메뉴 건너뛰기




Volumn 218, Issue 4, 2004, Pages 542-551

Limit dextrinase from germinating barley has endotransglycosylase activity, which explains its activation by maltodextrins

Author keywords

Amylopectin; Endotransglycosylation; Hordeum; Limit dextrinase; Pullulan; Starch

Indexed keywords

BIOASSAY; CATALYSTS; CROSSLINKING; DEGRADATION; DYES; ENZYMES; FLUORESCENCE; POLYMERIZATION; VISCOSITY;

EID: 1442291031     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-003-1141-1     Document Type: Article
Times cited : (10)

References (43)
  • 1
    • 0021321955 scopus 로고
    • A rapid, sensitive method for detection of alkaline phosphatase- conjugated anti-antibody on Western blots
    • Blake, MS, Johnston KH, Russell-Jones GJ, EC Gotsclich (1984) A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal Biochem 136:175-179
    • (1984) Anal Biochem , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnston, K.H.2    Russell-Jones, G.J.3    Gotsclich, E.C.4
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0033102225 scopus 로고    scopus 로고
    • A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley
    • Burton RA, Zhang X-Q, Hrmova M, Fincher GB (1999) A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol 199:859-871
    • (1999) Plant Physiol , vol.199 , pp. 859-871
    • Burton, R.A.1    Zhang, X.-Q.2    Hrmova, M.3    Fincher, G.B.4
  • 6
    • 0033428817 scopus 로고    scopus 로고
    • Over-expression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain
    • Cho M-J, Wong JH, Marx C, Jiang W, Lemaux PG, Buchanan BB (1999) Over-expression of thioredoxin h leads to enhanced activity of starch debranching enzyme (pullulanase) in barley grain. Proc Natl Acad Sci USA 96:14641-14646
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14641-14646
    • Cho, M.-J.1    Wong, J.H.2    Marx, C.3    Jiang, W.4    Lemaux, P.G.5    Buchanan, B.B.6
  • 7
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • Gilbert HJ, Davies G, Henrissat B, Svensson, B (eds) The Royal Society of Chemistry, Cambridge
    • Coutinho PM, Henrissat B (1999) Carbohydrate-active enzymes: an integrated database approach. In: Gilbert HJ, Davies G, Henrissat B, Svensson, B (eds) Recent advances in carbohydrate bioengineering. The Royal Society of Chemistry, Cambridge, pp 3-12
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 9
    • 0016466535 scopus 로고
    • The limit dextrinases from ungerminated oats (Avena sativa L.) and ungerminated rice (Orzya sativa L.)
    • Dunn G, Manners DJ (1975) The limit dextrinases from ungerminated oats (Avena sativa L.) and ungerminated rice (Orzya sativa L.). Carbohydr Res 39:283-293
    • (1975) Carbohydr Res , vol.39 , pp. 283-293
    • Dunn, G.1    Manners, D.J.2
  • 10
    • 84979186657 scopus 로고
    • Structural analysis of wort dextrins by means of beta-amylase and the debranching enzyme, pullulanase
    • Enevoldsen BS, Bathgate GN (1969) Structural analysis of wort dextrins by means of beta-amylase and the debranching enzyme, pullulanase. J Inst Brew London 75:433-443
    • (1969) J Inst Brew London , vol.75 , pp. 433-443
    • Enevoldsen, B.S.1    Bathgate, G.N.2
  • 11
    • 0030996421 scopus 로고    scopus 로고
    • Novel dot blot assays for glycosyltransferases and glycosylhydrolases: Optimisation for xyloglucan endotransgly-cosylase (XET) activity
    • Fry SC (1997) Novel dot blot assays for glycosyltransferases and glycosylhydrolases: optimisation for xyloglucan endotransgly-cosylase (XET) activity. Plant J 11:1141-1150
    • (1997) Plant J , vol.11 , pp. 1141-1150
    • Fry, S.C.1
  • 13
    • 0033998979 scopus 로고    scopus 로고
    • Review: Cyclodextrins and their interaction with amylolytic enzymes
    • Hamilton LM, Kelly CT, Fogarty WM (2000) Review: cyclodextrins and their interaction with amylolytic enzymes. Enzyme Microbial Technol 26:561-567
    • (2000) Enzyme Microbial Technol , vol.26 , pp. 561-567
    • Hamilton, L.M.1    Kelly, C.T.2    Fogarty, W.M.3
  • 14
    • 0016991188 scopus 로고
    • The limit dextrinase from malted sorghum (Sorghum vulgare)
    • Hardie DG, Manners DJ, Yellowlees D (1976) The limit dextrinase from malted sorghum (Sorghum vulgare) Carbohydr Res 50:75-85
    • (1976) Carbohydr Res , vol.50 , pp. 75-85
    • Hardie, D.G.1    Manners, D.J.2    Yellowlees, D.3
  • 16
    • 0034202503 scopus 로고    scopus 로고
    • Synthesis of novel heterobranched beta-cyclodextrins from 4(2)-O-beta-D-galactosyl-maltose and beta-cyclodextrin by the reverse action of pullulanase, and isolation and characterisation of the products
    • Kitahata S, Tanimoto T, Ikuta A, Tanaka K, Fujita K, Hashimoto H, Murakami H, Nakano H, Koizumi K (2000) Synthesis of novel heterobranched beta-cyclodextrins from 4(2)-O-beta-D-galactosyl-maltose and beta-cyclodextrin by the reverse action of pullulanase, and isolation and characterisation of the products. Biosci Biotechnol Biochem 64:1223-1229
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1223-1229
    • Kitahata, S.1    Tanimoto, T.2    Ikuta, A.3    Tanaka, K.4    Fujita, K.5    Hashimoto, H.6    Murakami, H.7    Nakano, H.8    Koizumi, K.9
  • 17
    • 0031873219 scopus 로고    scopus 로고
    • Large-scale purification and characterisation of barley limit dextrinase, a member of the alpha-amylase structural family
    • Kristensen M, Planchot V, Abe J-I, Svensson B (1998) Large-scale purification and characterisation of barley limit dextrinase, a member of the alpha-amylase structural family. Cereal Chem 75:473-479
    • (1998) Cereal Chem , vol.75 , pp. 473-479
    • Kristensen, M.1    Planchot, V.2    Abe, J.-I.3    Svensson, B.4
  • 18
    • 0032920149 scopus 로고    scopus 로고
    • Isolation and characterisation of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley
    • Kristensen M, Lok F, Planchot V, Svendson I, Leah R, Svensson B (1999) Isolation and characterisation of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley. BBA 1431:538-546
    • (1999) BBA , vol.1431 , pp. 538-546
    • Kristensen, M.1    Lok, F.2    Planchot, V.3    Svendson, I.4    Leah, R.5    Svensson, B.6
  • 19
    • 0032748917 scopus 로고    scopus 로고
    • The starch debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm
    • Kubo A, Fujita N, Harada K, Matsuda T, Satoh H, Nakamura Y (1999) The starch debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm. Plant Physiol 121:399-409
    • (1999) Plant Physiol , vol.121 , pp. 399-409
    • Kubo, A.1    Fujita, N.2    Harada, K.3    Matsuda, T.4    Satoh, H.5    Nakamura, Y.6
  • 20
    • 0015051534 scopus 로고
    • The substrate specificity of amylopectin-debranching enzymes from sweet corn
    • Lee EY, Marshall JJ, Whelan WJ (1971) The substrate specificity of amylopectin-debranching enzymes from sweet corn. Arch Biochem Biophys 143:365-374
    • (1971) Arch Biochem Biophys , vol.143 , pp. 365-374
    • Lee, E.Y.1    Marshall, J.J.2    Whelan, W.J.3
  • 21
    • 0002885532 scopus 로고
    • Barley malt limit dextrinase: Varietal, environmental and malting effect
    • Lee WJ, Pyler RE (1984) Barley malt limit dextrinase: varietal, environmental and malting effect. J Am Soc Brew Chemists 42:11-17
    • (1984) J Am Soc Brew Chemists , vol.42 , pp. 11-17
    • Lee, W.J.1    Pyler, R.E.2
  • 22
    • 0015333650 scopus 로고
    • A new reaction for colorimetric determination of carbohydrates
    • Lever M (1972) A new reaction for colorimetric determination of carbohydrates. Anal Biochem 47:273-279
    • (1972) Anal Biochem , vol.47 , pp. 273-279
    • Lever, M.1
  • 23
    • 0000687121 scopus 로고
    • Development of limit dextrinase in germinated barley (Hordeum vulgare L). Evidence of proteolytic activation
    • Longstaff MA, Bryce JH (1993) Development of limit dextrinase in germinated barley (Hordeum vulgare L). Evidence of proteolytic activation. Plant Physiol 101:881-889
    • (1993) Plant Physiol , vol.101 , pp. 881-889
    • Longstaff, M.A.1    Bryce, J.H.2
  • 24
    • 0030502120 scopus 로고    scopus 로고
    • Malting and brewing science: Challenges and opportunities
    • MacGregor AW (1996) Malting and brewing science: challenges and opportunities. J Inst Brew 102:97-102
    • (1996) J Inst Brew , vol.102 , pp. 97-102
    • MacGregor, A.W.1
  • 25
    • 0002895097 scopus 로고
    • Carbohydrates of the barley grain
    • MacGregor AW, Bhatty RS (eds) American Association of Cereal Chemists, St. Paul, MN
    • MacGregor AW, Fincher GB (1993) Carbohydrates of the barley grain. In: MacGregor AW, Bhatty RS (eds) Barley: chemistry and technology. American Association of Cereal Chemists, St. Paul, MN, pp 73-130
    • (1993) Barley: Chemistry and Technology , pp. 73-130
    • MacGregor, A.W.1    Fincher, G.B.2
  • 26
    • 0028095685 scopus 로고
    • Purification and characterisation of limit dextrinase inhibitors from barley
    • MacGregor AW, Macri LJ, Schroeder SW, Bazin SL (1994) Purification and characterisation of limit dextrinase inhibitors from barley. J Cereal Sci 20:33-41
    • (1994) J Cereal Sci , vol.20 , pp. 33-41
    • MacGregor, A.W.1    Macri, L.J.2    Schroeder, S.W.3    Bazin, S.L.4
  • 27
    • 0000573870 scopus 로고    scopus 로고
    • Modelling the contribution of alpha-amylase, beta-amylase and limit dextrinase to starch degradation during mashing
    • MacGregor AW, Bazin SL, Macri LJ, Babb JC (1999) Modelling the contribution of alpha-amylase, beta-amylase and limit dextrinase to starch degradation during mashing. J Cereal Sci 29:161-169
    • (1999) J Cereal Sci , vol.29 , pp. 161-169
    • MacGregor, A.W.1    Bazin, S.L.2    Macri, L.J.3    Babb, J.C.4
  • 28
    • 0036191744 scopus 로고    scopus 로고
    • Effect of starch hydrolysis products on the determination of limit dextrinase and limit dextrinase inhibitors in barley and malt
    • MacGregor AW, Bazin SL, Schroeder SW (2002) Effect of starch hydrolysis products on the determination of limit dextrinase and limit dextrinase inhibitors in barley and malt. J Cereal Sci 35:17-28
    • (2002) J Cereal Sci , vol.35 , pp. 17-28
    • MacGregor, A.W.1    Bazin, S.L.2    Schroeder, S.W.3
  • 30
    • 0027113459 scopus 로고
    • Measurement of the content of limit dextrinase in cereal flours
    • McCleary BV (1992) Measurement of the content of limit dextrinase in cereal flours. Carbohydr Res 227:257-268
    • (1992) Carbohydr Res , vol.227 , pp. 257-268
    • McCleary, B.V.1
  • 31
    • 0001123198 scopus 로고
    • Xyloglucan oligosaccharides promote growth and activate cellulase: Evidence for a role for cellulase in cell expansion
    • McDougall GJ, Fry SC (1990) Xyloglucan oligosaccharides promote growth and activate cellulase: evidence for a role for cellulase in cell expansion. Plant Physiol 93:1042-1048
    • (1990) Plant Physiol , vol.93 , pp. 1042-1048
    • McDougall, G.J.1    Fry, S.C.2
  • 32
    • 0035372096 scopus 로고    scopus 로고
    • Effect of small carbohydrates on the catalytic activity of a protease and two glycohydrolases
    • Merji M, Mathlouthi M (2001) Effect of small carbohydrates on the catalytic activity of a protease and two glycohydrolases. Carbohydr Polym 45:161-167
    • (2001) Carbohydr Polym , vol.45 , pp. 161-167
    • Merji, M.1    Mathlouthi, M.2
  • 34
    • 0031741515 scopus 로고    scopus 로고
    • Analysis of starch structure using fluorophore-assisted carbohydrate electrophoresis
    • Morell MK, Samuel MS, O'Shea MG (1998) Analysis of starch structure using fluorophore-assisted carbohydrate electrophoresis. Electrophoresis 19:2603-2611
    • (1998) Electrophoresis , vol.19 , pp. 2603-2611
    • Morell, M.K.1    Samuel, M.S.2    O'Shea, M.G.3
  • 35
    • 0030814320 scopus 로고    scopus 로고
    • Correlation between activities of starch debranching enzyme and alpha-polyglucan structure in endosperms of sugary-1 mutants of rice
    • Nakamura Y, Kubo A, Shimamune T, Matsuda T, Harada K, Satoh H (1997) Correlation between activities of starch debranching enzyme and alpha-polyglucan structure in endosperms of sugary-1 mutants of rice. Plant J 12:143-153
    • (1997) Plant J , vol.12 , pp. 143-153
    • Nakamura, Y.1    Kubo, A.2    Shimamune, T.3    Matsuda, T.4    Harada, K.5    Satoh, H.6
  • 36
    • 0000420233 scopus 로고
    • A debranching enzyme deficiency in endosperm of the sugary-1 mutants of maize (Zea mays)
    • Pan D, Nelson OE (1984) A debranching enzyme deficiency in endosperm of the sugary-1 mutants of maize (Zea mays). Plant Physiol 74:324-328
    • (1984) Plant Physiol , vol.74 , pp. 324-328
    • Pan, D.1    Nelson, O.E.2
  • 37
    • 0002005134 scopus 로고
    • Utilisation of wort carbohydrates
    • Panchal CJ, Stewart GG (1979) Utilisation of wort carbohydrates. Brew Dig 54:36-43
    • (1979) Brew Dig , vol.54 , pp. 36-43
    • Panchal, C.J.1    Stewart, G.G.2
  • 38
    • 0010980673 scopus 로고
    • Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels
    • Sissons MJ, Lance RCM, Sparrow DHB (1993) Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels. J Cereal Sci 17:19-24
    • (1993) J Cereal Sci , vol.17 , pp. 19-24
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 39
    • 7444225823 scopus 로고    scopus 로고
    • Malt limit dextrinase and its importance in brewing
    • VTT, Technical Research Centre of Finland, Espoo, Finland
    • Stenholm K (1997) Malt limit dextrinase and its importance in brewing. VTT publication no 323, VTT, Technical Research Centre of Finland, Espoo, Finland
    • (1997) VTT Publication No 323
    • Stenholm, K.1
  • 40
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family, catalytic mechanism, substrate specificity, and stability
    • Svensson B (1994) Protein engineering in the α-amylase family, catalytic mechanism, substrate specificity, and stability. Plant Mol Biol 25:141-157
    • (1994) Plant Mol Biol , vol.25 , pp. 141-157
    • Svensson, B.1
  • 41
    • 84987306048 scopus 로고
    • The effects of different steeping regimes on water uptake, germination rate, milling energy and hot water extract
    • Swanston JS, Taylor K (1990) The effects of different steeping regimes on water uptake, germination rate, milling energy and hot water extract. J Inst Brew 96:3-6
    • (1990) J Inst Brew , vol.96 , pp. 3-6
    • Swanston, J.S.1    Taylor, K.2
  • 42
    • 0027458378 scopus 로고
    • Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism
    • Takaha T, Yanase M, Okada S, Smith SM (1993) Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism. J Biol Chem 268:1391-1396
    • (1993) J Biol Chem , vol.268 , pp. 1391-1396
    • Takaha, T.1    Yanase, M.2    Okada, S.3    Smith, S.M.4
  • 43
    • 0026764917 scopus 로고
    • Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at the α-(1-4)-and α-(1-6)-glucosidic linkages
    • Takata H, Kuriki T, Okada S, Takesada Y, Iizuka M, Minamiura N, Imanaka T (1992) Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at the α-(1-4)-and α-(1-6)-glucosidic linkages. J Biol Chem 267:18447-18452
    • (1992) J Biol Chem , vol.267 , pp. 18447-18452
    • Takata, H.1    Kuriki, T.2    Okada, S.3    Takesada, Y.4    Iizuka, M.5    Minamiura, N.6    Imanaka, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.