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Volumn 64, Issue 2, 2006, Pages 69-78

The impact of microorganisms on barley and malt quality - A review

Author keywords

[No Author keywords available]

Indexed keywords

HORDEUM VULGARE SUBSP. VULGARE;

EID: 33646351977     PISSN: 03610470     EISSN: None     Source Type: Journal    
DOI: 10.1094/ASBCJ-64-0069     Document Type: Review
Times cited : (56)

References (167)
  • 1
    • 0032436775 scopus 로고    scopus 로고
    • Mycoflora of South African barley and malt
    • Ackermann, A. Mycoflora of South African barley and malt. J. Am. Soc. Brew. Chem. 56:169-176, 1998.
    • (1998) J. Am. Soc. Brew. Chem. , vol.56 , pp. 169-176
    • Ackermann, A.1
  • 4
    • 0007427410 scopus 로고
    • The microflora of barley and its effect on wort and beer
    • Anderson, K., Gjertsen, P., and Trolle, B. The microflora of barley and its effect on wort and beer. Brew. Dig. 42(8):76-81, 1967.
    • (1967) Brew. Dig. , vol.42 , Issue.8 , pp. 76-81
    • Anderson, K.1    Gjertsen, P.2    Trolle, B.3
  • 5
    • 0025296914 scopus 로고
    • Lipid transfer in plants
    • Arondel, V., and Kader, J. C. Lipid transfer in plants. Experimentia 46:576-585, 1991.
    • (1991) Experimentia , vol.46 , pp. 576-585
    • Arondel, V.1    Kader, J.C.2
  • 9
    • 33646344143 scopus 로고
    • Investigations into the microbiology of malting barley and wheat. Part 1: The composition of the microflora on freshly harvested grain
    • Beck, R., Lepschy, J., Steinke, S., and Suss, A. (1991) Investigations into the microbiology of malting barley and wheat. Part 1: The composition of the microflora on freshly harvested grain. Brauwelt 131:2472, 2474-2479.
    • (1991) Brauwelt , vol.131 , pp. 2472
    • Beck, R.1    Lepschy, J.2    Steinke, S.3    Suss, A.4
  • 10
    • 0025976182 scopus 로고
    • A new family of small (5 kDa) protein inhibitors in insect α-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat γ-purothionins
    • Bloch, C., and Richardson, M. A new family of small (5 kDa) protein inhibitors in insect α-amylases from seeds of sorghum (Sorghum bicolor (L) Moench) have sequence homologies with wheat γ-purothionins. FEBS (Fed. Eur. Brew. Soc.) Lett. 279:101-104, 1991.
    • (1991) FEBS (Fed. Eur. Brew. Soc.) Lett. , vol.279 , pp. 101-104
    • Bloch, C.1    Richardson, M.2
  • 11
    • 0027223990 scopus 로고
    • Complete amino acid sequence of puroindoline, a new basic and cysteine-rich protein with a unique tryptophan-rich domain, isolated from wheat endosperm by Triton X-114 phase partitioning
    • Blochet, J. E., Chevalier, C., Forest, E., Pebay-Peyroula, E., Gautier, M. F., Joudrier, P., Pezolet, M., and Marion, D. Complete amino acid sequence of puroindoline, a new basic and cysteine-rich protein with a unique tryptophan-rich domain, isolated from wheat endosperm by Triton X-114 phase partitioning. FEBS (Fed. Eur. Brew. Soc.) Lett. 329:336-340, 1993.
    • (1993) FEBS (Fed. Eur. Brew. Soc.) Lett. , vol.329 , pp. 336-340
    • Blochet, J.E.1    Chevalier, C.2    Forest, E.3    Pebay-Peyroula, E.4    Gautier, M.F.5    Joudrier, P.6    Pezolet, M.7    Marion, D.8
  • 12
    • 0023194814 scopus 로고
    • Isolation and characterisation of cDNAs coding leaf-specific thionins closely related to the endosperm-specific hordothionin in barley (Hordeum vulgare L.)
    • Bohlmann, H., and Apel, K. Isolation and characterisation of cDNAs coding leaf-specific thionins closely related to the endosperm-specific hordothionin in barley (Hordeum vulgare L.) Mol. Gen. Genet. 207:446-454, 1987.
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 446-454
    • Bohlmann, H.1    Apel, K.2
  • 13
    • 0008927955 scopus 로고    scopus 로고
    • Improvement of malt quality and safety by adding starter culture during the malting process
    • Boivin, P., and Malanda, M. Improvement of malt quality and safety by adding starter culture during the malting process. Tech. Q. Master Brew. Assoc. Am. 34:96-101, 1997.
    • (1997) Tech. Q. Master Brew. Assoc. Am. , vol.34 , pp. 96-101
    • Boivin, P.1    Malanda, M.2
  • 15
    • 0000954875 scopus 로고
    • B. Fritig, and M. Legrand, Eds. Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Boller, T. Mechanisms of Plant Defence Responses. B. Fritig, and M. Legrand, Eds. Kluwer Academic Publishers, Dordrecht, the Netherlands. Pp. 391-400, 1993.
    • (1993) Mechanisms of Plant Defence Responses , pp. 391-400
    • Boller, T.1
  • 16
    • 0037024075 scopus 로고    scopus 로고
    • Isolation, identification and changes in the composition of lactic acid bacteria during the malting of two different barley cultivars
    • Booysens, C., Dicks, L. T. M., Meijering, I., and Achermann, A. Isolation, identification and changes in the composition of lactic acid bacteria during the malting of two different barley cultivars. Int. J. Food Microbiol. 76:63-73, 2002.
    • (2002) Int. J. Food Microbiol. , vol.76 , pp. 63-73
    • Booysens, C.1    Dicks, L.T.M.2    Meijering, I.3    Achermann, A.4
  • 18
    • 33646342915 scopus 로고
    • Weeds, pests and diseases in the growing crop
    • Chapman and Hall, London
    • Briggs, D. E. Weeds, pests and diseases in the growing crop. In: Barley. Chapman and Hall, London. Pp. 399-404, 1978.
    • (1978) Barley , pp. 399-404
    • Briggs, D.E.1
  • 21
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defence system
    • Broekaert, W. F., Cammue, B. P. A., and Osborn, R. W. Plant defensins: Novel antimicrobial peptides as components of the host defence system. Plant Physiol. 108, 1353-1358, 1995.
    • (1995) Plant Physiol. , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Cammue, B.P.A.2    Osborn, R.W.3
  • 22
    • 33646339065 scopus 로고    scopus 로고
    • Biocidal chitin binding proteins. International Patent Application WO94/11511, 1994
    • Broekaert, W. F., Cammue, B. P. A., Osborn, R. W., and Rees, S. B. Biocidal chitin binding proteins. International Patent Application WO94/11511, 1994.
    • Broekaert, W.F.1    Cammue, B.P.A.2    Osborn, R.W.3    Rees, S.B.4
  • 24
    • 0027395308 scopus 로고
    • Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: Structural motif common to toxic arthropod proteins
    • Bruix, M., Jimenez, M. A., Santoro, J., Gonzalez, C., Colilla, F. J., Mendez, E., and Rico, M. Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: Structural motif common to toxic arthropod proteins. Biochemistry 19:32, 715-724, 1993.
    • (1993) Biochemistry , vol.19 , pp. 32
    • Bruix, M.1    Jimenez, M.A.2    Santoro, J.3    Gonzalez, C.4    Colilla, F.J.5    Mendez, E.6    Rico, M.7
  • 27
    • 0000662638 scopus 로고
    • The complete amino acid sequence of the bifunctional α-amylase/ trypsin inhibitor from seeds of ragi (Indian finger millet: Eleusine coracana Goertn.)
    • Campas, F. A. P., and Richardson, M. The complete amino acid sequence of the bifunctional α-amylase/trypsin inhibitor from seeds of ragi (Indian finger millet: Eleusine coracana Goertn.) FEBS (Fed. Eur. Brew. Soc.) Lett. 152:300-304, 1984.
    • (1984) FEBS (Fed. Eur. Brew. Soc.) Lett. , vol.152 , pp. 300-304
    • Campas, F.A.P.1    Richardson, M.2
  • 28
    • 0002476117 scopus 로고
    • The pathogenesis-related proteins in plants
    • J. K. Setlow, Ed. Plenum Press, New York
    • Carr, J. P., and Klessig, D, F. The pathogenesis-related proteins in plants. In: Genetic Engineering, Principles and Methods. J. K. Setlow, Ed. Plenum Press, New York. Vol. 11, pp. 65-109, 1989.
    • (1989) Genetic Engineering, Principles and Methods , vol.11 , pp. 65-109
    • Carr, J.P.1    Klessig, D.F.2
  • 29
    • 0001515690 scopus 로고    scopus 로고
    • Primary versus secondary gushing and assay procedures used to assess malt/beer gushing potential
    • Casey, G. Primary versus secondary gushing and assay procedures used to assess malt/beer gushing potential. Tech. Q. Master Brew. Assoc. Am. 33:229-235, 1996.
    • (1996) Tech. Q. Master Brew. Assoc. Am. , vol.33 , pp. 229-235
    • Casey, G.1
  • 30
    • 0026602945 scopus 로고
    • Extreme divergence of a novel wheat thionin generated by a mulational burst specifically affecting the mature protein domain of the precursor
    • Castagnero, A., Marana, C., Carbonero, R, and García-Olmedo, F. Extreme divergence of a novel wheat thionin generated by a mulational burst specifically affecting the mature protein domain of the precursor. J. Mol. Biol. 224:1003-1009, 1992.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1003-1009
    • Castagnero, A.1    Marana, C.2    Carbonero, R.3    García-Olmedo, F.4
  • 31
    • 0028168377 scopus 로고
    • A novel α-amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds
    • Chagolla-Lopez, A., Blanco-Labra, A., Patthy, A., Sanchez, R., and Ponger, S. A novel α-amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds. J. Biol. Chem. 269:23675-23680, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23675-23680
    • Chagolla-Lopez, A.1    Blanco-Labra, A.2    Patthy, A.3    Sanchez, R.4    Ponger, S.5
  • 32
    • 0025080513 scopus 로고
    • γ-Purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm
    • Colilla, F. J., Rocher, A., and Mendez, E. γ-Purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS (Fed. Eur. Brew. Soc.) Lett. 270:191-194, 1990.
    • (1990) FEBS (Fed. Eur. Brew. Soc.) Lett. , vol.270 , pp. 191-194
    • Colilla, F.J.1    Rocher, A.2    Mendez, E.3
  • 34
    • 0042358899 scopus 로고    scopus 로고
    • Effects of pathogen-related proteins from barley grain on brewers yeast
    • Cvetković, A., Blagojević, S., and Hranisavljević, J. Effects of pathogen-related proteins from barley grain on brewers yeast. J. Inst. Brew. 103:183-186, 1997.
    • (1997) J. Inst. Brew. , vol.103 , pp. 183-186
    • Cvetković, A.1    Blagojević, S.2    Hranisavljević, J.3
  • 35
    • 0026772271 scopus 로고
    • Amino acid sequence of a non-specific wheat phospholipid transfer protein and its conformation as revealed by infrared and Raman spectroscopy. Role of disulfide bridges and phospholipids in stabilisation of alpha-helix structure
    • Désormeaux, A., Blochet, J. E., Pézolet, M., and Mario, D. Amino acid sequence of a non-specific wheat phospholipid transfer protein and its conformation as revealed by infrared and Raman spectroscopy. Role of disulfide bridges and phospholipids in stabilisation of alpha-helix structure. Biochim. Biophys. Acta 1121:137-152, 1992.
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 137-152
    • Désormeaux, A.1    Blochet, J.E.2    Pézolet, M.3    Mario, D.4
  • 36
    • 84987378314 scopus 로고
    • A microbiological evaluation of barley mall production
    • Douglas, P. E., and Flannigan, B. A microbiological evaluation of barley mall production. J. Inst. Brew. 94:85-88, 1988.
    • (1988) J. Inst. Brew. , vol.94 , pp. 85-88
    • Douglas, P.E.1    Flannigan, B.2
  • 37
    • 0035078262 scopus 로고    scopus 로고
    • Disulphide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2
    • Douliez, J., Pato, C., Rabesona, H., Mollé, D., and Marion, D. Disulphide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2. Eur. J. Biochem. 268:1400-1403, 2001.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1400-1403
    • Douliez, J.1    Pato, C.2    Rabesona, H.3    Mollé, D.4    Marion, D.5
  • 38
    • 0032534468 scopus 로고    scopus 로고
    • Activation of cysreine proteases in cowpea plants during the hypersensitive response-A form of cell death
    • D'Silva, I., Poirier, G. G., and Heath, M. C. Activation of cysreine proteases in cowpea plants during the hypersensitive response-A form of cell death. Exp. Cell Res. 245:389-399, 1998.
    • (1998) Exp. Cell Res. , vol.245 , pp. 389-399
    • D'Silva, I.1    Poirier, G.G.2    Heath, M.C.3
  • 40
    • 33745903803 scopus 로고    scopus 로고
    • Starter culture during malting: From spore to final beer
    • Dufait, A., and Coppens, T. Starter culture during malting: From spore to final beer. Cerevisia Belg. J. Brew. Biotechnol. 29:34-52, 2004.
    • (2004) Cerevisia Belg. J. Brew. Biotechnol. , vol.29 , pp. 34-52
    • Dufait, A.1    Coppens, T.2
  • 41
    • 0003117134 scopus 로고
    • Microflora of barley and its effects on malt and beer properties: A review
    • Etchevers, G. C., Banasi, O. J., and Watson, C. A. Microflora of barley and its effects on malt and beer properties: A review. Brew. Dig. 52(1):46-50, 1977.
    • (1977) Brew. Dig. , vol.52 , Issue.1 , pp. 46-50
    • Etchevers, G.C.1    Banasi, O.J.2    Watson, C.A.3
  • 42
    • 0006048294 scopus 로고    scopus 로고
    • The influence of malt foam-positive proteins and non-starch polysaccharides on beer foam quality
    • Evans, D. E., Nischwitz, R., Stewart, D. C., Cole, N., and MacLeod, L. C. The influence of malt foam-positive proteins and non-starch polysaccharides on beer foam quality. Monogr. Eur. Brew. Conv. 27:114-128, 1999.
    • (1999) Monogr. Eur. Brew. Conv. , vol.27 , pp. 114-128
    • Evans, D.E.1    Nischwitz, R.2    Stewart, D.C.3    Cole, N.4    MacLeod, L.C.5
  • 43
    • 0006083315 scopus 로고    scopus 로고
    • Variations and genetic control of foam-positive proteins in Australian barley varieties
    • Evans, D. E., Ratcliffe, M., Jones, B. L., and Barr, A. R. Variations and genetic control of foam-positive proteins in Australian barley varieties. Proc. Aust. Barley Technol. Symp, 9:3.6.1-3.6.6, 1999.
    • (1999) Proc. Aust. Barley Technol. Symp , vol.9
    • Evans, D.E.1    Ratcliffe, M.2    Jones, B.L.3    Barr, A.R.4
  • 44
    • 0033450813 scopus 로고    scopus 로고
    • The impact of mall derived proteins on beer foam quality. Part 11. The influence of malt foam-positive proteins and non-starch polysaccharides on beer foam quality
    • Evans, D. E., Sheehan, M. C., and Stewart, D. C. The impact of mall derived proteins on beer foam quality. Part 11. The influence of malt foam-positive proteins and non-starch polysaccharides on beer foam quality. J. Inst. Brew. 105:171-177, 1999.
    • (1999) J. Inst. Brew. , vol.105 , pp. 171-177
    • Evans, D.E.1    Sheehan, M.C.2    Stewart, D.C.3
  • 45
    • 0015627522 scopus 로고
    • Current efforts of the food and drug administration to control mycotoxins in food
    • Fischbach, H., and Rodricks, J. V. Current efforts of the food and drug administration to control mycotoxins in food. J. Assoc. Off. Anal Chem. 56:767-770, 1973.
    • (1973) J. Assoc. Off. Anal Chem. , vol.56 , pp. 767-770
    • Fischbach, H.1    Rodricks, J.V.2
  • 46
    • 0002045320 scopus 로고    scopus 로고
    • The microflora of barley and mall
    • F. G. Priest and I. Campbell, Eds. Chapman and Hall, London. 2nd Ed.
    • Flannigan, B. The microflora of barley and mall. In: Brewing Microbiology F. G. Priest and I. Campbell, Eds. Chapman and Hall, London. 2nd Ed. Pp. 83-125, 1996.
    • (1996) Brewing Microbiology , pp. 83-125
    • Flannigan, B.1
  • 47
    • 0003094103 scopus 로고
    • Fusarium mycotoxins and mailing of barley
    • J. Lacey, Ed. John Wiley and Sons, New York
    • Flannigan, B., Morton, J. G., and Naylot, R. J. Fusarium mycotoxins and mailing of barley. In: Trichothecenes and other mycotoxins. J. Lacey, Ed. John Wiley and Sons, New York. Pp. 171-184, 1985.
    • (1985) Trichothecenes and Other Mycotoxins , pp. 171-184
    • Flannigan, B.1    Morton, J.G.2    Naylot, R.J.3
  • 48
    • 0026949234 scopus 로고
    • Expression pattern of a tobacco lipid transfer protein gene within the shool apex
    • Fleming, A. J., Mandel, T., Hofmann, S., de Vries, S. C., and Kuhlemeier, K. Expression pattern of a tobacco lipid transfer protein gene within the shool apex. Plant J. 2:855-862, 1992.
    • (1992) Plant J. , vol.2 , pp. 855-862
    • Fleming, A.J.1    Mandel, T.2    Hofmann, S.3    De Vries, S.C.4    Kuhlemeier, K.5
  • 49
    • 0028518533 scopus 로고
    • Thionins: Properties, possible biological roles and mechanisms of action
    • Florack, D. E. A., and Stiekema, W. J. Thionins: Properties, possible biological roles and mechanisms of action. Plant. Mol. Biol. 26:25-37, 1994.
    • (1994) Plant. Mol. Biol. , vol.26 , pp. 25-37
    • Florack, D.E.A.1    Stiekema, W.J.2
  • 51
    • 0032006219 scopus 로고    scopus 로고
    • Antimicrobial proteins in induced plant defence
    • Fritig, B., Heitz, T., and Legrand, M. Antimicrobial proteins in induced plant defence. Curr. Opin. Immunol. 10:16-22, 1998.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 16-22
    • Fritig, B.1    Heitz, T.2    Legrand, M.3
  • 52
    • 7244242042 scopus 로고
    • Some substances in material inducing early flocculation of yeast. II. Further investigation on a substance isolated from wort inducing early flocculation
    • Fujii, T., and Horie, Y. Some substances in material inducing early flocculation of yeast. II. Further investigation on a substance isolated from wort inducing early flocculation. Rep. Res. Lab. Kirin Brew. Co. Ltd. 18:75-85, 1975.
    • (1975) Rep. Res. Lab. Kirin Brew. Co. Ltd. , vol.18 , pp. 75-85
    • Fujii, T.1    Horie, Y.2
  • 53
    • 4243070746 scopus 로고
    • Premature flocculaton of yeast induced by some wort components
    • Fujino, S. and Yoshida, T. Premature flocculaton of yeast induced by some wort components. Rep. Res. Kirin Brew. Co. Ltd. 19:45-53, 1976.
    • (1976) Rep. Res. Kirin Brew. Co. Ltd. , vol.19 , pp. 45-53
    • Fujino, S.1    Yoshida, T.2
  • 54
    • 0028833949 scopus 로고
    • The defensive role of nonspecific; lipid-transfer proteins in plants
    • García-Olmedo, P., Molina, A., Segura, A., and Morena, M. The defensive role of nonspecific; lipid-transfer proteins in plants. Trends Microbiol. 3:72-74, 1995.
    • (1995) Trends Microbiol. , vol.3 , pp. 72-74
    • García-Olmedo, P.1    Molina, A.2    Segura, A.3    Morena, M.4
  • 56
    • 84978598014 scopus 로고
    • The mechanism of gushing-A review
    • Gardner, R. J. The mechanism of gushing-A review. J. Inst. Brew. 79:275-283, 1973.
    • (1973) J. Inst. Brew. , vol.79 , pp. 275-283
    • Gardner, R.J.1
  • 57
    • 0007609854 scopus 로고
    • Thionin genes specifically expressed in barley leaves
    • Causing, K. Thionin genes specifically expressed in barley leaves. Planta 171:241-246, 1987.
    • (1987) Planta , vol.171 , pp. 241-246
    • Causing, K.1
  • 58
    • 0028406286 scopus 로고
    • Triticum aestivum puroindolines, two basic cystine-rich seed proteins: CDNA sequence analysis and developmental gene expression
    • Gautier, M. F., Aleman, M. E., Guirao, A., Marion, D., and Joudrier, P. Triticum aestivum puroindolines, two basic cystine-rich seed proteins: cDNA sequence analysis and developmental gene expression. Plant Mol. Biol. 25:43-57, 1994.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 43-57
    • Gautier, M.F.1    Aleman, M.E.2    Guirao, A.3    Marion, D.4    Joudrier, P.5
  • 59
    • 0006438812 scopus 로고
    • Gushing in beer: It's nature, cause and prevention
    • Gjertsen, P. Gushing in beer: It's nature, cause and prevention. Brew. Dig. 42(5):80-84, 1967.
    • (1967) Brew. Dig. , vol.42 , Issue.5 , pp. 80-84
    • Gjertsen, P.1
  • 60
    • 0000432535 scopus 로고
    • Studies on gushing caused by microorganisms, specially Fusarium sp
    • Gjertsen, P., Trolle, B., and Anderson, K. Studies on gushing caused by microorganisms, specially Fusarium sp. Proc. Congr. Eur. Brew. Com. 10:428-438, 1965.
    • (1965) Proc. Congr. Eur. Brew. Com. , vol.10 , pp. 428-438
    • Gjertsen, P.1    Trolle, B.2    Anderson, K.3
  • 63
    • 0027728296 scopus 로고
    • Barley pathogenesis-related proteins with fungal cell wall lytic activity inhibit the growth of yeasts
    • Grenier, J., Potvin, C., and Asselin, A. Barley pathogenesis-related proteins with fungal cell wall lytic activity inhibit the growth of yeasts. Plant Physiol. 103:1277-1283, 1993.
    • (1993) Plant Physiol. , vol.103 , pp. 1277-1283
    • Grenier, J.1    Potvin, C.2    Asselin, A.3
  • 64
    • 0027202188 scopus 로고
    • Phosphate efflux through channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP
    • Guihard, G., Bénédetti, H., Besnard, M., and Letellier, L. Phosphate efflux through channels formed by colicins and phage T5 in Escherichia coli cells is responsible for the fall in cytoplasmic ATP. J. Biol. Chem. 286:17775-17780, 1993.
    • (1993) J. Biol. Chem. , vol.286 , pp. 17775-17780
    • Guihard, G.1    Bénédetti, H.2    Besnard, M.3    Letellier, L.4
  • 67
    • 0000731037 scopus 로고
    • Malt and beer from barley artificially contaminated with Fusarium in the field
    • Haikara, A. Malt and beer from barley artificially contaminated with Fusarium in the field. Proc. Congr. Eur. Brew. Conv 19:401-408, 1983.
    • (1983) Proc. Congr. Eur. Brew. Conv , vol.19 , pp. 401-408
    • Haikara, A.1
  • 68
    • 0002719387 scopus 로고
    • On the microflora of barley after harvesting, during storage and in malting
    • Haikara, A., Makinen, V., and Hakulinen, R. On the microflora of barley after harvesting, during storage and in malting. Proc. Congr. Eur. Brew. Conv. 16:35-46, 1977.
    • (1977) Proc. Congr. Eur. Brew. Conv. , vol.16 , pp. 35-46
    • Haikara, A.1    Makinen, V.2    Hakulinen, R.3
  • 69
    • 0036373247 scopus 로고    scopus 로고
    • Antimicrobial-producing lactic acid bacteria isolated from raw barley and sorghum
    • Hartnett, D. J., Vaughan, A., and van Sinderen, D. Antimicrobial- producing lactic acid bacteria isolated from raw barley and sorghum. J. Inst. Brew. 108:169-177, 2002.
    • (2002) J. Inst. Brew. , vol.108 , pp. 169-177
    • Hartnett, D.J.1    Vaughan, A.2    Van Sinderen, D.3
  • 71
    • 0002580242 scopus 로고
    • Origin of dominant beer protein immunochemical identity with β-amylase-associated protein from barley
    • Hejgaard, J. Origin of dominant beer protein immunochemical identity with β-amylase-associated protein from barley. J. Inst. Brew. 83:94-96, 1977.
    • (1977) J. Inst. Brew. , vol.83 , pp. 94-96
    • Hejgaard, J.1
  • 72
    • 84987319377 scopus 로고
    • Induction of premature yeast flocculation by on polysaccharide fraction isolated from malt husk
    • Herrera, V. E., and Axcell, B. C. Induction of premature yeast flocculation by on polysaccharide fraction isolated from malt husk. J. Inst Brew. 97:359-366, 1991.
    • (1991) J. Inst Brew. , vol.97 , pp. 359-366
    • Herrera, V.E.1    Axcell, B.C.2
  • 73
    • 84987337753 scopus 로고
    • Studies on the binding between yeast and a malt polysaccharide that induces heavy yeast flocculation
    • Herrera, V. E., and Axcell, B. C. Studies on the binding between yeast and a malt polysaccharide that induces heavy yeast flocculation. J. Inst Brew. 97:367-373, 1991.
    • (1991) J. Inst Brew. , vol.97 , pp. 367-373
    • Herrera, V.E.1    Axcell, B.C.2
  • 74
    • 84982354497 scopus 로고
    • The microflora of ripening barley grain and the effects of pre-harvest fungicide application
    • Hill, R. A., and Lacey, J. The microflora of ripening barley grain and the effects of pre-harvest fungicide application. Ann. Appl. Biol. 102:455-465, 1983.
    • (1983) Ann. Appl. Biol. , vol.102 , pp. 455-465
    • Hill, R.A.1    Lacey, J.2
  • 75
    • 0036370568 scopus 로고    scopus 로고
    • Minireview: Are hydrophobins and/or non-specific lipid transfer proteins responsible for gushing of beer? New hypothesis on the chemical nature of gushing inducing factors
    • Hippeli, S., and Elstner, E. F. Minireview: Are hydrophobins and/or non-specific lipid transfer proteins responsible for gushing of beer? New hypothesis on the chemical nature of gushing inducing factors. Z. Naturforsch. 57:1-8, 2002.
    • (2002) Z. Naturforsch. , vol.57 , pp. 1-8
    • Hippeli, S.1    Elstner, E.F.2
  • 76
    • 0002257926 scopus 로고
    • Cellulases of plant and microbial origin n germinating barley
    • Hoy, J. L., McCauley, B. J., and Fincher, B. Cellulases of plant and microbial origin n germinating barley. J. Inst. Brew. 87:77-80, 1981.
    • (1981) J. Inst. Brew. , vol.87 , pp. 77-80
    • Hoy, J.L.1    McCauley, B.J.2    Fincher, B.3
  • 77
    • 0030879874 scopus 로고    scopus 로고
    • Polysaccharide hydrolases in germinated barley and their role in the depolymerisation of plant and fungal cell walls
    • Hrmova, M., Banik, M., Harvey, A. J., Garrett, T. P. J., Varghese, J. N., Hoj, P. B., and Fincher, G. B. Polysaccharide hydrolases in germinated barley and their role in the depolymerisation of plant and fungal cell walls. Int. J. Biol Macromol. 21:67-72, 1997.
    • (1997) Int. J. Biol Macromol. , vol.21 , pp. 67-72
    • Hrmova, M.1    Banik, M.2    Harvey, A.J.3    Garrett, T.P.J.4    Varghese, J.N.5    Hoj, P.B.6    Fincher, G.B.7
  • 78
    • 33646357687 scopus 로고
    • Determination of fermentation behaviour-malt evaluation based on the original small scale fermentation test
    • Fachverlag Hans Carl, Nürnberg, Germany
    • Inagaki, H., Yamazumi, K., Uehara, H., and Mochzuki, K. Determination of fermentation behaviour-malt evaluation based on the original small scale fermentation test. In: Symposium on Malting Technology. Monogr. XXIII Eur. Brew. Conv. Symp. Fachverlag Hans Carl, Nürnberg, Germany. Pp. 110-136, 1994.
    • (1994) Symposium on Malting Technology. Monogr. XXIII Eur. Brew. Conv. Symp. , pp. 110-136
    • Inagaki, H.1    Yamazumi, K.2    Uehara, H.3    Mochzuki, K.4
  • 79
    • 0034773958 scopus 로고    scopus 로고
    • Evidence of the glycation and denaturation of LTP1 during the malting and brewing process
    • Jegou, S., Douliez, J.-P., Molle, D., Boivin, P., and Marion, D. Evidence of the glycation and denaturation of LTP1 during the malting and brewing process. J. Agric. Food Chem. 49:4942-4949, 2001.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4942-4949
    • Jegou, S.1    Douliez, J.-P.2    Molle, D.3    Boivin, P.4    Marion, D.5
  • 80
    • 0033782344 scopus 로고    scopus 로고
    • Purification and characterisation of LTP polypeptide from beer
    • Jegou, S. D., Molle, D., Boivin, P., and Marion, D. Purification and characterisation of LTP polypeptide from beer. J. Agric. Food Chem, 48:5023-5029, 2000.
    • (2000) J. Agric. Food Chem , vol.48 , pp. 5023-5029
    • Jegou, S.D.1    Molle, D.2    Boivin, P.3    Marion, D.4
  • 82
    • 0031081348 scopus 로고    scopus 로고
    • Lipid-transfer proteins: A puzzling family of plant proteins
    • Kader, J. C. Lipid-transfer proteins: A puzzling family of plant proteins. Trends Plant Sci. 2:66-70, 1997.
    • (1997) Trends Plant Sci. , vol.2 , pp. 66-70
    • Kader, J.C.1
  • 83
    • 0021402150 scopus 로고
    • Purification and characterisation of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts
    • Kader, J. C., Julienne, M., and Vergnolle, C. Purification and characterisation of a spinach-leaf protein capable of transferring phospholipids from liposomes to mitochondria or chloroplasts. Eur. J. Biochem. 139:411-416, 1984.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 411-416
    • Kader, J.C.1    Julienne, M.2    Vergnolle, C.3
  • 84
    • 0035111310 scopus 로고    scopus 로고
    • Growth of Trichoderma viride on crude cell wall preparations from barley
    • Kanauchi, M., and Bamforth, C. W. Growth of Trichoderma viride on crude cell wall preparations from barley. J. Agric. Food. Chem. 49:883-887, 2002.
    • (2002) J. Agric. Food. Chem. , vol.49 , pp. 883-887
    • Kanauchi, M.1    Bamforth, C.W.2
  • 85
    • 0031711659 scopus 로고    scopus 로고
    • Hydrophobins and repellents: Proteins with fundamental roles in fungal morphogenesis
    • Kershaw, M. J., and Talbot, N. J. Hydrophobins and repellents: Proteins with fundamental roles in fungal morphogenesis. Fungal Genet. Biol. 23:18-33, 1998.
    • (1998) Fungal Genet. Biol. , vol.23 , pp. 18-33
    • Kershaw, M.J.1    Talbot, N.J.2
  • 86
    • 0006480625 scopus 로고
    • A wort component responsible for gushing in beer
    • Kitabatake, K. A wort component responsible for gushing in beer. Bull. Brew. Sci. (Tokyo) 24:21-32, 1978.
    • (1978) Bull. Brew. Sci. (Tokyo) , vol.24 , pp. 21-32
    • Kitabatake, K.1
  • 87
    • 0006482166 scopus 로고
    • Production of gushing factor by Nigrospora sp. in liquid culture media
    • Kitabatake, K., and Amaha, M. Production of gushing factor by Nigrospora sp. in liquid culture media. Bull. Brew. Sci. 20:1-8, 1974.
    • (1974) Bull. Brew. Sci. , vol.20 , pp. 1-8
    • Kitabatake, K.1    Amaha, M.2
  • 88
    • 0017370172 scopus 로고
    • Effects of chemical modifications on the gushing inducing activity of a hydrophobic protein produced by Nigrospora sp
    • Kitabatake, K., and Amaha, M. Effects of chemical modifications on the gushing inducing activity of a hydrophobic protein produced by Nigrospora sp. Agric. Biol. Chem. 41:1011-1019, 1977.
    • (1977) Agric. Biol. Chem. , vol.41 , pp. 1011-1019
    • Kitabatake, K.1    Amaha, M.2
  • 91
    • 0036378177 scopus 로고    scopus 로고
    • Antifungal activities of two Lactobacillus plantarum strains against Fusarium moulds in vitro and in malting of barley
    • Laitila, A., Alakomi, H. L., Raaska, L., Mattila-Sandholm, T., and Haikara, A. Antifungal activities of two Lactobacillus plantarum strains against Fusarium moulds in vitro and in malting of barley. J. Appl. Microbiol. 93:566-576, 2002.
    • (2002) J. Appl. Microbiol. , vol.93 , pp. 566-576
    • Laitila, A.1    Alakomi, H.L.2    Raaska, L.3    Mattila-Sandholm, T.4    Haikara, A.5
  • 93
    • 0026063521 scopus 로고
    • Biochemical and molecular characterisation of three barley seed proteins with antifungal properties
    • Leah, R., Tommerup, H., Svendsen, I., and Mundy, J. Biochemical and molecular characterisation of three barley seed proteins with antifungal properties. J. Biol. Chem. 266:1564-1573, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1564-1573
    • Leah, R.1    Tommerup, H.2    Svendsen, I.3    Mundy, J.4
  • 94
    • 0025006196 scopus 로고
    • Molecular recognition between serine proteases and new bioactive micro-proteins with knotted structure
    • Le-Nguyen, D. L., Heitz, A., Chiche, L., Castro, B., Baigegrain, R., Favel, A., and Coletti-Previero, M. Molecular recognition between serine proteases and new bioactive micro-proteins with knotted structure. Biochimie 72:431-435, 1990.
    • (1990) Biochimie , vol.72 , pp. 431-435
    • Le-Nguyen, D.L.1    Heitz, A.2    Chiche, L.3    Castro, B.4    Baigegrain, R.5    Favel, A.6    Coletti-Previero, M.7
  • 95
    • 0035823634 scopus 로고    scopus 로고
    • Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification
    • Lindorff-Larsen, K., Lerche, M. H., Poulsen, F. M., Roepstroff, P., and Winther, J. R. Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification. J. Biol. Chem. 276:33547-33553, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33547-33553
    • Lindorff-Larsen, K.1    Lerche, M.H.2    Poulsen, F.M.3    Roepstroff, P.4    Winther, J.R.5
  • 96
    • 0029347025 scopus 로고
    • The Pto bacterial resistance gene and the Fen insecticide sensitivity gene encode functional protein kinases with serine/threonine specificity
    • Loh, Y.-T., and Martin, G. B. The Pto bacterial resistance gene and the Fen insecticide sensitivity gene encode functional protein kinases with serine/threonine specificity. Plant Physiol. 108:1735-1739, 1995.
    • (1995) Plant Physiol. , vol.108 , pp. 1735-1739
    • Loh, Y.-T.1    Martin, G.B.2
  • 97
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm
    • Mendez, E., Moreno, A., Colilla, F., Limas, G. G., Mendez, R., Soriano, F., Saunas, M., and De Haro, C. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm. Eur. J. Biochem. 194:533-539, 1990.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.3    Limas, G.G.4    Mendez, R.5    Soriano, F.6    Saunas, M.7    De Haro, C.8
  • 98
    • 0027722868 scopus 로고
    • Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins
    • Molina, A. and García-Olmedo, F. Developmental and pathogen-induced expression of three barley genes encoding lipid transfer proteins. Plant J. 4:983-991, 1993.
    • (1993) Plant J. , vol.4 , pp. 983-991
    • Molina, A.1    García-Olmedo, F.2
  • 99
    • 0027130971 scopus 로고
    • Inhibition of bacterial and fungal plant pathogens by thionins of types I and II
    • Molina, A., Goy, P. A., Fraile, A., Sanchez-Monge, R., and Garcia-Olmedo, F. Inhibition of bacterial and fungal plant pathogens by thionins of types I and II. Plant Sci. 92:169-177, 1993.
    • (1993) Plant Sci. , vol.92 , pp. 169-177
    • Molina, A.1    Goy, P.A.2    Fraile, A.3    Sanchez-Monge, R.4    Garcia-Olmedo, F.5
  • 100
    • 0027507001 scopus 로고
    • Lipid transfer proteins (ns-LTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens
    • Molina, A., Segura, A., and García-Olmedo, F. Lipid transfer proteins (ns-LTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS (Fed. Eur. Brew. Soc.) Lett. 316:119-122, 1993.
    • (1993) FEBS (Fed. Eur. Brew. Soc.) Lett. , vol.316 , pp. 119-122
    • Molina, A.1    Segura, A.2    García-Olmedo, F.3
  • 101
    • 4243128146 scopus 로고
    • Some substances in malt inducing early flocculation of yeast. I. Preliminary investigation on high molecular weight substances in malt and wort
    • Morimoto, K., Shimazu, T., Fujii, T., and Horie, Y. Some substances in malt inducing early flocculation of yeast. I. Preliminary investigation on high molecular weight substances in malt and wort. Rep. Res. Lab. Kirin Brew. Co. Ltd. 18:63-74, 1975.
    • (1975) Rep. Res. Lab. Kirin Brew. Co. Ltd. , vol.18 , pp. 63-74
    • Morimoto, K.1    Shimazu, T.2    Fujii, T.3    Horie, Y.4
  • 102
    • 0032883207 scopus 로고    scopus 로고
    • Fungal resistance to plant antibiotics as a mechanism of pathogenesis
    • Morrissey, J. P., and Osbourn, A. E. Fungal resistance to plant antibiotics as a mechanism of pathogenesis. Microbiol. Mol. Biol. Rev. 63:708-724, 1999.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 708-724
    • Morrissey, J.P.1    Osbourn, A.E.2
  • 103
    • 0002468465 scopus 로고
    • Selective expression of a probable amylase/protease inhibitor in barley aleurone cells: Comparison to the barley amylase/subtilisin inhibitor
    • Mundy, J., and Rogers, J. C. Selective expression of a probable amylase/protease inhibitor in barley aleurone cells: Comparison to the barley amylase/subtilisin inhibitor. Planta 169:51-63, 1986.
    • (1986) Planta , vol.169 , pp. 51-63
    • Mundy, J.1    Rogers, J.C.2
  • 105
    • 0032763883 scopus 로고    scopus 로고
    • From field barley to malt: Detection and specification of microbial activity for quality aspects
    • Noots, I., Delcour, J. A., and Michiels, C. W. From field barley to malt: Detection and specification of microbial activity for quality aspects. Crit. Rev. Microbiol. 25:121-125, 1998.
    • (1998) Crit. Rev. Microbiol. , vol.25 , pp. 121-125
    • Noots, I.1    Delcour, J.A.2    Michiels, C.W.3
  • 106
    • 0037215840 scopus 로고    scopus 로고
    • Studies on barley starchy endosperm cell wall degradation by Rhizopus VII
    • Noots, I., Derycke, V., Jensen, H. E., Decour, J. A., and Coppens, T. Studies on barley starchy endosperm cell wall degradation by Rhizopus VII. J. Cereal Sci. 37:81-90, 2003.
    • (2003) J. Cereal Sci. , vol.37 , pp. 81-90
    • Noots, I.1    Derycke, V.2    Jensen, H.E.3    Decour, J.A.4    Coppens, T.5
  • 108
    • 0345620458 scopus 로고
    • A lethal toxic substance for brewery yeast in wheat and barley. Part II. Isolation and some properties of toxic principle
    • Okada, T., and Yoshizumi, H. A lethal toxic substance for brewery yeast in wheat and barley. Part II. Isolation and some properties of toxic principle. Agric. Biol Chem. 34:1089-1094, 1970.
    • (1970) Agric. Biol Chem. , vol.34 , pp. 1089-1094
    • Okada, T.1    Yoshizumi, H.2
  • 109
    • 0015910349 scopus 로고
    • The mode of action of toxic protein in wheat barley on brewery yeast
    • Okada, T. and Yoshizumi, H. The mode of action of toxic protein in wheat barley on brewery yeast Agric. Biol. Chem. 37:2289-2294, 1973.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 2289-2294
    • Okada, T.1    Yoshizumi, H.2
  • 110
    • 84954938477 scopus 로고
    • A lethal toxic substance for brewery yeast in wheat and barley. Part I. Assay of toxicity on various yeast strains
    • Okada, T., Yoshizumi, H., and Terashima, Y. A lethal toxic substance for brewery yeast in wheat and barley. Part I. Assay of toxicity on various yeast strains. Agric. Biol. Chem. 34:1084-1088, 1970.
    • (1970) Agric. Biol. Chem. , vol.34 , pp. 1084-1088
    • Okada, T.1    Yoshizumi, H.2    Terashima, Y.3
  • 114
    • 49149140830 scopus 로고
    • Specificity of induction of the lignification response in wounded wheat leaves
    • Pearce, R. B., and Ride, J. P. Specificity of induction of the lignification response in wounded wheat leaves. Physiol. Plant Pathol. 16:197-204, 1980.
    • (1980) Physiol. Plant Pathol. , vol.16 , pp. 197-204
    • Pearce, R.B.1    Ride, J.P.2
  • 115
    • 0037288372 scopus 로고    scopus 로고
    • The serine proteinases of Fusarium grown on cereal proteins and in barley grain and their inhibition by barley proteins
    • Pekkarinen, A. The serine proteinases of Fusarium grown on cereal proteins and in barley grain and their inhibition by barley proteins. VVT Publ. 487:74, 90, 2003.
    • (2003) VVT Publ. , vol.487 , pp. 74
    • Pekkarinen, A.1
  • 116
    • 84985091512 scopus 로고
    • Quantitative and qualitative studies of the microflora of barley malt production
    • Petters, H. I., Flannigan, B., and Austin, B. Quantitative and qualitative studies of the microflora of barley malt production. J. Appl. Bacteriol. 65:279-297, 1988.
    • (1988) J. Appl. Bacteriol. , vol.65 , pp. 279-297
    • Petters, H.I.1    Flannigan, B.2    Austin, B.3
  • 117
    • 0012834181 scopus 로고
    • Synthesis and processing of thionin precursors in developing endosperm of barley (Hordeum vulgare L.)
    • Ponz, F., Hernandez-Lucas, C., Carbonero, P., and García-Olmedo, F. Synthesis and processing of thionin precursors in developing endosperm of barley (Hordeum vulgare L.) EMBO (Eur. Mol. Biol. Organ.) J. 2:1035-1040, 1983.
    • (1983) EMBO (Eur. Mol. Biol. Organ.) J. , vol.2 , pp. 1035-1040
    • Ponz, F.1    Hernandez-Lucas, C.2    Carbonero, P.3    García-Olmedo, F.4
  • 118
    • 0022701826 scopus 로고
    • Cloning nucleotide sequence of a cDNA encoding the precursor of the barley toxin α hordothionin
    • Ponz, F., Paz-Ares, J., Hernandez-Lucas, C., García-Olmedo, F., and Carbonero, P. Cloning nucleotide sequence of a cDNA encoding the precursor of the barley toxin α hordothionin. Eur. J. Biochem. 156:131-135, 1986.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 131-135
    • Ponz, F.1    Paz-Ares, J.2    Hernandez-Lucas, C.3    García-Olmedo, F.4    Carbonero, P.5
  • 119
    • 0002485830 scopus 로고
    • Studies on barley microflora of possible importance to malting and brewing quality. 1. The treatment of barley during malting with selected microorganism
    • Prentice, N., and Sloey, W. Studies on barley microflora of possible importance to malting and brewing quality. 1. The treatment of barley during malting with selected microorganism. Proc. Am. Soc. Brew. Chem. 1960, pp. 28-34.
    • (1960) Proc. Am. Soc. Brew. Chem. , pp. 28-34
    • Prentice, N.1    Sloey, W.2
  • 120
    • 0002045320 scopus 로고    scopus 로고
    • The microflora of barley and malt
    • Elsevier Applied Science, London
    • Priest, F. G., and Campell, I. The microflora of barley and malt. In: Brewing Microbiology. Elsevier Applied Science, London. Pp. 83-90, 1987.
    • (1987) Brewing Microbiology , pp. 83-90
    • Priest, F.G.1    Campell, I.2
  • 121
    • 0028363877 scopus 로고
    • Identification of a lipid transfer protein as the major protein in the surface wax of broccoli (Brassica oleracea) leaves
    • Pyee, J., Yu, H., and Kolattukudy, P. E. Identification of a lipid transfer protein as the major protein in the surface wax of broccoli (Brassica oleracea) leaves. Arch. Biochem. Biophys. 311:460-468, 1994.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 460-468
    • Pyee, J.1    Yu, H.2    Kolattukudy, P.E.3
  • 123
    • 0029199405 scopus 로고
    • Refinement of purothionins reveals solute particles important for lattice formation and toxicity. I. α-purothionin revisited
    • Rao, U., Stec, B., and Teeter, M. M. Refinement of purothionins reveals solute particles important for lattice formation and toxicity. I. α-purothionin revisited. Acta Crystallogr. Sect. D. Biol. Crystallogr. 51:904-913, 1995.
    • (1995) Acta Crystallogr. Sect. D. Biol. Crystallogr. , vol.51 , pp. 904-913
    • Rao, U.1    Stec, B.2    Teeter, M.M.3
  • 124
    • 5144225907 scopus 로고    scopus 로고
    • Improving the quality of malting barley by employing microbial starter cultures in the field
    • Reinikainen, P., Peltola, P., Lampinen, R., Haikara, A., and Olkku, J. Improving the quality of malting barley by employing microbial starter cultures in the field. Proc. Congr. Eur. Brew. Conv. 27:551-558, 1999.
    • (1999) Proc. Congr. Eur. Brew. Conv. , vol.27 , pp. 551-558
    • Reinikainen, P.1    Peltola, P.2    Lampinen, R.3    Haikara, A.4    Olkku, J.5
  • 125
    • 0031782954 scopus 로고    scopus 로고
    • Lanthibiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria
    • Sahl, H., and Bierbaum, G. Lanthibiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria. Annu. Rev. Microbiol. 52:41-79, 1998.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 41-79
    • Sahl, H.1    Bierbaum, G.2
  • 127
    • 0030703692 scopus 로고    scopus 로고
    • Impact of Fusarium head blight on the mailing and brewing quality of barley
    • Schwarz, P. B., Casper, H. H., Barr, J., and Musial, M. Impact of Fusarium head blight on the mailing and brewing quality of barley. Cereal Res. Commun. 25:813-814, 1997.
    • (1997) Cereal Res. Commun. , vol.25 , pp. 813-814
    • Schwarz, P.B.1    Casper, H.H.2    Barr, J.3    Musial, M.4
  • 128
  • 130
    • 0001408502 scopus 로고
    • Effects of food processing on mycotoxins
    • Scott, P. M. Effects of food processing on mycotoxins. J. Food Pront. 47:489-499, 1984.
    • (1984) J. Food Pront. , vol.47 , pp. 489-499
    • Scott, P.M.1
  • 131
    • 0027358813 scopus 로고
    • Purification and antipathogenic activity of lipid transfer proteins (LTPs) from leafs of Arabidopsis and spinach
    • Segura, A., Moreno, M., and García-Olmedo, F. Purification and antipathogenic activity of lipid transfer proteins (LTPs) from leafs of Arabidopsis and spinach. FEBS (Fed Eur. Brew. Soc.) Lett. 332:243-246, 1993.
    • (1993) FEBS (Fed Eur. Brew. Soc.) Lett. , vol.332 , pp. 243-246
    • Segura, A.1    Moreno, M.2    García-Olmedo, F.3
  • 132
    • 0015337334 scopus 로고
    • Incidence of antibacterial compounds in fungi
    • Singh, B., Gupta, K. G., and Gupta, G. S. Incidence of antibacterial compounds in fungi. Indian J. Exp. Biol. 10:228-231, 1971.
    • (1971) Indian J. Exp. Biol. , vol.10 , pp. 228-231
    • Singh, B.1    Gupta, K.G.2    Gupta, G.S.3
  • 133
    • 0026815874 scopus 로고
    • Structure and expression of barley lipid transfer protein gene LTP1
    • Skiver, K., Leah, R., Müller-Uri, F., Olsen, F. L., and Mundy, J. Structure and expression of barley lipid transfer protein gene LTP1. Plant Mol. Biol. 18:585-589, 1992.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 585-589
    • Skiver, K.1    Leah, R.2    Müller-Uri, F.3    Olsen, F.L.4    Mundy, J.5
  • 134
    • 0026448263 scopus 로고
    • Flocculence of Saccharomyces cerevisiae cells is induced by nutrient limitation, with cell surface hydrophobicity as a major determinant
    • Smit, G., Straver, M. H., Lugtenberg, J. J., and Kijne, J. W. Flocculence of Saccharomyces cerevisiae cells is induced by nutrient limitation, with cell surface hydrophobicity as a major determinant. April. Environ. Microbiol. 5:3709-3714, 1992.
    • (1992) April. Environ. Microbiol. , vol.5 , pp. 3709-3714
    • Smit, G.1    Straver, M.H.2    Lugtenberg, J.J.3    Kijne, J.W.4
  • 136
    • 33646339332 scopus 로고
    • Fungi on cereals and their effect on quality with special consideration of malting barley
    • Spicher, G. Fungi on cereals and their effect on quality with special consideration of malting barley. Monatsschr. Brauwiss. 42:68-77, 1989.
    • (1989) Monatsschr. Brauwiss. , vol.42 , pp. 68-77
    • Spicher, G.1
  • 138
    • 0029199404 scopus 로고
    • Refinement of purothionin reveals solute particles important for lattice formation toxicity of β-purothionin at 1.7A resolution
    • Stec, B., Rao, U., and Teeter, M. M. Refinement of purothionin reveals solute particles important for lattice formation toxicity of β-purothionin at 1.7A resolution. Acta Crystallogr. Sect. D. Biol. Crystallogr. 51:914-924, 1995.
    • (1995) Acta Crystallogr. Sect. D. Biol. Crystallogr. , vol.51 , pp. 914-924
    • Stec, B.1    Rao, U.2    Teeter, M.M.3
  • 139
    • 0022761205 scopus 로고
    • Tissue-specific and light-dependent changes of chromatin organisation in barley (Hordeum vulgare)
    • Steinmüller, K., Batschauer, A., and Apel, K. Tissue-specific and light-dependent changes of chromatin organisation in barley (Hordeum vulgare). Eur. J. Biochem. 158:519-525, 1986.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 519-525
    • Steinmüller, K.1    Batschauer, A.2    Apel, K.3
  • 140
  • 141
    • 0002573616 scopus 로고
    • Yeast flocculation: Restructuring the theories in line with research
    • Stratford, M. Yeast flocculation: Restructuring the theories in line with research. Cerevisiea. 21:38-45, 1992.
    • (1992) Cerevisiea , vol.21 , pp. 38-45
    • Stratford, M.1
  • 142
    • 0027158901 scopus 로고
    • Yeast flocculation: Lectin synthesis and activation
    • Stratford, M., and Carter, A. T. Yeast flocculation: Lectin synthesis and activation. Yeast 9:371-378, 1993.
    • (1993) Yeast , vol.9 , pp. 371-378
    • Stratford, M.1    Carter, A.T.2
  • 143
    • 0030808656 scopus 로고    scopus 로고
    • A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein
    • Tailor, R., Acland, D. P., Attenborough, S., Cammue, B. P. A., Evans, I. J., Osborn, R. W., Ray, J., Rees, S. B., and Broekaert, W. F. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein. J. Biol. Chem. 272:24480-24487, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24480-24487
    • Tailor, R.1    Acland, D.P.2    Attenborough, S.3    Cammue, B.P.A.4    Evans, I.J.5    Osborn, R.W.6    Ray, J.7    Rees, S.B.8    Broekaert, W.F.9
  • 144
    • 0000690996 scopus 로고
    • The amino-acid sequence of the nonspecific lipid transfer protein from germinated caster bean endosperm
    • Takishima, K., Watanabe, S, Ymamda, M., and Maniya, G. The amino-acid sequence of the nonspecific lipid transfer protein from germinated caster bean endosperm. Biochim. Biophys. Acta 870:248-255, 1986.
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 248-255
    • Takishima, K.1    Watanabe, S.2    Ymamda, M.3    Maniya, G.4
  • 145
    • 0030448263 scopus 로고    scopus 로고
    • Initiation of plant disease resistance by physical interaction of AvrPto and Pto kinase
    • Tang, X., Frederick, R. D., Zhou, J., Halterman, D. A., Jia, Y., and Martin, G. B. Initiation of plant disease resistance by physical interaction of AvrPto and Pto kinase. Science 274:2063-2065, 1996.
    • (1996) Science , vol.274 , pp. 2063-2065
    • Tang, X.1    Frederick, R.D.2    Zhou, J.3    Halterman, D.A.4    Jia, Y.5    Martin, G.B.6
  • 148
    • 0027132885 scopus 로고
    • Synergistic enhancement of antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors
    • Terras, F. R. G., Schoofs, H. M. E., Thevissen, K., Osborn, R. W., Vanderleyden, J., Cammue, B. P. A., and Broekaert, W. F. Synergistic enhancement of antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors. Plant Physiol. 103:1311-1319, 1993.
    • (1993) Plant Physiol. , vol.103 , pp. 1311-1319
    • Terras, F.R.G.1    Schoofs, H.M.E.2    Thevissen, K.3    Osborn, R.W.4    Vanderleyden, J.5    Cammue, B.P.A.6    Broekaert, W.F.7
  • 150
    • 0001469527 scopus 로고
    • In vitro anti-fungal activity of a radish (Raphanus sativus L.) seed protein homologous to lipid transfer proteins
    • Terras, F. R. G., Van Leuven, F., Vanderleyden, J., Cammue, B. P. A., and Broekaert, W. F. In vitro anti-fungal activity of a radish (Raphanus sativus L.) seed protein homologous to lipid transfer proteins. Plant Physiol. 100:1055-1058, 1992.
    • (1992) Plant Physiol. , vol.100 , pp. 1055-1058
    • Terras, F.R.G.1    Van Leuven, F.2    Vanderleyden, J.3    Cammue, B.P.A.4    Broekaert, W.F.5
  • 152
    • 0026810840 scopus 로고
    • A probable lipid transfer protein gene is induced by NaCl in stems of tomatoe plants
    • Torres-Schumann, S., Godoy, J. A., and Pintor-Toro, J. A. A probable lipid transfer protein gene is induced by NaCl in stems of tomatoe plants. Plant Mol. Biol. 18:749-757, 1992.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 749-757
    • Torres-Schumann, S.1    Godoy, J.A.2    Pintor-Toro, J.A.3
  • 153
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins
    • Van Loon, L. C., and Van Strien, E. A. The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol. 55:85-97, 1999.
    • (1999) Physiol. Mol. Plant Pathol. , vol.55 , pp. 85-97
    • Van Loon, L.C.1    Van Strien, E.A.2
  • 154
    • 33646344647 scopus 로고    scopus 로고
    • Screening of barley, malt and wort extracts for antiyeast activity
    • Chapter 7. Ph.D. thesis. Stellenbosch University, South Africa
    • Van Nierop, S. N. E. Screening of barley, malt and wort extracts for antiyeast activity. Chapter 7. In: Investigation of Malt Factors that Influence Beer Production and Quality. Ph.D. thesis. Stellenbosch University, South Africa, 2005.
    • (2005) Investigation of Malt Factors That Influence Beer Production and Quality
    • Van Nierop, S.N.E.1
  • 155
    • 33646371647 scopus 로고    scopus 로고
    • Partial characterisation of antimicrobial factors in barley malt
    • Chapter 9 Ph.D. thesis. Stellenbosch University, South Africa
    • Van Nierop, S.N.E. Partial characterisation of antimicrobial factors in barley malt. Chapter 9. In: Investigation of Malt Factors that Influence Beer Production and Quality. Ph.D. thesis. Stellenbosch University, South Africa, 2005.
    • (2005) Investigation of Malt Factors That Influence Beer Production and Quality
    • Van Nierop, S.N.E.1
  • 156
    • 7244229911 scopus 로고    scopus 로고
    • Enzymatic generation of factors from malt responsible for premature yeast flocculation
    • Van Nierop, S. N. E., Cameron-Clarke, A., and Axcell, B. C. Enzymatic generation of factors from malt responsible for premature yeast flocculation. J. Am. Soc. Brew. Chem. 62:108-116, 2004.
    • (2004) J. Am. Soc. Brew. Chem. , vol.62 , pp. 108-116
    • Van Nierop, S.N.E.1    Cameron-Clarke, A.2    Axcell, B.C.3
  • 157
    • 0034929958 scopus 로고    scopus 로고
    • An analysis of bacteriocins produced by lactic acid bacteria isolated from malted barley
    • Vaughan, A., Eijsink, V. G. H., O'Sullivan, T. F., O'Hanlon, K., and Sinderen, D. An analysis of bacteriocins produced by lactic acid bacteria isolated from malted barley. J Appl. Microbiol. 91:131-138, 2001.
    • (2001) J Appl. Microbiol. , vol.91 , pp. 131-138
    • Vaughan, A.1    Eijsink, V.G.H.2    O'Sullivan, T.F.3    O'Hanlon, K.4    Sinderen, D.5
  • 161
    • 0031060711 scopus 로고    scopus 로고
    • Hydrophobins: Proteins that change the nature of the fungal surface
    • Wessels, J. G. H. Hydrophobins: Proteins that change the nature of the fungal surface. Adv. Microb. Physiol. 38:1-45, 1997.
    • (1997) Adv. Microb. Physiol. , vol.38 , pp. 1-45
    • Wessels, J.G.H.1
  • 162
    • 0001574888 scopus 로고
    • Hydrophobin genes involved in formation of aerial hyphae and fruit bodies in Schizophyllum
    • Wessels, J. G. H., de Vries, O. M. H., Asgeisdottir, S. A., and Schuren, F. H. I. Hydrophobin genes involved in formation of aerial hyphae and fruit bodies in Schizophyllum. Plant Cell 3:793-799, 1991.
    • (1991) Plant Cell , vol.3 , pp. 793-799
    • Wessels, J.G.H.1    De Vries, O.M.H.2    Asgeisdottir, S.A.3    Schuren, F.H.I.4
  • 163
    • 0036234128 scopus 로고    scopus 로고
    • Mycotoxins and fermentation-beer production
    • Wolf-Hall, C. E., and Schwarz, P. B. Mycotoxins and fermentation-beer production. Adv. Exp. Med. Biol. 504, 217-226, 2002.
    • (2002) Adv. Exp. Med. Biol. , vol.504 , pp. 217-226
    • Wolf-Hall, C.E.1    Schwarz, P.B.2
  • 165
    • 33847487608 scopus 로고
    • Lipid transfer proteins in plants and microorganisms
    • Yamada, M. Lipid transfer proteins in plants and microorganisms. Plant Cell Physiol. 33:1-6, 1992.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 1-6
    • Yamada, M.1
  • 166
    • 0024075865 scopus 로고
    • Amino acid sequence of a probable amylase/protease inhibitor from rice seeds
    • Yu, Y. G., Chung, C. H., Fowler, A., and Suh, S. W. Amino acid sequence of a probable amylase/protease inhibitor from rice seeds. Arch. Biochem. Biophys. 265:465-475, 1988.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 465-475
    • Yu, Y.G.1    Chung, C.H.2    Fowler, A.3    Suh, S.W.4
  • 167
    • 0029560869 scopus 로고
    • The tomatoe gene Pti I encodes a serine/thrionine kinase that is phosphorylation by Pto and is involved in the plant hypersensitivity response
    • Zhou, J., Loh, Y.-T., Bressan, R. A., and Martin, G. B. The tomatoe gene Pti I encodes a serine/thrionine kinase that is phosphorylation by Pto and is involved in the plant hypersensitivity response. Cell 83:925-935, 1995.
    • (1995) Cell , vol.83 , pp. 925-935
    • Zhou, J.1    Loh, Y.-T.2    Bressan, R.A.3    Martin, G.B.4


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