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Volumn 26, Issue 2, 1997, Pages 241-250

Measurement of beta-amylase in malting barley (Hordeum vulgare L.). II. The effect of germination and kilning

Author keywords

Barley; beta amylase; ELISA; Malting

Indexed keywords

HORDEUM; HORDEUM VULGARE SUBSP. VULGARE;

EID: 0000261095     PISSN: 07335210     EISSN: None     Source Type: Journal    
DOI: 10.1006/jcrs.1997.0120     Document Type: Article
Times cited : (61)

References (24)
  • 2
    • 84981588438 scopus 로고
    • Free and protein-bound β-amylases of barley grain. Characterisation by two dimensional immuno-electrophoresis
    • Hejgaard, J. Free and protein-bound β-amylases of barley grain. Characterisation by two dimensional immuno-electrophoresis. Physiologia Plantarum 38 (1976) 293-299.
    • (1976) Physiologia Plantarum , vol.38 , pp. 293-299
    • Hejgaard, J.1
  • 3
    • 84897584785 scopus 로고
    • Release and activity of bound β-amylase in germinating barley grain
    • Sopanen, T. and Laurière, C. Release and activity of bound β-amylase in germinating barley grain. Plant Physiology 89 (1989) 244-249.
    • (1989) Plant Physiology , vol.89 , pp. 244-249
    • Sopanen, T.1    Laurière, C.2
  • 4
    • 0001876687 scopus 로고
    • Release and activation of barley beta-amylase by malt endopeptidases
    • Guerin, J.R., Lance, R.C.M. and Wallace, W. Release and activation of barley beta-amylase by malt endopeptidases. Journal of the Cereal Science 15 (1992) 5-14.
    • (1992) Journal of the Cereal Science , vol.15 , pp. 5-14
    • Guerin, J.R.1    Lance, R.C.M.2    Wallace, W.3
  • 5
    • 0040860049 scopus 로고
    • Association of bound beta-amylase with protein bodies in barley
    • Tronier, B. and Ory, R.L. Association of bound beta-amylase with protein bodies in barley. Cereal Chemistry 47 (1970) 464-471.
    • (1970) Cereal Chemistry , vol.47 , pp. 464-471
    • Tronier, B.1    Ory, R.L.2
  • 6
    • 0000992348 scopus 로고
    • Conversion of free β-amylase to bound β-amylase on starch granules in barley endosperm during desiccation phase of seed development
    • Hara-Nishimura, I., Nishimura, M. and Daussant, J. Conversion of free β-amylase to bound β-amylase on starch granules in barley endosperm during desiccation phase of seed development. Protoplasma 134 (1986) 149-153.
    • (1986) Protoplasma , vol.134 , pp. 149-153
    • Hara-Nishimura, I.1    Nishimura, M.2    Daussant, J.3
  • 7
    • 84913845038 scopus 로고
    • Immuno-histochemical localisation of β-amylase in resting barley seeds
    • Laurière, C., Laurière, M. and Daussant, J. Immuno-histochemical localisation of β-amylase in resting barley seeds. Physiologia Plantarum 67 (1986) 383-388.
    • (1986) Physiologia Plantarum , vol.67 , pp. 383-388
    • Laurière, C.1    Laurière, M.2    Daussant, J.3
  • 8
    • 0001391690 scopus 로고
    • The four major forms of barley beta-amylase, purification, characterisation and structural relationship
    • Lundgard, R. and Svensson, B.N. The four major forms of barley beta-amylase, purification, characterisation and structural relationship. Carlsberg Research Communications 52 (1987) 313-326.
    • (1987) Carlsberg Research Communications , vol.52 , pp. 313-326
    • Lundgard, R.1    Svensson, B.N.2
  • 13
    • 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. Journal of Cereal Science 9 (1989) 17-33.
    • (1989) Journal of Cereal Science , vol.9 , pp. 17-33
    • McCleary, B.V.1    Codd, R.2
  • 14
    • 0001220955 scopus 로고
    • Relationships of barley proteins soluble in sodium dodecyl sulphate to malting quality and varietal identification
    • Smith, D.B. and Simpson, P.A. Relationships of barley proteins soluble in sodium dodecyl sulphate to malting quality and varietal identification. Journal of Cereal Science 1 (1983) 185-197.
    • (1983) Journal of Cereal Science , vol.1 , pp. 185-197
    • Smith, D.B.1    Simpson, P.A.2
  • 15
    • 0000828213 scopus 로고
    • Wheat starch granule proteins and their technological significance
    • (I.D. Morton, ed.), Ellis Horwood, Chichester, UK
    • Schofield, J.D. and Greenwell, P. Wheat starch granule proteins and their technological significance. In 'Cereals in a European context' (I.D. Morton, ed.), Ellis Horwood, Chichester, UK, (1987) pp 407-420.
    • (1987) Cereals in a European Context , pp. 407-420
    • Schofield, J.D.1    Greenwell, P.2
  • 16
    • 0040265601 scopus 로고
    • Latent β-amylase of wheat: Its mode of attachment to glutenin and its release
    • Rowsell, R.V. and Goad, L.J. Latent β-amylase of wheat: its mode of attachment to glutenin and its release. Biochemical Journal 84 (1962) 73-74.
    • (1962) Biochemical Journal , vol.84 , pp. 73-74
    • Rowsell, R.V.1    Goad, L.J.2
  • 17
    • 0001368750 scopus 로고
    • Genetic control and biochemical properties of some high molecular weight albumins in bread wheat
    • Gupta, R.B., Shepherd, K.W. and MacRichie, F. Genetic control and biochemical properties of some high molecular weight albumins in bread wheat. Journal of Cereal Science 13 (1991) 221-235.
    • (1991) Journal of Cereal Science , vol.13 , pp. 221-235
    • Gupta, R.B.1    Shepherd, K.W.2    MacRichie, F.3
  • 19
    • 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 (1984) 172-177.
    • (1984) Planta , vol.161 , pp. 172-177
    • Giese, H.1    Hejgaard, J.2
  • 20
    • 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. Photochemistry 14 (1975) 1719-1722.
    • (1975) Photochemistry , vol.14 , pp. 1719-1722
    • Hardie, D.G.1
  • 21
    • 84987277559 scopus 로고
    • Malt diastatic power. Part II. A modified EBC diastatic power assay for the selective estimation of beta-amylase activity. Time and temperature dependence of the release of reducing sugar
    • Delcour, J.A. and Verschaeve, S.G. Malt diastatic power. Part II. A modified EBC diastatic power assay for the selective estimation of beta-amylase activity. Time and temperature dependence of the release of reducing sugar. Journal of Institute of Brewing 93 (1987) 296-301.
    • (1987) Journal of Institute of Brewing , vol.93 , pp. 296-301
    • Delcour, J.A.1    Verschaeve, S.G.2
  • 23
    • 0029141870 scopus 로고
    • Genetic and environmental variation in the diastatic power of Australian barley
    • Arends, A.M., Fox, G.P., Henry, R.J. and Symons, M.H. Genetic and environmental variation in the diastatic power of Australian barley. Journal of Cereal Science 21 (1995) 63-70.
    • (1995) Journal of Cereal Science , vol.21 , pp. 63-70
    • Arends, A.M.1    Fox, G.P.2    Henry, R.J.3    Symons, M.H.4
  • 24
    • 84987278682 scopus 로고
    • Diastatic power in malted barley: Contributions of malt parameters to its development and the potential of barley grain beta-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 beta-amylase to predict malt diastatic power. Journal of the Institute of Brewing 101 (1995) 277-280.
    • (1995) Journal of the Institute of Brewing , vol.101 , pp. 277-280
    • Gibson, T.S.1    Solah, V.2    Glennie-Holmes, M.R.3    Taylor, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.