메뉴 건너뛰기




Volumn 132, Issue 2, 2000, Pages 111-118

Thermostabilities of grain β-amylase and β-glucanase in Finnish landrace barleys and their putative past adaptedness

Author keywords

[No Author keywords available]

Indexed keywords

BETA AMYLASE; BETA GLUCAN HYDROLASE;

EID: 0033920434     PISSN: 00180661     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1601-5223.2000.00111.x     Document Type: Article
Times cited : (6)

References (47)
  • 1
    • 0343174753 scopus 로고    scopus 로고
    • Megareduction of genetic variation in Finnish cereals by breeding in response to demands of technology and modernization ideology, 1905-1955
    • (ed A-M Niskanen). Dept. Plant Biol., Fac. Agric. Forest., Univ. of Helsinki
    • Ahokas H, (1998). Megareduction of genetic variation in Finnish cereals by breeding in response to demands of technology and modernization ideology, 1905-1955. In: Plant breeding and forest tree breeding today (ed A-M Niskanen). Dept. Plant Biol., Fac. Agric. Forest., Univ. of Helsinki, p. 6-7.
    • (1998) Plant Breeding and Forest Tree Breeding Today , pp. 6-7
    • Ahokas, H.1
  • 2
    • 0003999581 scopus 로고    scopus 로고
    • Impacts on agricultural development by Constantin Boije, a missionary and the first plant breeder in Finland
    • Helsinki
    • Ahokas H, (2000). Impacts on agricultural development by Constantin Boije, a missionary and the first plant breeder in Finland. Yliopistopaino, Helsinki.
    • (2000) Yliopistopaino
    • Ahokas, H.1
  • 3
    • 0033922813 scopus 로고    scopus 로고
    • Retrospecting genetic variation of Finnish oat (Avena sativa) landraces and observations on revived lines grown prior to 1957
    • In press
    • Ahokas H and Manninen M-L, (2000). Retrospecting genetic variation of Finnish oat (Avena sativa) landraces and observations on revived lines grown prior to 1957. Genet. Resour. Crop Evol. (In press)
    • (2000) Genet. Resour. Crop Evol.
    • Ahokas, H.1    Manninen, M.-L.2
  • 4
    • 0002070281 scopus 로고
    • Geographic variation of α-amylase, β-amylase, β-glucanase, pullulanase and chitinase activity in germinating Hordeum spontaneum barley from Israel and Jordan
    • Ahokas H and Naskali L, (1990). Geographic variation of α-amylase, β-amylase, β-glucanase, pullulanase and chitinase activity in germinating Hordeum spontaneum barley from Israel and Jordan. Genetica 82: 73-78.
    • (1990) Genetica , vol.82 , pp. 73-78
    • Ahokas, H.1    Naskali, L.2
  • 5
    • 0033429266 scopus 로고    scopus 로고
    • Malting enzyme activities, grain protein variation and yield potentials in the displaced genetic resources of barley landraces of Finland
    • Ahokas H and Poukkula M, (1999). Malting enzyme activities, grain protein variation and yield potentials in the displaced genetic resources of barley landraces of Finland. Genet. Resour. Crop Evol. 46: 251-260.
    • (1999) Genet. Resour. Crop Evol. , vol.46 , pp. 251-260
    • Ahokas, H.1    Poukkula, M.2
  • 6
    • 84978591794 scopus 로고
    • Relationships between β-amylase polymorphisms in developing, mature and germinating grains of barley
    • Allison MJ and Swanston JS, (1974). Relationships between β-amylase polymorphisms in developing, mature and germinating grains of barley. J. Inst. Brew. 80: 285-291.
    • (1974) J. Inst. Brew. , vol.80 , pp. 285-291
    • Allison, M.J.1    Swanston, J.S.2
  • 7
    • 84987368804 scopus 로고
    • The development of β-D-glucanases during the germination of barley and the effect of kilning on individual isoenzymes
    • Brunswick P, Manners DJ and Stark JR, (1987). The development of β-D-glucanases during the germination of barley and the effect of kilning on individual isoenzymes. J. Inst. Brew. 93: 181-186.
    • (1987) J. Inst. Brew. , vol.93 , pp. 181-186
    • Brunswick, P.1    Manners, D.J.2    Stark, J.R.3
  • 8
    • 0000704990 scopus 로고    scopus 로고
    • Thermostability variation in alleles of barley beta-amylase
    • Eglinton JK, Langridge P and Evans DE, (1998). Thermostability variation in alleles of barley beta-amylase. J. Cereal Sci. 28: 301-309.
    • (1998) J. Cereal Sci. , vol.28 , pp. 301-309
    • Eglinton, J.K.1    Langridge, P.2    Evans, D.E.3
  • 11
    • 0033180204 scopus 로고    scopus 로고
    • Some thaumatin-like proteins hydrolyse polymeric β-1,3-glucans
    • Grenier J, Potvin C, Trudel J and Asselin A, (1999). Some thaumatin-like proteins hydrolyse polymeric β-1,3-glucans. Plant J. 19: 473-480.
    • (1999) Plant J. , vol.19 , pp. 473-480
    • Grenier, J.1    Potvin, C.2    Trudel, J.3    Asselin, A.4
  • 12
    • 0342305205 scopus 로고
    • Det primitiva jordbrukets metoder i Finland under den historiska tiden
    • Helsinki (Helsingfors)
    • Grotenfelt G, (1899). Det primitiva jordbrukets metoder i Finland under den historiska tiden. J. Simelii Arfvingars Boktryckeri, Helsinki (Helsingfors).
    • (1899) J. Simelii Arfvingars Boktryckeri
    • Grotenfelt, G.1
  • 13
    • 0006190607 scopus 로고
    • Suomalainen peltokasviviljelys
    • eds T Arola et al.
    • Grotenfelt G, (1922). Suomalainen peltokasviviljelys. In: (eds T Arola et al.). Maatalouden tietokirja. Vol. 4: 1-517
    • (1922) Maatalouden Tietokirja , vol.4 , pp. 1-517
    • Grotenfelt, G.1
  • 14
    • 0024318948 scopus 로고
    • Chemical deglycosylation of hen ovomucoid: Protective effect of carbohydrate moiety on tryptic hydrolysis and heat denaturation
    • Gu J, Matsuda T, Nakamura R, Ishiguro H, Ohkubo I, Sasaki M and Takahashi N, (1989). Chemical deglycosylation of hen ovomucoid: protective effect of carbohydrate moiety on tryptic hydrolysis and heat denaturation. J. Biochem. 106: 66-70.
    • (1989) J. Biochem. , vol.106 , pp. 66-70
    • Gu, J.1    Matsuda, T.2    Nakamura, R.3    Ishiguro, H.4    Ohkubo, I.5    Sasaki, M.6    Takahashi, N.7
  • 15
    • 0031150345 scopus 로고    scopus 로고
    • Spring and summer daily subsurface temperatures in three microhabitats in a flat natural loess area in the Negev Desert, Israel
    • Gutterman Y, (1997). Spring and summer daily subsurface temperatures in three microhabitats in a flat natural loess area in the Negev Desert, Israel. J. Arid Environ. 36: 225-235.
    • (1997) J. Arid Environ. , vol.36 , pp. 225-235
    • Gutterman, Y.1
  • 17
    • 0002732304 scopus 로고
    • Kaskiviljelyksen vaikutus suomen metsiin. German summary: Der einfluss der brandwirtschaft auf die wälder Finnlands
    • and appendices
    • Heikinheimo O, (1915). Kaskiviljelyksen vaikutus Suomen metsiin. German summary: Der Einfluss der Brandwirtschaft auf die Wälder Finnlands. Acta Forest. Fenn. 4 Part 2: 1-264 and appendices.
    • (1915) Acta Forest. Fenn. , vol.4 , Issue.PART 2 , pp. 1-264
    • Heikinheimo, O.1
  • 18
    • 0029257339 scopus 로고
    • Molecular evolution of plant β-glucan endohydrolases
    • Høj PB and Fincher GB, (1995). Molecular evolution of plant β-glucan endohydrolases. Plant J. 7: 367-379.
    • (1995) Plant J. , vol.7 , pp. 367-379
    • Høj, P.B.1    Fincher, G.B.2
  • 19
    • 0029866675 scopus 로고    scopus 로고
    • Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-β-glucanase during germination
    • Jensen LG, Olsen O, Kops O, Wolf N, Thomsen KK and Wettstein D von, (1996). Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-β-glucanase during germination. Proc. Natl. Acad. Sci. USA 93: 3487-3491.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3487-3491
    • Jensen, L.G.1    Olsen, O.2    Kops, O.3    Wolf, N.4    Thomsen, K.K.5    Von Wettstein, D.6
  • 20
    • 0032406612 scopus 로고    scopus 로고
    • Inheritance of a codon-optimized transgene expressing heat stable (1,3-1,4)-β-glucanase in scutellum and aleurone of germinating barley
    • Jensen LG, Politz O, Olsen O, Thomsen KK and Wettstein D von, (1998). Inheritance of a codon-optimized transgene expressing heat stable (1,3-1,4)-β-glucanase in scutellum and aleurone of germinating barley. Hereditas 129: 215-225.
    • (1998) Hereditas , vol.129 , pp. 215-225
    • Jensen, L.G.1    Politz, O.2    Olsen, O.3    Thomsen, K.K.4    Von Wettstein, D.5
  • 21
    • 0031735767 scopus 로고    scopus 로고
    • Genetic variation of β-amylase thermostability among varieties of barley, Hordeum vulgare L., and relation to malting quality
    • Kihara M, Kaneko T and Ito K, (1998). Genetic variation of β-amylase thermostability among varieties of barley, Hordeum vulgare L., and relation to malting quality. Plant Breed. 117: 425-428.
    • (1998) Plant Breed. , vol.117 , pp. 425-428
    • Kihara, M.1    Kaneko, T.2    Ito, K.3
  • 22
    • 0032737239 scopus 로고    scopus 로고
    • Geographical variation of β-amylase thermostability among varieties of barley (Hordeum vulgare) and β-amylase deficiency
    • Kihara M, Kaneko T, Ito K, Aida Y and Takeda K, (1999). Geographical variation of β-amylase thermostability among varieties of barley (Hordeum vulgare) and β-amylase deficiency. Plant Breed. 118: 453-455.
    • (1999) Plant Breed. , vol.118 , pp. 453-455
    • Kihara, M.1    Kaneko, T.2    Ito, K.3    Aida, Y.4    Takeda, K.5
  • 23
    • 0342760225 scopus 로고
    • Development of a world cataloguing service for plant breeders and genetics
    • Kirk LE, (1949). Development of a world cataloguing service for plant breeders and genetics. Hereditas Suppl. (1): 608.
    • (1949) Hereditas Suppl. , Issue.1 , pp. 608
    • Kirk, L.E.1
  • 24
    • 0342965271 scopus 로고
    • Main features of agricultural plant breeding in Finland
    • Kivi EI, (1969). Main features of agricultural plant breeding in Finland. Peat Plant News 1: 45-53.
    • (1969) Peat Plant News , vol.1 , pp. 45-53
    • Kivi, E.I.1
  • 25
    • 0031080526 scopus 로고    scopus 로고
    • Purification and characterization of wall-bound exo-1,3-β-D-glucanase from barley (Hordeum vulgare E.) seedlings
    • Kotake T, Nakagawa N, Takeda K and Sakurai N, (1997). Purification and characterization of wall-bound exo-1,3-β-D-glucanase from barley (Hordeum vulgare E.) seedlings. Plant Cell Physiol. 38: 194-200.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 194-200
    • Kotake, T.1    Nakagawa, N.2    Takeda, K.3    Sakurai, N.4
  • 26
    • 0023657286 scopus 로고
    • Primary structure and differential expression of β-amylase in normal and mutant barleys
    • Kreis M, Williamson M, Buxton B, Pywell J, Hejgaard J and Svendsen I, (1987). Primary structure and differential expression of β-amylase in normal and mutant barleys. Eur. J. Biochem. 169: 517-525.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 517-525
    • Kreis, M.1    Williamson, M.2    Buxton, B.3    Pywell, J.4    Hejgaard, J.5    Svendsen, I.6
  • 29
    • 84987323244 scopus 로고
    • Survival of barley (1 → 3, 1 → 4)-β-glucanase isoenzymes during kilning and mashing
    • Loi L, Barton PA and Fincher GB, (1987). Survival of barley (1 → 3, 1 → 4)-β-glucanase isoenzymes during kilning and mashing. J. Cereal Sci. 5: 45-50.
    • (1987) J. Cereal Sci. , vol.5 , pp. 45-50
    • Loi, L.1    Barton, P.A.2    Fincher, G.B.3
  • 30
    • 0001475691 scopus 로고
    • Expression sites and development regulation of genes encoding (1 → 1 → 4)-β-glucanases in germinating barley
    • McFadden GI, Ahluwalia B, Clarke AE and Fincher GB, (1988). Expression sites and development regulation of genes encoding (1 → 1 → 4)-β-glucanases in germinating barley. Planta 173: 500-508.
    • (1988) Planta , vol.173 , pp. 500-508
    • McFadden, G.I.1    Ahluwalia, B.2    Clarke, A.E.3    Fincher, G.B.4
  • 31
    • 0033593468 scopus 로고    scopus 로고
    • The crystal structure of the sevenfold mutant of barley β-amylase with increased thermostability at 2.5 Å resolution
    • Mikami B, Yoon H-J and Yoshigi N, (1999). The crystal structure of the sevenfold mutant of barley β-amylase with increased thermostability at 2.5 Å resolution. J. Mol. Biol. 285: 1235-1243.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1235-1243
    • Mikami, B.1    Yoon, H.-J.2    Yoshigi, N.3
  • 32
    • 0003357057 scopus 로고    scopus 로고
    • Effects of polymannosylation of recombinant cystatin C in yeast on its stability and activity
    • Nakamura S, Ogawa M and Nakai S, (1998). Effects of polymannosylation of recombinant cystatin C in yeast on its stability and activity. J. Agric. Food Chem. 46: 2882-2887.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 2882-2887
    • Nakamura, S.1    Ogawa, M.2    Nakai, S.3
  • 33
    • 0029318605 scopus 로고
    • Increase in thermostability of recombinant barley β-amylase by random mutagenesis
    • Okada Y, Yoshigi N, Sahara H and Koshino S, (1995). Increase in thermostability of recombinant barley β-amylase by random mutagenesis. Biosci. Biotechnol. Biochem. 59: 1152-1153.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1152-1153
    • Okada, Y.1    Yoshigi, N.2    Sahara, H.3    Koshino, S.4
  • 34
    • 0025974948 scopus 로고
    • Improvement of bacterial β-glucanase thermostability by glycosylation
    • Olsen O and Thomsen KK, (1991). Improvement of bacterial β-glucanase thermostability by glycosylation. J. Gen. Microbiol 137: 579-585.
    • (1991) J. Gen. Microbiol , vol.137 , pp. 579-585
    • Olsen, O.1    Thomsen, K.K.2
  • 36
    • 0342740286 scopus 로고
    • Lantstråsädes-och ärtsorternas tidigare och nutida utbredning i Finland, deras egenskaper och betydelse för växtförädlingen samt tillvaratagningen av desamma
    • Pesola VA, (1951). Lantstråsädes-och ärtsorternas tidigare och nutida utbredning i Finland, deras egenskaper och betydelse för växtförädlingen samt tillvaratagningen av desamma. English summary: The Finnish country cereal and pea varieties, their distribution, their agronomic characteristics, and their value for plant breeding. J. Sci. Agric. Soc. Finl. 23: 193-210.
    • (1951) J. Sci. Agric. Soc. Finl. , vol.23 , pp. 193-210
    • Pesola, V.A.1
  • 37
    • 0343400458 scopus 로고
    • Department of Chemical Engineering, University of Technology, Helsinki
    • Simberg NH, (1950). Undersökning av maltkorn. Department of Chemical Engineering, University of Technology, Helsinki.
    • (1950) Undersökning av Maltkorn
    • Simberg, N.H.1
  • 38
    • 0025649961 scopus 로고
    • Structure and tissue-specific regulation of gene encoding barley (1 → 3, 1 → 4)-β-glucan endohydrolases
    • Slakeski N, Baulcombe DC, Devos KM, Ahluwalia B, Doan DNP and Fincher GB, (1990). Structure and tissue-specific regulation of gene encoding barley (1 → 3, 1 → 4)-β-glucan endohydrolases. Mol. Gen. Genet. 224: 437-449.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 437-449
    • Slakeski, N.1    Baulcombe, D.C.2    Devos, K.M.3    Ahluwalia, B.4    Doan, D.N.P.5    Fincher, G.B.6
  • 39
    • 0000211193 scopus 로고
    • Developmental regulation of (1 → 3, 1 → 4)-β-glucanase gene expression in barley
    • Slakeski N and Fincher GB, (1992). Developmental regulation of (1 → 3, 1 → 4)-β-glucanase gene expression in barley. Plant Physiol. 99: 1226-1231.
    • (1992) Plant Physiol. , vol.99 , pp. 1226-1231
    • Slakeski, N.1    Fincher, G.B.2
  • 40
    • 84948499871 scopus 로고
    • Varietal and environmental variations in (1 → 3, 1 → 4)-β-glucan levels and (1 → 3,1 → 4)-β-glucanase potential in barley: Relationships to malting quality
    • Stuart IM, Loi L and Fincher GB, (1988). Varietal and environmental variations in (1 → 3, 1 → 4)-β-glucan levels and (1 → 3,1 → 4)-β-glucanase potential in barley: Relationships to malting quality. J. Cereal Sci. 7: 61-71.
    • (1988) J. Cereal Sci. , vol.7 , pp. 61-71
    • Stuart, I.M.1    Loi, L.2    Fincher, G.B.3
  • 41
    • 0039899325 scopus 로고
    • Effect of β-amylase stability and starch gelatinization during heating on varietal differences in maltose content in sweetpotatoes
    • Takahata Y, Noda T and Nagata T, (1994). Effect of β-amylase stability and starch gelatinization during heating on varietal differences in maltose content in sweetpotatoes. J. Agric. Food Chem. 42: 2564-2569.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2564-2569
    • Takahata, Y.1    Noda, T.2    Nagata, T.3
  • 42
    • 0343194825 scopus 로고
    • Den nordosteuropeiska rian. German summary: Die nordosteuropäische riege
    • Talve I, (1961). Den nordosteuropeiska rian. German summary: Die nordosteuropäische Riege. Skrifter Utgivna av Svenska Litteratursällskapet i Finland Syllabication: 387 (Folklivsstudier VI): 1-341.
    • (1961) Skrifter Utgivna av Svenska Litteratursällskapet i Finland Syllabication , vol.387 , Issue.FOLKLIVSSTUDIER VI , pp. 1-341
    • Talve, I.1
  • 43
    • 0001808111 scopus 로고
    • High surface soil temperatures. On methods of investigation, and thermocouple observations on a wooded heath in the South of Finland
    • Vaartaja O, (1949). High surface soil temperatures. On methods of investigation, and thermocouple observations on a wooded heath in the South of Finland. Oikos 1: 6-28.
    • (1949) Oikos , vol.1 , pp. 6-28
    • Vaartaja, O.1
  • 44
    • 0002706453 scopus 로고
    • Effects of forest fire on soil
    • (eds TT Kozlowski and CE Ahlgren) Academic Press, New York, San Fransisco, London
    • Viro PJ, (1974). Effects of forest fire on soil. Fire and Ecosystems. In: (eds TT Kozlowski and CE Ahlgren) Academic Press, New York, San Fransisco, London, p. 7-45.
    • (1974) Fire and Ecosystems , pp. 7-45
    • Viro, P.J.1
  • 45
    • 0026643229 scopus 로고
    • Structure of the genes encoding Hordeum vulgare (1 → 3,1 → 4)-β-glucanase isoenzymes I and II and functional analysis of their promotors in barley aleurone protoplasts
    • Wolf N, (1992). Structure of the genes encoding Hordeum vulgare (1 → 3,1 → 4)-β-glucanase isoenzymes I and II and functional analysis of their promotors in barley aleurone protoplasts. Mol. Gen. Genet. 234: 33-42.
    • (1992) Mol. Gen. Genet. , vol.234 , pp. 33-42
    • Wolf, N.1
  • 46
    • 0020023025 scopus 로고
    • Purification and chemical properties of two 1,3;1,4-β-glucan endohydrolases from germinating barley
    • Woodward JR and Fincher GB, (1982). Purification and chemical properties of two 1,3;1,4-β-glucan endohydrolases from germinating barley. Eur. J. Biochem. 121: 663-669.
    • (1982) Eur. J. Biochem. , vol.121 , pp. 663-669
    • Woodward, J.R.1    Fincher, G.B.2
  • 47
    • 0031982892 scopus 로고    scopus 로고
    • Expression of the Schwanniomyces occidentalis SWA2 amylase in Saccharomyces cerevisiae: Role of N-glycosylation on activity, stability and secretion
    • Yáñez E, Carmona TA, Tiemblo M, Jiménez A and Fernández-Lobato M, (1998). Expression of the Schwanniomyces occidentalis SWA2 amylase in Saccharomyces cerevisiae: role of N-glycosylation on activity, stability and secretion. Biochem. J. 329: 65-71.
    • (1998) Biochem. J. , vol.329 , pp. 65-71
    • Yáñez, E.1    Carmona, T.A.2    Tiemblo, M.3    Jiménez, A.4    Fernández-Lobato, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.