Res., 1991. Vol. 215, pp. 179-192.
    • (1991) Carbohydr. Res. , vol.215 , pp. 179-192
    • Ammeraal, R.N.1    Delgado, G.A.2    Tenbarge, F.L.3    Friedman, R.B.4
  • 4
    • 0016780766 scopus 로고
    • The development of carbohydrases in germinating rye
    • Ballance, G.M. & Manners, D.J. The development of carbohydrases in germinating rye. Biochem. Soc. Trans., 1975. Vol. 3, pp. 989-991.
    • (1975) Biochem. Soc. Trans. , vol.3 , pp. 989-991
    • Ballance, G.M.1    Manners, D.J.2
  • 5
    • 0002331513 scopus 로고
    • Untersuchungen an Pullulan. II. Spezifischer Abbau durch ein bakterielles
    • In German
    • Bender, H. & Wallenfels, K. Untersuchungen an Pullulan. II. Spezifischer Abbau durch ein bakterielles Enzym. Biochem. Z., 1961. Vol. 334, pp. 79-95. (In German)
    • (1961) Enzym. Biochem. Z. , vol.334 , pp. 79-95
    • Bender, H.1    Wallenfels, K.2
  • 6
    • 33748037939 scopus 로고
    • Amylases, α and β
    • Colowick, S.P. & Kaplan, N.O. (eds.) New York: Academic Press Inc.
    • Bernfeld, P. Amylases, α and β. In: Colowick, S.P. & Kaplan, N.O. (eds.) Methods in enzymology. Vol. I. New York: Academic Press Inc., 1955. Pp. 149-159.
    • (1955) Methods in Enzymology , vol.1 , pp. 149-159
    • Bernfeld, P.1
  • 7
    • 84979368611 scopus 로고
    • Effect of pH, temperature and calcium ions on barley malt α-amylase isoenzymes
    • Bertoft, E., Andtfolk, C. & Kulp S-E. Effect of pH, temperature and calcium ions on barley malt α-amylase isoenzymes. J. Inst. Brew., 1984. Vol. 90, pp. 298-302.
    • (1984) J. Inst. Brew. , vol.90 , pp. 298-302
    • Bertoft, E.1    Andtfolk, C.2    Kulp, S.-E.3
  • 8
    • 84979407550 scopus 로고
    • A gel filtration study on the action of barley α-amylase isoenzymes on granular starch
    • Bertoft, E. & Kulp, S-E. A gel filtration study on the action of barley α-amylase isoenzymes on granular starch. J. Inst. Brew., 1986. Vol. 92, pp. 69-72.
    • (1986) J. Inst. Brew. , vol.92 , pp. 69-72
    • Bertoft, E.1    Kulp, S.-E.2
  • 9
    • 0002806530 scopus 로고
    • Starch granule structure and function: A physicochemical approach
    • Galliard, T. (ed.) New York: John Wiley & Sons
    • Blanshard, J.M.V. Starch granule structure and function: a physicochemical approach. In: Galliard, T. (ed.) Starch: Properties and potential. New York: John Wiley & Sons, 1987. Pp. 16-54.
    • (1987) Starch: Properties and Potential , pp. 16-54
    • Blanshard, J.M.V.1
  • 10
    • 84987316950 scopus 로고
    • The contribution of dextrins to sensory properties. Part II. Aftertaste
    • Bréfort, H., Guinard, J-X., Buhlert, J.E. & Lewis, M.J. The contribution of dextrins to sensory properties. Part II. Aftertaste. J. Inst. Brew., 1989. Vol. 95, pp. 431-435.
    • (1989) J. Inst. Brew. , vol.95 , pp. 431-435
    • Bréfort, H.1    Guinard, J.-X.2    Buhlert, J.E.3    Lewis, M.J.4
  • 13
    • 84866193055 scopus 로고
    • Development and properties of malt α-amylase
    • Madrid 1987. Oxford: IRL Press
    • Byrne, H. & Harmey, M. A. Development and properties of malt α-amylase. Proc. 21st Congr. Eur. Brew. Conv., Madrid 1987. Oxford: IRL Press, 1987. Pp. 297-304.
    • (1987) Proc. 21st Congr. Eur. Brew. Conv. , pp. 297-304
    • Byrne, H.1    Harmey, M.A.2
  • 14
    • 7444233797 scopus 로고
    • An assay for pullulanase in the presence of other carbohydrases
    • Catley, B.J. An assay for pullulanase in the presence of other carbohydrases. Carbohydr. Res., 1978. Vol. 61, pp. 419-424.
    • (1978) Carbohydr. Res. , vol.61 , pp. 419-424
    • Catley, B.J.1
  • 15
    • 0012189626 scopus 로고
    • Involatile constituents of beer
    • Pollock, J.R. (ed.) London: Academic Press
    • Charalambous, G. Involatile constituents of beer. In: Pollock, J.R. (ed.) Brewing science, Vol. 2. London: Academic Press, 1981. Pp. 180-196.
    • (1981) Brewing Science , vol.2 , pp. 180-196
    • Charalambous, G.1
  • 16
    • 7444259203 scopus 로고
    • Immunochemical characterization of the debranching enzyme of barley and malt
    • Madrid 1987. Oxford: IRL Press, (In French)
    • Daussant, J., Mayer, C. & MacGregor, A. W. Immunochemical characterization of the debranching enzyme of barley and malt. Proc. 21st Congr. Eur. Brew. Conv., Madrid 1987. Oxford: IRL Press, 1987. Pp. 305-312. (In French)
    • (1987) Proc. 21st Congr. Eur. Brew. Conv. , pp. 305-312
    • Daussant, J.1    Mayer, C.2    MacGregor, A.W.3
  • 17
    • 0041623280 scopus 로고
    • On the specificity of starch debranching enzymes
    • Drummond, G.S., Smith, E.E. & Whelan, W.J. On the specificity of starch debranching enzymes. FEBS Letters, 1970. Vol. 9, pp. 136-140.
    • (1970) FEBS Letters , vol.9 , pp. 136-140
    • Drummond, G.S.1    Smith, E.E.2    Whelan, W.J.3
  • 19
    • 0001765463 scopus 로고
    • A model for starch breakdown in higher plants
    • Dunn, G. A model for starch breakdown in higher plants. Phytochem., 1974. Vol. 13, pp. 1341-1346.
    • (1974) Phytochem. , vol.13 , pp. 1341-1346
    • Dunn, G.1
  • 20
    • 0015847290 scopus 로고
    • Observations on the action of limit dextrinase on amylopectin-like polysaccharides
    • Dunn, G., Hardie, H. & Manners, D.J. Observations on the action of limit dextrinase on amylopectin-like polysaccharides. Biochem. J., 1973. Vol. 133, pp. 413-416.
    • (1973) Biochem. J. , vol.133 , pp. 413-416
    • Dunn, G.1    Hardie, H.2    Manners, D.J.3
  • 21
    • 0016466535 scopus 로고
    • The limit dextrinase from ungerminated oats (Avena sativa L.) and ungermianted rice (Oryzae sativa L.)
    • Dunn, G. & Manners, D.J. The limit dextrinase from ungerminated oats (Avena sativa L.) and ungermianted rice (Oryzae sativa L.). Carbohydr. Res., 1975. Vol. 39, pp. 283-293.
    • (1975) Carbohydr. Res. , vol.39 , pp. 283-293
    • Dunn, G.1    Manners, D.J.2
  • 22
    • 0004233127 scopus 로고
    • Zürich: Brauerei- und Getränke-Rundschau
    • EBC (European Brewery Convention), Analytica-EBC. 4th ed. Zürich: Brauerei- und Getränke-Rundschau, 1987. 291 pp.
    • (1987) Analytica-EBC. 4th Ed.
  • 23
    • 84966609154 scopus 로고
    • Dextrins in brewing
    • Interlaken 1969. Amsterdam: Elsevier Publishing Company
    • Enevoldsen, B.S. Dextrins in brewing. Proc. 12th Congr. Eur. Brew. Conv., Interlaken 1969. Amsterdam: Elsevier Publishing Company, 1970a. Pp. 205-223.
    • (1970) Proc. 12th Congr. Eur. Brew. Conv. , pp. 205-223
    • Enevoldsen, B.S.1
  • 24
    • 7444229377 scopus 로고
    • Application of the debranching enzyme, pullulanase, in brewing from unmalted cereals. I. Condition of mashing and carbohydrate composition of the wort
    • Enevoldsen, B.S. Application of the debranching enzyme, pullulanase, in brewing from unmalted cereals. I. Condition of mashing and carbohydrate composition of the wort. J. Inst. Brew., 1970b. Vol. 76, pp. 546-552.
    • (1970) J. Inst. Brew. , vol.76 , pp. 546-552
    • Enevoldsen, B.S.1
  • 25
    • 0008554796 scopus 로고
    • Debranching enzymes in brewing
    • Nice 1975. Zoeterwounde: European Brewery Convention
    • Enevoldsen, B.S. Debranching enzymes in brewing. Proc. 15th Congr. Eur. Brew. Conv., Nice 1975. Zoeterwounde: European Brewery Convention, 1975. Pp.683-697.
    • (1975) Proc. 15th Congr. Eur. Brew. Conv. , pp. 683-697
    • Enevoldsen, B.S.1
  • 26
    • 1042272791 scopus 로고
    • Degradation of starch by amylases in beer brewing
    • Enevoldsen, B.S. Degradation of starch by amylases in beer brewing. J. Jap. Soc. Starch Sci., 1978. Vol. 25, pp. 89-99.
    • (1978) J. Jap. Soc. Starch Sci. , vol.25 , pp. 89-99
    • Enevoldsen, B.S.1
  • 27
    • 84979186657 scopus 로고
    • Structural analysis of wort dextrins by means of β-amylase and the debranching enzyme, pullulanase
    • Enevoldsen, B.S. & Bathgate, G.N. Structural analysis of wort dextrins by means of β-amylase and the debranching enzyme, pullulanase. J. Inst. Brew., 1969. Vol. 75, pp. 433-443.
    • (1969) J. Inst. Brew. , vol.75 , pp. 433-443
    • Enevoldsen, B.S.1    Bathgate, G.N.2
  • 28
    • 0008549987 scopus 로고
    • Dextrins in brewing. II. Distribution of oligo- and megalosaccharides during mashing, in wort and in beer
    • Salzburg 1973. Amsterdam: Elsevier Scientific Publishing Company
    • Enevoldsen, B.S. & Schmidt, F. Dextrins in brewing. II. Distribution of oligo- and megalosaccharides during mashing, in wort and in beer. Proc. 14th Congr. Eur. Brew. Conv., Salzburg 1973. Amsterdam: Elsevier Scientific Publishing Company, 1974a. Pp. 135-148.
    • (1974) Proc. 14th Congr. Eur. Brew. Conv. , pp. 135-148
    • Enevoldsen, B.S.1    Schmidt, F.2
  • 29
    • 84978550007 scopus 로고
    • Dextrins in brewing. Studies on singly-branched and multiply-branched dextrins in brewing
    • Enevoldsen, B.S. & Schmidt, F. Dextrins in brewing. Studies on singly-branched and multiply-branched dextrins in brewing. J. Inst. Brew., 1974b. Vol. 80, pp. 520-533.
    • (1974) J. Inst. Brew. , vol.80 , pp. 520-533
    • Enevoldsen, B.S.1    Schmidt, F.2
  • 30
    • 0028093146 scopus 로고
    • Direct detection of pullulanase activity in electrophoretic polyacrylamide gels
    • Furegon, L., Curioni, A. & Peruffo, A.D.B. Direct detection of pullulanase activity in electrophoretic polyacrylamide gels. Anal. Biochem., 1994. Vol. 221, pp. 200-201.
    • (1994) Anal. Biochem. , vol.221 , pp. 200-201
    • Furegon, L.1    Curioni, A.2    Peruffo, A.D.B.3
  • 31
    • 0008609929 scopus 로고
    • The limit dextrinase from the broad bean (Vicia faba L.)
    • Gordon, R.W., Manners, D.J. & Stark, J.R. The limit dextrinase from the broad bean (Vicia faba L.). Carbohydr. Res., 1975. Vol. 42, pp. 125-134.
    • (1975) Carbohydr. Res. , vol.42 , pp. 125-134
    • Gordon, R.W.1    Manners, D.J.2    Stark, J.R.3
  • 32
    • 84983960861 scopus 로고
    • Some observations on the stability of amylose and amylopectin in aqueous solution
    • Greenwood, C.T. & Hourston, D.J. Some observations on the stability of amylose and amylopectin in aqueous solution. Starch 1971, Vol. 23, pp. 344-347.
    • (1971) Starch , vol.23 , pp. 344-347
    • Greenwood, C.T.1    Hourston, D.J.2
  • 33
    • 84980118629 scopus 로고
    • Limit-dextrinase activity in malted barley
    • Greig, C.G. Limit-dextrinase activity in malted barley. J. Inst. Brew., 1963. Vol. 69, pp. 412-417.
    • (1963) J. Inst. Brew. , vol.69 , pp. 412-417
    • Greig, C.G.1
  • 34
    • 84987277401 scopus 로고
    • Release and activation of barley β-amylase
    • Grime, K.H. & Briggs, D.E. Release and activation of barley β-amylase. J. Inst. Brew., 1995. Vol. 101, pp. 337-343.
    • (1995) J. Inst. Brew. , vol.101 , pp. 337-343
    • Grime, K.H.1    Briggs, D.E.2
  • 35
    • 0000274656 scopus 로고    scopus 로고
    • The release of bound β-amylase by macromolecules
    • Grime, K.H. & Briggs, D.E. The release of bound β-amylase by macromolecules. J. Inst. Brew., 1996. Vol. 102, pp. 261-270.
    • (1996) J. Inst. Brew. , vol.102 , pp. 261-270
    • Grime, K.H.1    Briggs, D.E.2
  • 36
    • 0001876687 scopus 로고
    • Release and activation of barley beta-amylase by malt endopeptidases
    • Guerin, J.R., Lance, R.C.M. & Wallace, W. Release and activation of barley beta-amylase by malt endopeptidases. J. Cer. Sci., 1992. Vol. 15, pp. 5-14.
    • (1992) J. Cer. Sci. , vol.15 , pp. 5-14
    • Guerin, J.R.1    Lance, R.C.M.2    Wallace, W.3
  • 37
    • 0001992521 scopus 로고
    • Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers
    • Hammerton, R. W. & Ho, T-H.D. Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers. Plant Physiol., 1986. Vol. 80, pp. 692-697.
    • (1986) Plant Physiol. , vol.80 , pp. 692-697
    • Hammerton, R.W.1    Ho, T.-H.D.2
  • 38
    • 0000992348 scopus 로고
    • Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during the desiccation phase of seed development
    • Hara-Nishimura, I., Nishimura, M. & Daussant, J. Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during the desiccation phase of seed development. Protoplasma, 1986. Vol. 134, pp. 149-153.
    • (1986) Protoplasma , vol.134 , pp. 149-153
    • Hara-Nishimura, I.1    Nishimura, M.2    Daussant, J.3
  • 39
    • 0004681026 scopus 로고
    • Control of carbohydrase formation by gibberellic acid in barley endosperm
    • Hardie, D.G. Control of carbohydrase formation by gibberellic acid in barley endosperm. Phytochem., 1975. Vol. 14, pp. 1719-1722.
    • (1975) Phytochem. , vol.14 , pp. 1719-1722
    • Hardie, D.G.1
  • 40
    • 0016097703 scopus 로고
    • A viscosimetric assay for pullulanase-type debranching enzymes
    • Hardie, D.G. & Manners, D.J. A viscosimetric assay for pullulanase-type debranching enzymes. Carbohydr. Res., 1974. Vol. 36, pp. 207-210.
    • (1974) Carbohydr. Res. , vol.36 , pp. 207-210
    • Hardie, D.G.1    Manners, D.J.2
  • 41
    • 0016991188 scopus 로고
    • The limit dextrinase from malted sorghum (Sorghum vulgare)
    • Hardie, D.H., Manners, D.J. & Yellowlees, D. The limit dextrinase from malted sorghum (Sorghum vulgare). Carbohydr. Res., 1976. Vol. 50, pp. 75-85.
    • (1976) Carbohydr. Res. , vol.50 , pp. 75-85
    • Hardie, D.H.1    Manners, D.J.2    Yellowlees, D.3
  • 42
    • 0040687034 scopus 로고
    • Polymodal distribution of chain lengths of amylopectins, and its significance
    • Hizukuri, S. Polymodal distribution of chain lengths of amylopectins, and its significance. Carbohydr. Res., 1986. Vol. 147, pp. 342-347.
    • (1986) Carbohydr. Res. , vol.147 , pp. 342-347
    • Hizukuri, S.1
  • 43
    • 0041623285 scopus 로고
    • The enzymic synthesis and degradation of starch. Part XIV. R-enzyme
    • Hobson, P.N., Whealan, W.J. & Peat S. The enzymic synthesis and degradation of starch. Part XIV. R-enzyme. J. Chem. Soc., 1951. Pp. 1451-1459.
    • (1951) J. Chem. Soc. , pp. 1451-1459
    • Hobson, P.N.1    Whealan, W.J.2    Peat, S.3
  • 44
    • 84866189654 scopus 로고
    • Development of β-amylase in six-row barleys
    • Helsinki 1985. Oxford: IRL Press
    • Home, S., Aikasalo, R. & Linko, M. Development of β-amylase in six-row barleys. Proc. 20th Congr. Eur. Brew. Conv., Helsinki 1985. Oxford: IRL Press, 1985. Pp. 659-666.
    • (1985) Proc. 20th Congr. Eur. Brew. Conv. , pp. 659-666
    • Home, S.1    Aikasalo, R.2    Linko, M.3
  • 45
    • 0007184468 scopus 로고
    • Limit dextrinase. I. Action of limit dextrinase in distilling
    • Hopkins, R.H. & Wiener, S. Limit dextrinase. I. Action of limit dextrinase in distilling. J. Inst. Brew., 1955. Vol. 61, pp. 488-492.
    • (1955) J. Inst. Brew. , vol.61 , pp. 488-492
    • Hopkins, R.H.1    Wiener, S.2
  • 46
    • 84989102139 scopus 로고
    • Recent advances in knowledge of starch structure
    • Imberty, A., Buléon, A., Tran, V. & Pérez, S. Recent advances in knowledge of starch structure. Starch, 1991. Vol. 43, pp. 375-384.
    • (1991) Starch , vol.43 , pp. 375-384
    • Imberty, A.1    Buléon, A.2    Tran, V.3    Pérez, S.4
  • 47
    • 0003450992 scopus 로고
    • San Diego: Academic Press, Inc.
    • IUBMB (International Union of Biochemistry and Molecular Biology). Enzyme Nomenclature. San Diego: Academic Press, Inc., 1992. Pp 346-369.
    • (1992) Enzyme Nomenclature , pp. 346-369
  • 48
    • 0042625250 scopus 로고
    • Purification and some properties of debranching enzymes of germinating rice endosperm
    • Iwaki, K. & Fuwa, H. Purification and some properties of debranching enzymes of germinating rice endosperm. Agric. Biol. Chem., 1981. Vol. 45, pp. 2683-2688.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 2683-2688
    • Iwaki, K.1    Fuwa, H.2
  • 49
    • 7444236577 scopus 로고
    • Action mode of debranching enzyme of germinating rice endosperm on several oligosaccharides and polysaccharides
    • Iwaki, K. & Fuwa, H. Action mode of debranching enzyme of germinating rice endosperm on several oligosaccharides and polysaccharides. Agric. Biol. Chem., 1982. Vol. 46, pp. 2233-2240.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 2233-2240
    • Iwaki, K.1    Fuwa, H.2
  • 50
    • 0002262344 scopus 로고
    • A plate culture method for the simultaneous detection of bacteria producing pullulan- and/or starch-hydrolyzing enzymes
    • Kanno, M. & Tomimura, E. A plate culture method for the simultaneous detection of bacteria producing pullulan- and/or starch-hydrolyzing enzymes. Agr. Biol. Chem., 1985. Vol. 49, pp. 1529-1530.
    • (1985) Agr. Biol. Chem. , vol.49 , pp. 1529-1530
    • Kanno, M.1    Tomimura, E.2
  • 51
    • 1642497136 scopus 로고
    • Effect of environment and genotype on the fermentability of malt produced from four Australian barley varieties
    • Kenn, D.A., Dagg, A.H.S. & Stuart, I.M. Effect of environment and genotype on the fermentability of malt produced from four Australian barley varieties. J. Am. Soc. Brew. Chem., 1993. Vol. 51, pp. 119-122.
    • (1993) J. Am. Soc. Brew. Chem. , vol.51 , pp. 119-122
    • Kenn, D.A.1    Dagg, A.H.S.2    Stuart, I.M.3
  • 52
    • 0042338846 scopus 로고
    • Sorghum amylase
    • Kneen, E. Sorghum amylase. Cer. Chem., 1945. Vol. 22, pp. 112-134.
    • (1945) Cer. Chem. , vol.22 , pp. 112-134
    • Kneen, E.1
  • 53
    • 0343271152 scopus 로고
    • The limit dextrinase activity of barley malts
    • 1948. St. Paul: American Society of Brewing Chemists
    • Kneen, E. & Spoerl, J.M. The limit dextrinase activity of barley malts. Proc. Am. Soc. Brew. Chem., 1948. St. Paul: American Society of Brewing Chemists, 1948. Pp. 20-27.
    • (1948) Proc. Am. Soc. Brew. Chem. , pp. 20-27
    • Kneen, E.1    Spoerl, J.M.2
  • 55
    • 0008587470 scopus 로고
    • Purification and characterization of barley limit dextrinase during malting
    • Oslo 1993. Oxford: IRL Press
    • Kristensen, M., Svensson, B. & Larsen, J. Purification and characterization of barley limit dextrinase during malting. Proc. 24th Congr. Eur. Brew. Conv., Oslo 1993. Oxford: IRL Press, 1993. Pp. 37-43.
    • (1993) Proc. 24th Congr. Eur. Brew. Conv. , pp. 37-43
    • Kristensen, M.1    Svensson, B.2    Larsen, J.3
  • 56
    • 84888291523 scopus 로고
    • Note on the presence of debranching enzymes in mature wheat kernels
    • Kruger, J.E. & Marchylo, B. Note on the presence of debranching enzymes in mature wheat kernels. Cer. Chem., 1978. Vol. 55, pp. 529-533.
    • (1978) Cer. Chem. , vol.55 , pp. 529-533
    • Kruger, J.E.1    Marchylo, B.2
  • 57
    • 84866186523 scopus 로고
    • Stärkeeinschlußverbindungen und ihre Bedeutung beim Maischen
    • In German
    • Krüger, E. & Strobl, M. Stärkeeinschlußverbindungen und ihre Bedeutung beim Maischen. Montasschr. Brauwiss., 1984. Vol. 37, pp. 505-512. (In German)
    • (1984) Montasschr. Brauwiss. , vol.37 , pp. 505-512
    • Krüger, E.1    Strobl, M.2
  • 58
    • 84866188457 scopus 로고
    • Die Bedeutung der Stärkeeinschlußverbindungen für die Bierbereitung
    • Helsinki 1985. Oxford: IRL Press, (In German)
    • Krüger, E. & Strobl, M. Die Bedeutung der Stärkeeinschlußverbindungen für die Bierbereitung. Proc. 20th Congr. Eur. Brew. Conv., Helsinki 1985. Oxford: IRL Press, 1985. Pp. 347-354. (In German)
    • (1985) Proc. 20th Congr. Eur. Brew. Conv. , pp. 347-354
    • Krüger, E.1    Strobl, M.2
  • 59
    • 84987357428 scopus 로고
    • The mouthfeel of beer - A review
    • Langstaff, S.A. & Lewis, M.J. The mouthfeel of beer - a review. J. Inst. Brew., 1993. Vol. 99, pp. 31-37.
    • (1993) J. Inst. Brew. , vol.99 , pp. 31-37
    • Langstaff, S.A.1    Lewis, M.J.2
  • 60
    • 84989102504 scopus 로고
    • Purification and characterization of Bacillus acidopullulyticus pullulanase for enzymatic starch modification
    • Lappalainen, A., Niku-Paavola, M-L., Suortti, T. & Poutanen, K. Purification and characterization of Bacillus acidopullulyticus pullulanase for enzymatic starch modification. Starch, 1991. Vol. 43, pp. 477-482.
    • (1991) Starch , vol.43 , pp. 477-482
    • Lappalainen, A.1    Niku-Paavola, M.-L.2    Suortti, T.3    Poutanen, K.4
  • 61
    • 1042284422 scopus 로고
    • Maturation du caryopse d'orge: Évolution des isoformes des α- et β-amylases, de l'enzyme débranchante, de l'inhibitoteur d'α-amylases chez plusieurs variétés
    • Helsinki 1985. Oxford: IRL Press, (In French)
    • Laurière, C., Mayer, C., Renard, H., MacGregor, A. & Daussant, J. Maturation du caryopse d'orge: évolution des isoformes des α- et β-amylases, de l'enzyme débranchante, de l'inhibitoteur d'α-amylases chez plusieurs variétés, Proc. 20th Congr. Eur. Brew. Conv., Helsinki 1985. Oxford: IRL Press, 1985. Pp. 675-682. (In French)
    • (1985) Proc. 20th Congr. Eur. Brew. Conv. , pp. 675-682
    • Laurière, C.1    Mayer, C.2    Renard, H.3    MacGregor, A.4    Daussant, J.5
  • 63
    • 0344417721 scopus 로고
    • Purification of germinated barley α-amylase isoenzymes and limit dextrinase by chromatofocusing and affinity chromatography
    • Lecommandeur, D., MacGregor, A.W. & Daussant, J. Purification of germinated barley α-amylase isoenzymes and limit dextrinase by chromatofocusing and affinity chromatography. J. Chromatogr., 1988. Vol. 441, pp. 436-442.
    • (1988) J. Chromatogr. , vol.441 , pp. 436-442
    • Lecommandeur, D.1    MacGregor, A.W.2    Daussant, J.3
  • 64
    • 0015051534 scopus 로고
    • The substrate specificity of amylopectin-debranching enzymes from sweet corn
    • Lee, E.Y.C., Marshall, J.J. & Whealan, W.J. The substrate specificity of amylopectin-debranching enzymes from sweet corn. Arch. of Biochem. Biophys., 1971. Vol. 143, pp. 365-374.
    • (1971) Arch. of Biochem. Biophys. , vol.143 , pp. 365-374
    • Lee, E.Y.C.1    Marshall, J.J.2    Whealan, W.J.3
  • 65
    • 7444255024 scopus 로고
    • Improved assay procedure for limit dextrinase in malt extracts
    • Lee, W.J. & Pyler, R.E. Improved assay procedure for limit dextrinase in malt extracts. Brew. Dig., 1982. Vol. 57, No 7, pp. 24-26.
    • (1982) Brew. Dig. , vol.57 , Issue.7 , pp. 24-26
    • Lee, W.J.1    Pyler, R.E.2
  • 66
    • 0002885532 scopus 로고
    • Barley malt limit dextrinase: Varietal, environmental and malting effect
    • Lee, W.J. & Pyler, R.E. Barley malt limit dextrinase: varietal, environmental and malting effect. J. Am. Soc. Brew. Chem., 1984. Vol. 42, pp. 11-17.
    • (1984) J. Am. Soc. Brew. Chem. , vol.42 , pp. 11-17
    • Lee, W.J.1    Pyler, R.E.2
  • 67
    • 77956944021 scopus 로고
    • Glycogen and starch debranching enzymes
    • Boyer, P.D. (ed.) New York: Academic Press
    • Lee, E.Y.C. & Whealan, W.J. Glycogen and starch debranching enzymes. In: Boyer, P.D. (ed.) The enzymes. Vol. V, 3rd ed., New York: Academic Press, 1971. Pp. 191-234.
    • (1971) The Enzymes. Vol. V, 3rd Ed. , vol.5 , pp. 191-234
    • Lee, E.Y.C.1    Whealan, W.J.2
  • 68
    • 0021260351 scopus 로고
    • Identification de la R-enzyme de l'orge et du malt par focalisation isoélectrique
    • serie III, (In French)
    • Lenoir, P., MacGregor, A.W., Moll, M. & Daussant, J. Identification de la R-enzyme de l'orge et du malt par focalisation isoélectrique. C.R. Acad. Sc. Paris, 1984. Vol. 298, serie III, pp. 243-248. (In French)
    • (1984) C.R. Acad. Sc. Paris , vol.298 , pp. 243-248
    • Lenoir, P.1    MacGregor, A.W.2    Moll, M.3    Daussant, J.4
  • 69
    • 0001489664 scopus 로고
    • Characterization and subcellular localization of debranching enzyme and endoamylase from leaves of sugar beet
    • Li, B., Servaites J.C. & Geiger, D.R. Characterization and subcellular localization of debranching enzyme and endoamylase from leaves of sugar beet. Plant. Physiol., 1992. Vol. 98, pp. 1277-1284.
    • (1992) Plant. Physiol. , vol.98 , pp. 1277-1284
    • Li, B.1    Servaites, J.C.2    Geiger, D.R.3
  • 70
    • 0001243968 scopus 로고
    • Main fermentation with immobilized yeast
    • Lisbon 1991. Oxford: IRL Press
    • Linko, M. & Kronlöf, J. Main fermentation with immobilized yeast. Proc. 23rd Congr. Eur. Brew. Conv., Lisbon 1991. Oxford: IRL Press, 1991. Pp. 353-359.
    • (1991) Proc. 23rd Congr. Eur. Brew. Conv. , pp. 353-359
    • Linko, M.1    Kronlöf, J.2
  • 71
    • 0002304304 scopus 로고
    • Levels of limit dextrinase activity in malting barley
    • Lisbon 1991. Oxford: IRL Press
    • Longstaff, M.A. & Bryce, J.H. Levels of limit dextrinase activity in malting barley. Proc. 23rd Congr. Eur. Brew. Conv., Lisbon 1991. Oxford: IRL Press, 1991. Pp. 593-600.
    • (1991) Proc. 23rd Congr. Eur. Brew. Conv. , pp. 593-600
    • Longstaff, M.A.1    Bryce, J.H.2
  • 72
    • 0000687121 scopus 로고
    • Development of limit dextrinase in germinated barley (Hordeum vulgare L.) Evidence of proteolytic activation
    • Longstaff, M.A. & Bryce, J.H. Development of limit dextrinase in germinated barley (Hordeum vulgare L.) Evidence of proteolytic activation. Plant. Physiol., 1993. Vol. 101, pp. 881-889.
    • (1993) Plant. Physiol. , vol.101 , pp. 881-889
    • Longstaff, M.A.1    Bryce, J.H.2
  • 73
    • 0343138677 scopus 로고
    • Effect of dextrins composition on flavour characteristics
    • Lisbon 1991. Oxford: IRL Press
    • Louant, G. & Dufour, J-P. Effect of dextrins composition on flavour characteristics. Proc. 23rd Congr. Eur. Brew. Conv., Lisbon 1991. Oxford: IRL Press, 1991. Pp. 417-424.
    • (1991) Proc. 23rd Congr. Eur. Brew. Conv. , pp. 417-424
    • Louant, G.1    Dufour, J.-P.2
  • 74
    • 7444240936 scopus 로고
    • Limit-dextrinase activity of malts from ten barley varieties grown at ten stations during four seasons
    • Toronto 1952. Madison: American Society of Brewing Chemists
    • Lowry, M.T., Robbins, G.S., Ohlson, W.J. & Dickson, A.D. Limit-dextrinase activity of malts from ten barley varieties grown at ten stations during four seasons. Proc. Am. Soc. Brew. Chem., Toronto 1952. Madison: American Society of Brewing Chemists, 1952. Pp. 21-25.
    • (1952) Proc. Am. Soc. Brew. Chem. , pp. 21-25
    • Lowry, M.T.1    Robbins, G.S.2    Ohlson, W.J.3    Dickson, A.D.4
  • 75
    • 0001741402 scopus 로고
    • Purification and properties of spinach leaf debranching enzyme
    • Ludwig, I., Ziegler, P. & Beck, E. Purification and properties of spinach leaf debranching enzyme. Plant Physiol., 1984. Vol. 74, pp. 856-861.
    • (1984) Plant Physiol. , vol.74 , pp. 856-861
    • Ludwig, I.1    Ziegler, P.2    Beck, E.3
  • 76
    • 7444262066 scopus 로고
    • Changes in α-amylase enzymes during germination
    • MacGregor, A.W. Changes in α-amylase enzymes during germination. J. Am. Soc. Brew. Chem., 1978. Vol. 36, pp. 1-5.
    • (1978) J. Am. Soc. Brew. Chem. , vol.36 , pp. 1-5
    • MacGregor, A.W.1
  • 77
    • 0040020893 scopus 로고
    • α-amylase, limit dextrinase and α-glucosidase enzymes in barley and malt
    • MacGregor, A.W. α-amylase, limit dextrinase and α-glucosidase enzymes in barley and malt. CRC Crit. Rev. Biotechnol., 1987. Vol. 5, pp. 117-128.
    • (1987) CRC Crit. Rev. Biotechnol. , vol.5 , pp. 117-128
    • MacGregor, A.W.1
  • 78
    • 0000877608 scopus 로고
    • Starch degrading enzymes
    • MacGregor, A.W. Starch degrading enzymes. Ferment, 1991. Vol. 4, pp. 178-182.
    • (1991) Ferment , vol.4 , pp. 178-182
    • MacGregor, A.W.1
  • 79
    • 0000808171 scopus 로고
    • Hydrolysis of large and small starch granules from normal and waxy barley cultivars by alpha-amylase from barley malt
    • MacGregor, A.W. & Ballance, D.L. Hydrolysis of large and small starch granules from normal and waxy barley cultivars by alpha-amylase from barley malt. Cer. Chem., 1980. Vol. 57, pp. 397-402.
    • (1980) Cer. Chem. , vol.57 , pp. 397-402
    • MacGregor, A.W.1    Ballance, D.L.2
  • 80
    • 84987367688 scopus 로고
    • α-amylase in developing barley kernels - A reappraisal
    • MacGregor, A.W. & Dushnicky, L. α-amylase in developing barley kernels - a reappraisal. J. Inst. Brew., 1989a. Vol. 95, pp. 29-33.
    • (1989) J. Inst. Brew. , vol.95 , pp. 29-33
    • MacGregor, A.W.1    Dushnicky, L.2
  • 81
    • 84987340413 scopus 로고
    • Starch degradation in endosperms of developing barley kernels
    • MacGregor, A.W. & Dushnicky, L. Starch degradation in endosperms of developing barley kernels. J. Inst. Brew, 1989b. Vol. 95, pp. 321-325.
    • (1989) J. Inst. Brew , vol.95 , pp. 321-325
    • MacGregor, A.W.1    Dushnicky, L.2
  • 82
    • 0002895097 scopus 로고
    • Carbohydrates in the barley grain
    • MacGregor, A.W. & Bhatty, R.S. (eds.) St. Paul: American Association of Cereal Chemists
    • MacGregor, A.W. & Fincher, G.B. Carbohydrates in the barley grain, In: MacGregor, A.W. & Bhatty, R.S. (eds.) Barley. Chemistry and technology. St. Paul: American Association of Cereal Chemists, 1993. Pp. 73-130.
    • (1993) Barley. Chemistry and Technology , pp. 73-130
    • MacGregor, A.W.1    Fincher, G.B.2
  • 83
    • 0001703223 scopus 로고
    • Changes in kernels during growth and maturation
    • MacGregor, A.W., LaBerge, D.E. & Meridith, W.O.S. Changes in kernels during growth and maturation. Cer. Chem., 1971. Vol. 48, pp. 255-269.
    • (1971) Cer. Chem. , vol.48 , pp. 255-269
    • MacGregor, A.W.1    LaBerge, D.E.2    Meridith, W.O.S.3
  • 84
    • 0001932045 scopus 로고
    • Limit dextrinase inhibitor in barley and malt and its possible role in malting and brewing
    • Brussels 1995. Oxford: IRL Press
    • 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. Proc. 25th Congr. Eur. Brew. Conv., Brussels 1995. Oxford: IRL Press, 1995. Pp. 185-192.
    • (1995) Proc. 25th Congr. Eur. Brew. Conv. , pp. 185-192
    • MacGregor, A.W.1    Macri, L.J.2    Bazin, S.L.3    Sadler, G.W.4
  • 85
    • 0000955950 scopus 로고
    • Limit dextrinase from malted barley: Extraction, purification and characterization
    • MacGregor, A.W., Macri, L.J., Schroeder S.W. & Bazin, S.L. Limit dextrinase from malted barley: extraction, purification and characterization. Cer. Chem., 1994a. Vol. 71, pp. 610-617.
    • (1994) Cer. Chem. , vol.71 , pp. 610-617
    • MacGregor, A.W.1    Macri, L.J.2    Schroeder, S.W.3    Bazin, S.L.4
  • 86
    • 0028095685 scopus 로고
    • Purification and characterisation of limit dextrinase inhibitors from barley
    • MacGregor, A.W., Macri, L.J., Schroeder, S.W. & Bazin, S.L. Purification and characterisation of limit dextrinase inhibitors from barley. J. Cer. Sci., 1994b. Vol. 20, pp. 33-41.
    • (1994) J. Cer. Sci. , vol.20 , pp. 33-41
    • MacGregor, A.W.1    Macri, L.J.2    Schroeder, S.W.3    Bazin, S.L.4
  • 87
    • 84979347204 scopus 로고
    • α-amylase components in excised, incubated barley embryos
    • MacGregor, A.W. & Marchylo, B.A. α-Amylase components in excised, incubated barley embryos. J. Inst. Brew., 1986. Vol. 92, pp. 159-161.
    • (1986) J. Inst. Brew. , vol.92 , pp. 159-161
    • MacGregor, A.W.1    Marchylo, B.A.2
  • 88
    • 0000922236 scopus 로고
    • Structure of amylopectins isolated from large and small starch granules of normal and waxy barley
    • MacGregor, A.W. & Morgan, J.E. Structure of amylopectins isolated from large and small starch granules of normal and waxy barley. Cer. Chem., 1984. Vol. 61, pp. 222-228.
    • (1984) Cer. Chem. , vol.61 , pp. 222-228
    • MacGregor, A.W.1    Morgan, J.E.2
  • 90
    • 7444266924 scopus 로고
    • The separation of limit dextrinase from R-enzyme and aspects of the activities of the separated enzymes
    • MacWilliam, I.C. & Harris, G. The separation of limit dextrinase from R-enzyme and aspects of the activities of the separated enzymes. Arch. Biochem. Biophys., 1959. Vol. 84, pp. 442-454.
    • (1959) Arch. Biochem. Biophys. , vol.84 , pp. 442-454
    • MacWilliam, I.C.1    Harris, G.2
  • 91
    • 0030066994 scopus 로고    scopus 로고
    • Application of gradient ion chromatography with pulsed electrochemical detection to the analysis of carbohydrates in brewing
    • Madigan, D., McMurrough, I. & Smyth, M.R., Application of gradient ion chromatography with pulsed electrochemical detection to the analysis of carbohydrates in brewing. J. Am. Soc. Brew. Chem., 1996. Vol. 54, pp. 45-49.
    • (1996) J. Am. Soc. Brew. Chem. , vol.54 , pp. 45-49
    • Madigan, D.1    McMurrough, I.2    Smyth, M.R.3
  • 92
    • 0001383739 scopus 로고
    • Purification of R-enzyme from malted barley and its role in in vitro digestion of barley starch granules
    • In Japanese
    • Maeda, I., Jimi, N., Taniguchi, H. & Nakamura, M. Purification of R-enzyme from malted barley and its role in in vitro digestion of barley starch granules. J. Jap. Soc. Starch Sci., 1979. Vol. 26, pp. 117-127. (In Japanese)
    • (1979) J. Jap. Soc. Starch Sci. , vol.26 , pp. 117-127
    • Maeda, I.1    Jimi, N.2    Taniguchi, H.3    Nakamura, M.4
  • 93
    • 0017896120 scopus 로고
    • Digestion of barley starch granules by the combined action of α- and β-amylase purified from barley and barley malt
    • Maeda, I., Kiribuchi, S. & Nakamura, M. Digestion of barley starch granules by the combined action of α- and β-amylase purified from barley and barley malt. Agric. Biol. Chem., 1978a. Vol. 42, pp. 259-267.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 259-267
    • Maeda, I.1    Kiribuchi, S.2    Nakamura, M.3
  • 94
    • 0000190052 scopus 로고
    • Purification of a debranching enzyme (R-enzyme) from malted barley, and the role of the enzyme in the digestion of starch granules during the germination of barley seeds
    • Maeda, I., Nikuni, Z., Taniguchi, H. & Nakamura, M. Purification of a debranching enzyme (R-enzyme) from malted barley, and the role of the enzyme in the digestion of starch granules during the germination of barley seeds. Carbohydr. Res., 1978b. Vol. 61, pp. 309-320.
    • (1978) Carbohydr. Res. , vol.61 , pp. 309-320
    • Maeda, I.1    Nikuni, Z.2    Taniguchi, H.3    Nakamura, M.4
  • 95
    • 0015173743 scopus 로고
    • Specificity of debranching enzymes
    • Manners, D.J. Specificity of debranching enzymes. Nature New Biology, 1971. Vol. 234, pp. 150-151.
    • (1971) Nature New Biology , vol.234 , pp. 150-151
    • Manners, D.J.1
  • 96
    • 0002773633 scopus 로고
    • Starch degradation during malting and mashing
    • Manners, D.J. Starch degradation during malting and mashing. Brew. Dig., 1974. Vol. 49, No 12, pp. 56-62.
    • (1974) Brew. Dig. , vol.49 , Issue.12 , pp. 56-62
    • Manners, D.J.1
  • 97
    • 0016657923 scopus 로고
    • Debranching enzymes in plant tissues
    • Manners, D.J. Debranching enzymes in plant tissues. Biochem. Soc. Trans., 1975. Vol. 3, pp. 49-53.
    • (1975) Biochem. Soc. Trans. , vol.3 , pp. 49-53
    • Manners, D.J.1
  • 98
    • 0000630359 scopus 로고
    • Some aspects on the structure of starch
    • Manners, D.J. Some aspects on the structure of starch. Cereal Foods World, 1985a. Vol. 30, pp. 461-467.
    • (1985) Cereal Foods World , vol.30 , pp. 461-467
    • Manners, D.J.1
  • 99
    • 0000063717 scopus 로고
    • Some aspects on the metabolism of starch
    • Manners, D.J. Some aspects on the metabolism of starch. Cereal Foods World, 1985b. Vol. 30, pp. 722-727.
    • (1985) Cereal Foods World , vol.30 , pp. 722-727
    • Manners, D.J.1
  • 100
    • 0008547976 scopus 로고
    • Studies on debranching enzymes. Part VI: The starch-debranching enzyme system of germinated barley
    • Manners, D.J. & Hardie, D.G. Studies on debranching enzymes. Part VI: The starch-debranching enzyme system of germinated barley. MBAA Tech. Quart., 1977. Vol. 14, pp. 120-125.
    • (1977) MBAA Tech. Quart. , vol.14 , pp. 120-125
    • Manners, D.J.1    Hardie, D.G.2
  • 101
    • 0014733151 scopus 로고
    • The specificity of cereal limit dextrinases
    • Manners, D.J., Marshall, J.J. & Yellowless, D. The specificity of cereal limit dextrinases. Biochem. J., 1970. Vol. 116, pp. 539-541.
    • (1970) Biochem. J. , vol.116 , pp. 539-541
    • Manners, D.J.1    Marshall, J.J.2    Yellowless, D.3
  • 102
    • 84978558746 scopus 로고
    • Studies on carbohydrate-metabolizing enzymes. Part XXV. The debranching enzyme system in germinated barley
    • Manners, D.J. & Rowe, K.L. Studies on carbohydrate-metabolizing enzymes. Part XXV. The debranching enzyme system in germinated barley. J. Inst. Brew, 1971. Vol. 77, pp. 358-365.
    • (1971) J. Inst. Brew , vol.77 , pp. 358-365
    • Manners, D.J.1    Rowe, K.L.2
  • 103
    • 84979183283 scopus 로고
    • Studies on carbohydrate-metabolizing enzymes. Part XIV. The specificity of R-enzyme from malted barley
    • Manners, D.J. & Sparra, K.L. Studies on carbohydrate-metabolizing enzymes. Part XIV. The specificity of R-enzyme from malted barley. J. Inst. Brew., 1966. Vol. 72, pp. 360-365.
    • (1966) J. Inst. Brew. , vol.72 , pp. 360-365
    • Manners, D.J.1    Sparra, K.L.2
  • 104
    • 84983947206 scopus 로고
    • Studies on carbohydrate metabolising enzymes. Part XXVI. The limit dextrinase from germinated barley
    • Manners, D.J. & Yellowlees, D. Studies on carbohydrate metabolising enzymes. Part XXVI. The limit dextrinase from germinated barley. Starch, 1971. Vol. 23, pp. 228-234.
    • (1971) Starch , vol.23 , pp. 228-234
    • Manners, D.J.1    Yellowlees, D.2
  • 105
    • 84978584849 scopus 로고
    • Studies on debranching enzymes. Part I. The limit dextrinase activity of extracts of certain higher plants and commercial malts
    • Manners, D.J. & Yellowlees, D. Studies on debranching enzymes. Part I. The limit dextrinase activity of extracts of certain higher plants and commercial malts. J. Inst. Brew., 1973. Vol. 79, pp. 377-385.
    • (1973) J. Inst. Brew. , vol.79 , pp. 377-385
    • Manners, D.J.1    Yellowlees, D.2
  • 106
    • 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., 1992. Vol. 227, pp. 257-268.
    • (1992) Carbohydr. Res. , vol.227 , pp. 257-268
    • McCleary, B.V.1
  • 107
    • 84987346517 scopus 로고
    • Measurement of β-amylase in cereal flours and commercial enzyme preparations
    • McCleary, B.V. & Codd, R. Measurement of β-amylase in cereal flours and commercial enzyme preparations. J. Cer. Sci., 1989. Vol. 9, pp. 17-33.
    • (1989) J. Cer. Sci. , vol.9 , pp. 17-33
    • McCleary, B.V.1    Codd, R.2
  • 108
    • 0011817910 scopus 로고
    • Measurement of cereal α-amylase: A new assay procedure
    • McCleary, B.V. & Sheenan, H. Measurement of cereal α-amylase: a new assay procedure. J. Cer. Sci., 1987. Vol. 6, pp. 237-251.
    • (1987) J. Cer. Sci. , vol.6 , pp. 237-251
    • McCleary, B.V.1    Sheenan, H.2
  • 110
    • 84866196182 scopus 로고
    • Limit dextrinase from sorghum. In vivo synthesis and purification of the enzyme
    • Mélotte, L., Debuysschere, S. & Dufour, J.P. Limit dextrinase from sorghum. In vivo synthesis and purification of the enzyme. Brew. Dig., 1994. Vol. 69, No 3, pp. 17-18.
    • (1994) Brew. Dig. , vol.69 , Issue.3 , pp. 17-18
    • Mélotte, L.1    Debuysschere, S.2    Dufour, J.P.3
  • 111
    • 7444254463 scopus 로고
    • Distribution of protein and free and bound amylase in cereal species
    • Meredith, W.O.S. Distribution of protein and free and bound amylase in cereal species. Proc. Am. Soc. Brew. Chem., 1966. Pp. 32-38.
    • (1966) Proc. Am. Soc. Brew. Chem. , pp. 32-38
    • Meredith, W.O.S.1
  • 113
    • 85016668976 scopus 로고
    • An improved colorimetric procedure for determining apparent and total amylose in cereal and other starches
    • Morrison, W.R. & Laignelet, B. An improved colorimetric procedure for determining apparent and total amylose in cereal and other starches. J. Cer. Sci., 1983. Vol. 1, pp. 9-20.
    • (1983) J. Cer. Sci. , vol.1 , pp. 9-20
    • Morrison, W.R.1    Laignelet, B.2
  • 114
    • 0002294076 scopus 로고
    • Barley α-amylase/subtilsin inhibitor. I. Isolation and characterization
    • Mundy, J., Svendsen, I. & Hejgaard, J. Barley α-amylase/subtilsin inhibitor. I. Isolation and characterization. Carlsberg Res. Comm., 1983. Vol. 48, pp. 81-90.
    • (1983) Carlsberg Res. Comm. , vol.48 , pp. 81-90
    • Mundy, J.1    Svendsen, I.2    Hejgaard, J.3
  • 115
    • 84871005770 scopus 로고
    • Über Grenzdextrine und Stärke. XVIII. Mitteilung. Über Grenzdextrine aus Kartoffel-, Reis- und Weizenstärke
    • In German
    • Myrbäck, K., Örtenblad, B. & Ahlborg, K. Über Grenzdextrine und Stärke. XVIII. Mitteilung. Über Grenzdextrine aus Kartoffel-, Reis- und Weizenstärke. Biochem. Z. 1943. Vol. 315, pp. 240-249. (In German)
    • (1943) Biochem. Z. , vol.315 , pp. 240-249
    • Myrbäck, K.1    Örtenblad, B.2    Ahlborg, K.3
  • 116
    • 84928194867 scopus 로고
    • Der Einfluss des Schwelkprozesses auf die Entwicklung der Enzyme und einiger anderen Stoffgruppen des Malzes
    • Salzburg 1973, Amsterdam: Elsevier Scientific Publishing Company (In German)
    • Narziß, L., Rusitzka, P. & Stippler, K. Der Einfluss des Schwelkprozesses auf die Entwicklung der Enzyme und einiger anderen Stoffgruppen des Malzes. Proc. 14th Congr. Eur. Brew. Conv., Salzburg 1973, Amsterdam: Elsevier Scientific Publishing Company 1974. Pp. 85-98. (In German)
    • (1974) Proc. 14th Congr. Eur. Brew. Conv. , pp. 85-98
    • Narziß, L.1    Rusitzka, P.2    Stippler, K.3
  • 117
    • 0007709824 scopus 로고
    • Brewing with barley and enzymes - A review
    • Estoril 1971. Amsterdam: Elsevier Publishing Company
    • Nielsen, E.B. Brewing with barley and enzymes - a review. Proc. 13th Congr. Eur. Brew. Conv., Estoril 1971. Amsterdam: Elsevier Publishing Company, 1972. Pp. 149-170.
    • (1972) Proc. 13th Congr. Eur. Brew. Conv. , pp. 149-170
    • Nielsen, E.B.1
  • 118
    • 0016585779 scopus 로고
    • Some properties of crystalline extra- and intra-cellular pullulanases from Aerobacter aerogenes
    • Ohba, R. & Ueda, S. Some properties of crystalline extra- and intra-cellular pullulanases from Aerobacter aerogenes. Agr. Biol. Chem., 1975. Vol. 39, pp. 967-972.
    • (1975) Agr. Biol. Chem. , vol.39 , pp. 967-972
    • Ohba, R.1    Ueda, S.2
  • 119
    • 0007551883 scopus 로고
    • Starch degradation in spinach leaves
    • Okita, T.W. & Preiss, J. Starch degradation in spinach leaves. Plant Physiol., 1980. Vol. 66, pp. 870-876.
    • (1980) Plant Physiol. , vol.66 , pp. 870-876
    • Okita, T.W.1    Preiss, J.2
  • 120
    • 7444252312 scopus 로고
    • The analysis of beer, worts and brewing suryps for sugars and oligosaccharides
    • Interlaken 1969. Amsterdam: Elsevier Publishing Company
    • Otter, G.E., Popplewell, J.A. & Taylor, L. The analysis of beer, worts and brewing suryps for sugars and oligosaccharides. Proc. 12th Congr. Eur. Brew. Conv., Interlaken 1969. Amsterdam: Elsevier Publishing Company, 1970. Pp 481-495.
    • (1970) Proc. 12th Congr. Eur. Brew. Conv. , pp. 481-495
    • Otter, G.E.1    Popplewell, J.A.2    Taylor, L.3
  • 121
    • 0000105922 scopus 로고
    • Cereals in malting and brewing
    • Palmer, G.H. (ed.) Aberdeen: Aberdeen University Press
    • Pakner, G.H. Cereals in malting and brewing, In: Palmer, G.H. (ed.) Cereal science and technology. Aberdeen: Aberdeen University Press, 1989. Pp. 61-242.
    • (1989) Cereal Science and Technology , pp. 61-242
    • Pakner, G.H.1
  • 122
    • 7444231125 scopus 로고    scopus 로고
    • Pat. US 4251630. Preparation of a malt high in alpha-1,6-hydrolase. Kurth Malting. (Pratt, G.W., Chapelle, T.W. & Fahy, M.J). Appl. 928812 28.07.1978, Publ. 17.02.1981
    • Pat. US 4251630. Preparation of a malt high in alpha-1,6-hydrolase. Kurth Malting. (Pratt, G.W., Chapelle, T.W. & Fahy, M.J). Appl. 928812 28.07.1978, Publ. 17.02.1981.
  • 123
    • 0347906300 scopus 로고
    • Malt modification and mashing conditions as influencing factors on the carbohydrates of wort
    • Piendl, A. Malt modification and mashing conditions as influencing factors on the carbohydrates of wort. Brew. Dig., 1973. Vol. 48, No 9, pp. 58-72.
    • (1973) Brew. Dig. , vol.48 , Issue.9 , pp. 58-72
    • Piendl, A.1
  • 125
    • 84987306900 scopus 로고
    • The contribution of dextrins to sensory properties. Part I. Mouthfeel
    • Ragot, F., Guinard, J-X., Shoemaker, C.F. & Lewis, M.J. The contribution of dextrins to sensory properties. Part I. Mouthfeel. J. Inst. Brew., 1989. Vol. 95, pp. 427-430.
    • (1989) J. Inst. Brew. , vol.95 , pp. 427-430
    • Ragot, F.1    Guinard, J.-X.2    Shoemaker, C.F.3    Lewis, M.J.4
  • 126
    • 7444254084 scopus 로고
    • Sequence of a cDNA of the Spinacia oleracea L. Starch Debranching enzyme (EMBL/GenBank X83969) (PGR95-010)
    • Renz, A., Schmid, B.R., Koámann, O.J. and Beck, E. Sequence of a cDNA of the Spinacia oleracea L. Starch Debranching enzyme (EMBL/GenBank X83969) (PGR95-010). Plant Physiol., 1995. Vol. 108, p. 1342.
    • (1995) Plant Physiol. , vol.108 , pp. 1342
    • Renz, A.1    Schmid, B.R.2    Koámann, O.J.3    Beck, E.4
  • 127
    • 0000443871 scopus 로고
    • On barley amylase and proteinase
    • Sandegren, E. & Klang, N. On barley amylase and proteinase. J. Inst. Brew., 1950. Vol. 56, pp. 313-318.
    • (1950) J. Inst. Brew. , vol.56 , pp. 313-318
    • Sandegren, E.1    Klang, N.2
  • 128
    • 0028857759 scopus 로고
    • Structural analysis of starch from normal and shx (shrunken endosperm) barley (Hordeum vulgare L.)
    • Schulman, A.H., Tomooka, S., Suzuki, A., Myllärinen, P. & Hizukuri, S. Structural analysis of starch from normal and shx (shrunken endosperm) barley (Hordeum vulgare L.). Carbohydr. Res., 1995. Vol. 275, pp. 361-369.
    • (1995) Carbohydr. Res. , vol.275 , pp. 361-369
    • Schulman, A.H.1    Tomooka, S.2    Suzuki, A.3    Myllärinen, P.4    Hizukuri, S.5
  • 129
    • 84866190460 scopus 로고
    • Beurteilung der Sudhausarbeit anhand des Stärkeabbaugrades
    • In German
    • Schur, F. Beurteilung der Sudhausarbeit anhand des Stärkeabbaugrades. Brauwelt, 1985. Vol. 125, pp. 1195-1199. (In German)
    • (1985) Brauwelt , vol.125 , pp. 1195-1199
    • Schur, F.1
  • 130
    • 7444230548 scopus 로고
    • Charackterisierung filtrationshemmender Stoffe. 2. Mitteilung: Photometrische Jodprobe
    • In German
    • Schur, F., Anderegg, P. & Pfenninger, H. Charackterisierung filtrationshemmender Stoffe. 2. Mitteilung: Photometrische Jodprobe. Brauerei-Rundschau, 1978. Vol. 89, pp. 129-132. (In German)
    • (1978) Brauerei-Rundschau , vol.89 , pp. 129-132
    • Schur, F.1    Anderegg, P.2    Pfenninger, H.3
  • 131
    • 0342730390 scopus 로고
    • Limit dextrinase in cereal seeds
    • Serre, L. & Laurière, C. Limit dextrinase in cereal seeds. Sciences des Aliments, 1989. Vol. 9, pp. 645-663.
    • (1989) Sciences des Aliments , vol.9 , pp. 645-663
    • Serre, L.1    Laurière, C.2
  • 132
    • 0025327498 scopus 로고
    • Specific assay of α-dextrin-6-glucanohydrolase using labeled pullulan
    • Serre, L. & Laurière, C. Specific assay of α-dextrin-6-glucanohydrolase using labeled pullulan. Anal. Biochem., 1990. Vol. 186, pp. 312-315.
    • (1990) Anal. Biochem. , vol.186 , pp. 312-315
    • Serre, L.1    Laurière, C.2
  • 133
    • 84980151293 scopus 로고
    • Activation of enzymes during germination: Amylopectin-1,6-glucosidase in peas
    • Shain, Y. & Mayer, A.M. Activation of enzymes during germination: amylopectin-1,6-glucosidase in peas. Physiologia Plantarum, 1968. Vol. 21, pp. 765-776.
    • (1968) Physiologia Plantarum , vol.21 , pp. 765-776
    • Shain, Y.1    Mayer, A.M.2
  • 134
    • 0001864307 scopus 로고    scopus 로고
    • Studies on the activation and release of bound limit dextrinase in malted barley
    • Sissons, M.J. Studies on the activation and release of bound limit dextrinase in malted barley. J. Am. Soc. Brew. Chem., 1996. Vol. 54, pp. 19-25.
    • (1996) J. Am. Soc. Brew. Chem. , vol.54 , pp. 19-25
    • Sissons, M.J.1
  • 135
    • 7444252311 scopus 로고
    • Relationship between limit dextrinase activity and apparent attenuation limit in barley malted for extended periods
    • Sissons, M.J., Lance, R.C.M. & Sparrow, D.H.B. Relationship between limit dextrinase activity and apparent attenuation limit in barley malted for extended periods. Chem. Aust., 1991. Vol. 58, pp. 306-308.
    • (1991) Chem. Aust. , vol.58 , pp. 306-308
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 136
    • 85013160792 scopus 로고
    • Studies on limit dextrinase in barley: I. Purification of malt limit dextrinase and production of monospecific antibodies
    • Sissons, M.J., Lance, R.C.M. & Sparrow, D.H.B. Studies on limit dextrinase in barley: I. Purification of malt limit dextrinase and production of monospecific antibodies. J. Cer. Sci., 1992a. Vol. 16, pp. 107-116.
    • (1992) J. Cer. Sci. , vol.16 , pp. 107-116
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 137
    • 0343530563 scopus 로고
    • Studies on limit dextrinase in barley: II. Application of an ELISA and immunoblotting to studies of genetic variability and malting effects
    • Sissons, M.J., Lance, R.C.M. & Sparrow, D.H.B. Studies on limit dextrinase in barley: II. Application of an ELISA and immunoblotting to studies of genetic variability and malting effects, J. Cer. Sci., 1992b. Vol. 16, pp. 117-128.
    • (1992) J. Cer. Sci. , vol.16 , pp. 117-128
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 138
    • 0010980673 scopus 로고
    • Studies on limit dextrinase in barley: 3. Limit dextrinase in developing kernels
    • Sissons, M.J., Lance, R.C.M. & Sparrow, D.H.B. Studies on limit dextrinase in barley: 3. Limit dextrinase in developing kernels. J. Cer. Sci., 1993. Vol. 17, pp. 19-24.
    • (1993) J. Cer. Sci. , vol.17 , pp. 19-24
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 139
    • 1042272793 scopus 로고
    • Bound and free forms of barley limit dextrinase
    • Sissons, M.J., Lance, R.C.M. & Wallance, W. Bound and free forms of barley limit dextrinase. Cer. Chem., 1994. Vol. 71, pp. 520-521.
    • (1994) Cer. Chem. , vol.71 , pp. 520-521
    • Sissons, M.J.1    Lance, R.C.M.2    Wallance, W.3
  • 140
    • 0004670366 scopus 로고
    • Hydrolysis of barley starch granules by α-glucosidases from malt
    • Sissons, M.J. & MacGregor, A.W. Hydrolysis of barley starch granules by α-glucosidases from malt. J. Cer. Sci., 1994. Vol. 19, pp. 161-169.
    • (1994) J. Cer. Sci. , vol.19 , pp. 161-169
    • Sissons, M.J.1    MacGregor, A.W.2
  • 141
    • 0003149025 scopus 로고
    • Barley malt limit dextrinase: Its extraction, heat stability and activity during malting and mashing
    • Sissons, M.J., Taylor, M. & Proudlove, M. Barley malt limit dextrinase: Its extraction, heat stability and activity during malting and mashing. J. Am. Soc. Brew. Chem., 1995. Vol. 53, pp. 104-110.
    • (1995) J. Am. Soc. Brew. Chem. , vol.53 , pp. 104-110
    • Sissons, M.J.1    Taylor, M.2    Proudlove, M.3
  • 142
    • 0001133521 scopus 로고
    • Is there a role for limit dextrinase in mashing?
    • Brussels 1995. Oxford: IRL Press
    • Sjöholm, K., Macri, L.J. & MacGregor, A.W. Is there a role for limit dextrinase in mashing? Proc. 25th Congr. Eur. Brew. Conv., Brussels 1995. Oxford: IRL Press, 1995. Pp. 277-284.
    • (1995) Proc. 25th Congr. Eur. Brew. Conv. , pp. 277-284
    • Sjöholm, K.1    Macri, L.J.2    MacGregor, A.W.3
  • 144
    • 7444262992 scopus 로고
    • Versuche zur Opimierung des Maischverfahrens
    • In German
    • Sommer, G. Versuche zur Opimierung des Maischverfahrens. Brauwelt, 1985. Vol. 125, pp. 1121-1126. (In German)
    • (1985) Brauwelt , vol.125 , pp. 1121-1126
    • Sommer, G.1
  • 145
    • 84897584785 scopus 로고
    • Release and activity of bound β-amylase in germinating barley grain
    • Sopanen, T. & Laurière, C. Release and activity of bound β-amylase in germinating barley grain. Plant Physiol., 1989. Vol. 89, pp. 244-249.
    • (1989) Plant Physiol. , vol.89 , pp. 244-249
    • Sopanen, T.1    Laurière, C.2
  • 146
    • 84987368494 scopus 로고
    • Evidence for the presence of maltase and α-glucosidase isoenzymes in barley
    • Stark, J.R. & Yin, X.S. Evidence for the presence of maltase and α-glucosidase isoenzymes in barley. J. Inst. Brew., 1987. Vol. 93, pp. 108-112.
    • (1987) J. Inst. Brew. , vol.93 , pp. 108-112
    • Stark, J.R.1    Yin, X.S.2
  • 147
    • 7444261502 scopus 로고    scopus 로고
    • Are the days of congress mashing over?
    • The Inst. Brew. Victoria falls, 1996. The Institute of Brewing
    • Stenholm, K., Home, S., Pietilä, K., Jaakkola, N. & Leino, E. Are the days of congress mashing over? Proc. Barley, Malt & Wort Symposium. The Inst. Brew. Victoria falls, 1996. The Institute of Brewing 1996b. Pp. 149-163.
    • (1996) Proc. Barley, Malt & Wort Symposium , pp. 149-163
    • Stenholm, K.1    Home, S.2    Pietilä, K.3    Jaakkola, N.4    Leino, E.5
  • 149
    • 0026017112 scopus 로고
    • Gel permeation chromatographic determination of starches using alkaline eluents
    • Suortti, T. & Pessa, E. Gel permeation chromatographic determination of starches using alkaline eluents. J. Chromatogr., 1991. Vol. 536, pp. 251-254.
    • (1991) J. Chromatogr. , vol.536 , pp. 251-254
    • Suortti, T.1    Pessa, E.2
  • 150
    • 0026028264 scopus 로고
    • A hypertermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability
    • Suzuki, Y., Hatagaki, K. & Oda, H. A hypertermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability. Appl. Microbiol. Biotechnol., 1991. Vol. 34, pp. 707-714.
    • (1991) Appl. Microbiol. Biotechnol. , vol.34 , pp. 707-714
    • Suzuki, Y.1    Hatagaki, K.2    Oda, H.3
  • 151
    • 0001592425 scopus 로고
    • Carbohydrates in brewing. 1. Determination of fermentable sugars and oligosaccharides in wort and beer by partition HPLC
    • Uchida, M., Nakatani, K., Ono, M. & Nagami, K. Carbohydrates in brewing. 1. Determination of fermentable sugars and oligosaccharides in wort and beer by partition HPLC. J. Am. Soc. Brew. Chem., 1991. Vol. 49, pp. 65-73.
    • (1991) J. Am. Soc. Brew. Chem. , vol.49 , pp. 65-73
    • Uchida, M.1    Nakatani, K.2    Ono, M.3    Nagami, K.4
  • 152
    • 0019319617 scopus 로고
    • On the ability of pullulanse to stimulate the enzymic digestion of starch
    • Ueda, S. & Marshall, J.J. On the ability of pullulanse to stimulate the enzymic digestion of starch. Carbohydr. Res., 1980. Vol. 84, pp. 196-199.
    • (1980) Carbohydr. Res. , vol.84 , pp. 196-199
    • Ueda, S.1    Marshall, J.J.2
  • 153
    • 7444224808 scopus 로고
    • Pullulanase responsible for digesting raw starch
    • Ueda, S. & Ohba, R. Pullulanase responsible for digesting raw starch. Starch, 1976. Vol. 28, pp. 20-22.
    • (1976) Starch , vol.28 , pp. 20-22
    • Ueda, S.1    Ohba, R.2
  • 154
    • 0001432052 scopus 로고
    • An endogenous α-amylase inhibitor in barley kernels
    • Weselake, R.J., MacGregor, A.W. & Hill, R.D. An endogenous α-amylase inhibitor in barley kernels. Plant Physiol., 1983. Vol. 72, pp. 809-812.
    • (1983) Plant Physiol. , vol.72 , pp. 809-812
    • Weselake, R.J.1    MacGregor, A.W.2    Hill, R.D.3
  • 155
    • 0007317320 scopus 로고
    • The addition of starch debranching enzymes to mashing and fermentation and their influence on attenuation
    • Willox, I.C., Rader, S.R., Riolo, J.M. & Stem, H. The addition of starch debranching enzymes to mashing and fermentation and their influence on attenuation. MBAA Tech. Quart., 1977. Vol. 14, pp. 105-110.
    • (1977) MBAA Tech. Quart. , vol.14 , pp. 105-110
    • Willox, I.C.1    Rader, S.R.2    Riolo, J.M.3    Stem, H.4
  • 156
    • 0008530430 scopus 로고
    • Conversion of active and inactive debranching enzymes in rice seeds
    • Yamada, J. Conversion of active and inactive debranching enzymes in rice seeds. Agric. Biol. Chem., 1981a. Vol. 45, pp. 747-750.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 747-750
    • Yamada, J.1
  • 157
    • 0008567441 scopus 로고
    • Inactive debranching-enzyme in rice seeds, and its activation
    • Yamada, J. Inactive debranching-enzyme in rice seeds, and its activation. Carbohydr. Res., 1981b. Vol. 90, pp. 153-157.
    • (1981) Carbohydr. Res. , vol.90 , pp. 153-157
    • Yamada, J.1
  • 158
    • 0041623284 scopus 로고
    • Purification of oat debranching enzyme and occurrence of inactive debranching enzyme in cereals
    • Yamada, J. Purification of oat debranching enzyme and occurrence of inactive debranching enzyme in cereals. Agric. Biol. Chem., 1981c. Vol. 45, pp. 1013-1015.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 1013-1015
    • Yamada, J.1
  • 159
    • 0043126076 scopus 로고
    • Purification of debranching enzyme from mature rice seeds
    • Yamada, J. Purification of debranching enzyme from mature rice seeds. Agr. Biol. Chem., 1981d. Vol. 45, pp. 1269-1270.
    • (1981) Agr. Biol. Chem. , vol.45 , pp. 1269-1270
    • Yamada, J.1
  • 160
    • 0043126075 scopus 로고
    • A debranching enzyme of rice seeds at milky stage, its purification and substrates specificities
    • Yamada, J. & Izawa, M. A debranching enzyme of rice seeds at milky stage, its purification and substrates specificities. Agric. Biol. Chem., 1979a. Vol. 43, pp. 37-44.
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 37-44
    • Yamada, J.1    Izawa, M.2
  • 161
    • 7444256198 scopus 로고
    • Mode of action of a rice debranching enzyme on pullulan and its related oligosaccharides
    • Yamada, J. & Izawa, M. Mode of action of a rice debranching enzyme on pullulan and its related oligosaccharides. Agric. Biol. Chem., 1979b. Vol. 43, pp. 2515-2521.
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 2515-2521
    • Yamada, J.1    Izawa, M.2
  • 162
    • 7444239814 scopus 로고
    • Purification and characterization of a debranching enzyme of germinated rice seeds
    • Yamada, J., Tanba, H. & Izawa, M. Purification and characterization of a debranching enzyme of germinated rice seeds. J. Fac. Agr. Hokk. Univ., 1980. Vol. 60, pp. 10-22.
    • (1980) J. Fac. Agr. Hokk. Univ. , vol.60 , pp. 10-22
    • Yamada, J.1    Tanba, H.2    Izawa, M.3
  • 163
    • 0023287102 scopus 로고
    • Detection of pullulanase in polyacrylamide gels using pullulan-Reactive Red agar plates
    • Yang, S-S. & Coleman, R.D. Detection of pullulanase in polyacrylamide gels using pullulan-Reactive Red agar plates. Anal. Biochem., 1987. Vol. 160, pp. 480-482.
    • (1987) Anal. Biochem. , vol.160 , pp. 480-482
    • Yang, S.-S.1    Coleman, R.D.2
  • 164
    • 0019050301 scopus 로고
    • Purification and characterization of limit dextrinase from Pisum sativum L.
    • Yellowlees, D. Purification and characterization of limit dextrinase from Pisum sativum L. Carbohydr. Res., 1980. Vol. 83, pp. 109-118.
    • (1980) Carbohydr. Res. , vol.83 , pp. 109-118
    • Yellowlees, D.1
  • 165
    • 0000700014 scopus 로고
    • Characterization of germinated barley endoproteolytic enzymes by two-dimensional gel electrophoresis
    • Zhang, N. & Jones, B.L. Characterization of germinated barley endoproteolytic enzymes by two-dimensional gel electrophoresis. J. Cer. Sci., 1995. Vol. 21, pp. 145-153.
    • (1995) J. Cer. Sci. , vol.21 , pp. 145-153
    • Zhang, N.1    Jones, B.L.2


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