메뉴 건너뛰기




Volumn 56, Issue 1, 2008, Pages 126-131

Enzymatic synthesis and properties of highly branched rice starch amylose and amylopectin cluster

Author keywords

Amylopectin cluster (APC); Bacillus stearothermophilus maltogenic amylase (BSMA); Bacillus subtilis 168 branching enzyme (BBE); Branched amylose (BA); Highly branched amylopectin cluster (HBAPC); Highly branched amylose (HBA)

Indexed keywords

1,4 ALPHA GLUCAN BRANCHING ENZYME; 4 ALPHA GLUCANOTRANSFERASE; 4 ALPHA-GLUCANOTRANSFERASE; AMYLOPECTIN; AMYLOSE; GLUCAN 1,4 ALPHA MALTOHYDROLASE; GLUCAN 1,4-ALPHA-MALTOHYDROLASE; GLYCOGEN DEBRANCHING ENZYME; GLYCOSIDASE; STARCH; UNCLASSIFIED DRUG;

EID: 38549118304     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf072508s     Document Type: Article
Times cited : (92)

References (32)
  • 1
    • 0031908527 scopus 로고    scopus 로고
    • Multifactorial causation of obesity: Implications for prevention
    • Scott, M. G. Multifactorial causation of obesity: implications for prevention. Am. J. Clin. Nutr. 1998, 67, 563-572.
    • (1998) Am. J. Clin. Nutr , vol.67 , pp. 563-572
    • Scott, M.G.1
  • 2
    • 2642685925 scopus 로고
    • Effect of a high-carbohydrate, low-saturated-fat diet on apolipoprotein B and triglyceride metabolism in Pima Indians
    • Abbott, W.; Swinburn, B.; Ruotolo, G.; Hara, H.; Patti, L.; Harper, I.; Grundy, S.; Howard, B. Effect of a high-carbohydrate, low-saturated-fat diet on apolipoprotein B and triglyceride metabolism in Pima Indians. J. Clin. Invest. 1990, 150, 1313-1319.
    • (1990) J. Clin. Invest , vol.150 , pp. 1313-1319
    • Abbott, W.1    Swinburn, B.2    Ruotolo, G.3    Hara, H.4    Patti, L.5    Harper, I.6    Grundy, S.7    Howard, B.8
  • 3
    • 0032810126 scopus 로고    scopus 로고
    • The functions of 4-α-glucanotransferases and their use for the production of cyclic glucans
    • Takaha, T.; Smith, S. M. The functions of 4-α-glucanotransferases and their use for the production of cyclic glucans. Biotechnol. Genet. Eng. Rev. 1999, 16, 257-280.
    • (1999) Biotechnol. Genet. Eng. Rev , vol.16 , pp. 257-280
    • Takaha, T.1    Smith, S.M.2
  • 4
    • 0027458378 scopus 로고    scopus 로고
    • Takaha, T.; Yanase, M.; Takata, H.; Okada, S.; Smith, S. M. Disproportionating enzyme (4-α-glucanotransferase; E.C 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism. J. Biol. Chem. 1993, 268, 1391-1396.
    • Takaha, T.; Yanase, M.; Takata, H.; Okada, S.; Smith, S. M. Disproportionating enzyme (4-α-glucanotransferase; E.C 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism. J. Biol. Chem. 1993, 268, 1391-1396.
  • 5
    • 33751005820 scopus 로고    scopus 로고
    • The action mode of Thermus aquaticus YT-1,4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin
    • Park, J. H.; Kim, H. J.; Kim, Y. H.; Cha, H. J.; Kim, Y. W.; Kim, T. J.; Kim, Y. R.; Park, K. H. The action mode of Thermus aquaticus YT-1,4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin. Carbohydr. Polym. 2007, 67, 164-173.
    • (2007) Carbohydr. Polym , vol.67 , pp. 164-173
    • Park, J.H.1    Kim, H.J.2    Kim, Y.H.3    Cha, H.J.4    Kim, Y.W.5    Kim, T.J.6    Kim, Y.R.7    Park, K.H.8
  • 6
    • 0032543440 scopus 로고    scopus 로고
    • Cyclic glucans produced by the intramolecular transglycosylation activity of potato D-enzyme on amylopectin
    • Takaha, T.; Yanase, M.; Takata, H.; Okada, S.; Smith, S. M. Cyclic glucans produced by the intramolecular transglycosylation activity of potato D-enzyme on amylopectin. Biochem. Biophys. Res. Commun. 1998, 247, 493-497.
    • (1998) Biochem. Biophys. Res. Commun , vol.247 , pp. 493-497
    • Takaha, T.1    Yanase, M.2    Takata, H.3    Okada, S.4    Smith, S.M.5
  • 7
    • 0037375065 scopus 로고    scopus 로고
    • A cycloamylose-forming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli
    • Bhuiyan, S. H.; Kitaoka, M.; Hayashi, K. A cycloamylose-forming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli. J. Mol. Catal B 2003, 22, 45-53.
    • (2003) J. Mol. Catal B , vol.22 , pp. 45-53
    • Bhuiyan, S.H.1    Kitaoka, M.2    Hayashi, K.3
  • 8
    • 0034302052 scopus 로고    scopus 로고
    • Acceptor specificity of 4-α-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose
    • Tachibana, Y.; Takaha, T.; Fujiwara, S.; Takagi, M.; Imanaka, T. Acceptor specificity of 4-α-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose. J. Biosci. Bioeng. 2000, 90, 406-409.
    • (2000) J. Biosci. Bioeng , vol.90 , pp. 406-409
    • Tachibana, Y.1    Takaha, T.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 9
    • 0030062091 scopus 로고    scopus 로고
    • Potato D-enzyme catalyzes the cyclization of amylose to produce cycloamylose, a novel cyclic glucan
    • Takaha, T.; Yanase, M.; Takata, H.; Okada, S.; Smith, S. M. Potato D-enzyme catalyzes the cyclization of amylose to produce cycloamylose, a novel cyclic glucan. J. Biol. Chem. 1996, 271, 2902-2908.
    • (1996) J. Biol. Chem , vol.271 , pp. 2902-2908
    • Takaha, T.1    Yanase, M.2    Takata, H.3    Okada, S.4    Smith, S.M.5
  • 10
    • 34547851183 scopus 로고    scopus 로고
    • Structural characterization of rice starch in rice cake modified by Thermus scotoductus 4-α-glucanotransferase
    • Seo, N. S.; Roh, S. A.; Auh, J. H.; Park, J. H.; Kim, Y. R.; Park, K. H. Structural characterization of rice starch in rice cake modified by Thermus scotoductus 4-α-glucanotransferase. J. Food. Sci. 2007, 72, C331-C336.
    • (2007) J. Food. Sci , vol.72
    • Seo, N.S.1    Roh, S.A.2    Auh, J.H.3    Park, J.H.4    Kim, Y.R.5    Park, K.H.6
  • 12
    • 0034705064 scopus 로고    scopus 로고
    • Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family
    • Park, K. H.; Kim, T. J.; Cheong, T. K.; Kim, J. W.; Oh, B. H.; Svensson, B. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochem. Biophys. Acta 2000, 1478, 165-185.
    • (2000) Biochem. Biophys. Acta , vol.1478 , pp. 165-185
    • Park, K.H.1    Kim, T.J.2    Cheong, T.K.3    Kim, J.W.4    Oh, B.H.5    Svensson, B.6
  • 13
    • 34247614099 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1
    • Kim, J. W.; Kim, Y. H.; Lee, H. S.; Yang, S. J.; Kim, Y. W.; Lee, M. H.; Kim, J. W.; Seo, N. S.; Park, C. S.; Park, K. H. Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1. Biochem. Biophys. Acta 2007, 661-669
    • (2007) Biochem. Biophys. Acta , pp. 661-669
    • Kim, J.W.1    Kim, Y.H.2    Lee, H.S.3    Yang, S.J.4    Kim, Y.W.5    Lee, M.H.6    Kim, J.W.7    Seo, N.S.8    Park, C.S.9    Park, K.H.10
  • 14
    • 84996335527 scopus 로고
    • New shuttle vectors for Escherichia coli and Bacillus subtilis. IV. The nucleotide sequence of pHY300PLK and some properties in relation to transformation
    • Ishiwa, H.; Shibahara-Sone, H. New shuttle vectors for Escherichia coli and Bacillus subtilis. IV. The nucleotide sequence of pHY300PLK and some properties in relation to transformation. Jpn. J. Genet. 1986, 61, 515-528.
    • (1986) Jpn. J. Genet , vol.61 , pp. 515-528
    • Ishiwa, H.1    Shibahara-Sone, H.2
  • 15
    • 0042642238 scopus 로고
    • Properties of rice starch prepared by alkali method with various conditions
    • Yamamoto, K.; Sawada, S.; Onogaki, T. Properties of rice starch prepared by alkali method with various conditions. J. Jpn. Soc. Starch Sci. 1973, 20, 99-104.
    • (1973) J. Jpn. Soc. Starch Sci , vol.20 , pp. 99-104
    • Yamamoto, K.1    Sawada, S.2    Onogaki, T.3
  • 16
    • 0003089629 scopus 로고
    • Separation of amylose from amylopectin of starch by extraction-sedimentation procedure
    • Montgomery, E. M.; Senti, F. R. Separation of amylose from amylopectin of starch by extraction-sedimentation procedure. J. Polym. Sci. 1958, 28, 1-9.
    • (1958) J. Polym. Sci , vol.28 , pp. 1-9
    • Montgomery, E.M.1    Senti, F.R.2
  • 17
    • 0026079801 scopus 로고
    • Genetic competence in Bacillus subtilis
    • Dubnau, D. Genetic competence in Bacillus subtilis. Microbiol. Mol. Biol. Rev. 1991, 55, 395-424.
    • (1991) Microbiol. Mol. Biol. Rev , vol.55 , pp. 395-424
    • Dubnau, D.1
  • 18
    • 0032053544 scopus 로고    scopus 로고
    • Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose
    • Cha, H. J.; Yoon, H. G.; Kim, Y. W.; Lee, H. S.; Kim, J. W.; Kweon, K. S.; Oh, B. H.; Park, K. H. Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose. Eur. J. Biochem. 1998, 253, 251-262.
    • (1998) Eur. J. Biochem , vol.253 , pp. 251-262
    • Cha, H.J.1    Yoon, H.G.2    Kim, Y.W.3    Lee, H.S.4    Kim, J.W.5    Kweon, K.S.6    Oh, B.H.7    Park, K.H.8
  • 19
    • 0035960637 scopus 로고    scopus 로고
    • Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the TV-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium
    • Kim, T. J.; Nguyen, V. D.; Lee, H. S.; Kim, M. J.; Cho, H. Y.; Kim, Y. W.; Moon, T. W.; Park, C. S.; Kim, J. W.; Oh, B. H.; Lee, S. B.; Svensson, B.; Park, K. H. Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the TV-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium. Biochemistry 2001, 40, 14182-14190.
    • (2001) Biochemistry , vol.40 , pp. 14182-14190
    • Kim, T.J.1    Nguyen, V.D.2    Lee, H.S.3    Kim, M.J.4    Cho, H.Y.5    Kim, Y.W.6    Moon, T.W.7    Park, C.S.8    Kim, J.W.9    Oh, B.H.10    Lee, S.B.11    Svensson, B.12    Park, K.H.13
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0027991845 scopus 로고
    • Properties and active center of the thermostable branching enzyme from Bacillus stearothermophilus
    • Takata, H. T.; Takaha, T.; Kuriki, S.; Okada, M.; Takagi; Imanaka, T. Properties and active center of the thermostable branching enzyme from Bacillus stearothermophilus. Appl. Environ. Microbiol. 1994, 60, 3096-3104.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 3096-3104
    • Takata, H.T.1    Takaha, T.2    Kuriki, S.3    Okada, M.4    Takagi5    Imanaka, T.6
  • 22
    • 0026660023 scopus 로고
    • Purification and characterization of a novel thermostable 4-α- glucanotransferase of Thermotoga maritima cloned in Escherichia coli
    • Liebl, W.; Feil, R.; Gabelsberger, J.; Kellermann, J.; Schleifer, K. Purification and characterization of a novel thermostable 4-α- glucanotransferase of Thermotoga maritima cloned in Escherichia coli. Eur. J. Biochem. 1992, 207, 81-88.
    • (1992) Eur. J. Biochem , vol.207 , pp. 81-88
    • Liebl, W.1    Feil, R.2    Gabelsberger, J.3    Kellermann, J.4    Schleifer, K.5
  • 23
    • 33747333106 scopus 로고
    • Use of dinitrosalycylic acid reagent for determination of reducing sugar
    • Miller, C. L. Use of dinitrosalycylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31, 426-428.
    • (1959) Anal. Chem , vol.31 , pp. 426-428
    • Miller, C.L.1
  • 24
    • 38549164519 scopus 로고    scopus 로고
    • Keston, A. S. Colorimetric enzymatic reagents for glucose. Abstracts of Papers; 129th Meeting of the American Chemical Society; American Chemical Society: Washington, DC, 1956; p 31.
    • Keston, A. S. Colorimetric enzymatic reagents for glucose. Abstracts of Papers; 129th Meeting of the American Chemical Society; American Chemical Society: Washington, DC, 1956; p 31.
  • 25
    • 0025766291 scopus 로고
    • Miniaturization of three carbohydrate analyses using a microsample plate reader
    • Fox, J. D.; Robyt, J. F. Miniaturization of three carbohydrate analyses using a microsample plate reader. Anal. Biochem. 1991, 195, 93-96.
    • (1991) Anal. Biochem , vol.195 , pp. 93-96
    • Fox, J.D.1    Robyt, J.F.2
  • 27
    • 33645752829 scopus 로고    scopus 로고
    • Modification of rice starch by selective degradation of amylose using alkalophilic Bacillus cyclomaltodextrinase
    • Auh, J. H.; Chae, H. Y.; Kim, Y. R.; Shim, K. H.; Yoo, S. H.; Park, K. H. Modification of rice starch by selective degradation of amylose using alkalophilic Bacillus cyclomaltodextrinase. J. Agric. Food Chem. 2006, 54, 2413-2419.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 2413-2419
    • Auh, J.H.1    Chae, H.Y.2    Kim, Y.R.3    Shim, K.H.4    Yoo, S.H.5    Park, K.H.6
  • 28
    • 0041600012 scopus 로고    scopus 로고
    • The enzymatic determination of starch in food, feed and raw materials of the starch industry
    • Brunt, K.; Sanders, P.; Rozema, T. The enzymatic determination of starch in food, feed and raw materials of the starch industry. Starch 1998, 10, 413-419.
    • (1998) Starch , vol.10 , pp. 413-419
    • Brunt, K.1    Sanders, P.2    Rozema, T.3
  • 29
    • 0014939925 scopus 로고
    • The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme
    • Robyt, J. F.; French, D. The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme. J. Biol. Chem. 1970, 245, 3917-3927.
    • (1970) J. Biol. Chem , vol.245 , pp. 3917-3927
    • Robyt, J.F.1    French, D.2
  • 30
    • 38549104469 scopus 로고    scopus 로고
    • Mechanism of porcine pancreatic α-amylase: Inhibition of amylose and maltopentaose hydrolysis by α-, β- and γ-cyclodextrins
    • Desseaux, V.; Koukiekolo, R.; Moreau, Y.; Santimone, M.; Marchis-Mouren, G. Mechanism of porcine pancreatic α-amylase: Inhibition of amylose and maltopentaose hydrolysis by α-, β- and γ-cyclodextrins. Eur. J. Biochem. 2001, 265, 20-26.
    • (2001) Eur. J. Biochem , vol.265 , pp. 20-26
    • Desseaux, V.1    Koukiekolo, R.2    Moreau, Y.3    Santimone, M.4    Marchis-Mouren, G.5
  • 31
    • 77957078845 scopus 로고
    • Phospholipid hydrolysate and antistaling amylase effects on retrogradation of starch in bread
    • Kweon, M. R.; Park, C. S.; Auh, J. H.; Cho, B. M.; Yang, N. S.; Park, K. H. Phospholipid hydrolysate and antistaling amylase effects on retrogradation of starch in bread. J. Food Sci. 1994, 59, 1072-1076.
    • (1994) J. Food Sci , vol.59 , pp. 1072-1076
    • Kweon, M.R.1    Park, C.S.2    Auh, J.H.3    Cho, B.M.4    Yang, N.S.5    Park, K.H.6
  • 32
    • 0030664918 scopus 로고    scopus 로고
    • Retrogradation of starches from different botanical sources
    • Jacobson, M. R.; Obanni, M.; Bemiller, J. N. Retrogradation of starches from different botanical sources. Cereal Chem. 1997, 74, 511-518.
    • (1997) Cereal Chem , vol.74 , pp. 511-518
    • Jacobson, M.R.1    Obanni, M.2    Bemiller, J.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.