메뉴 건너뛰기




Volumn 26, Issue 1, 2012, Pages 231-239

Hydrolysis of β-limit dextrins by α-amylases from porcine pancreas, Bacillus subtilis, Pseudomonas saccharophila and Bacillus stearothermophilus

Author keywords

Action pattern; Amylase; Hydrolysis; Limit dextrin

Indexed keywords

AMYLASES; BACTERIA; BACTERIOLOGY; CHAIN LENGTH; CHAINS; IODINE;

EID: 79961167039     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2011.06.001     Document Type: Article
Times cited : (22)

References (26)
  • 2
    • 0000930747 scopus 로고
    • Physical properties of starch I. Relationship between iodine stain and chain length
    • Bailey J.M., Whelan W.J. Physical properties of starch I. Relationship between iodine stain and chain length. Journal of Biological Chemistry 1961, 236(4):969-973.
    • (1961) Journal of Biological Chemistry , vol.236 , Issue.4 , pp. 969-973
    • Bailey, J.M.1    Whelan, W.J.2
  • 3
    • 0000029314 scopus 로고
    • Fractional precipitation of amylopectin alpha-dextrins using methanol
    • Bertoft E., Spoof L. Fractional precipitation of amylopectin alpha-dextrins using methanol. Carbohydrate Research 1989, 189(1):169-180.
    • (1989) Carbohydrate Research , vol.189 , Issue.1 , pp. 169-180
    • Bertoft, E.1    Spoof, L.2
  • 4
    • 33947689800 scopus 로고    scopus 로고
    • Temperature impacts the multiple attack action of amylases
    • Bijttebier A., Goesaert H., Delcour J.A. Temperature impacts the multiple attack action of amylases. Biomacromolecules 2007, 8(3):765-772.
    • (2007) Biomacromolecules , vol.8 , Issue.3 , pp. 765-772
    • Bijttebier, A.1    Goesaert, H.2    Delcour, J.A.3
  • 5
    • 72649092791 scopus 로고    scopus 로고
    • Hydrolysis of amylopectin by amylolytic enzymes: structural analysis of the residual amylopectin population
    • Bijttebier A., Goesaert H., Delcour J.A. Hydrolysis of amylopectin by amylolytic enzymes: structural analysis of the residual amylopectin population. Carbohydrate Research 2010, 345(2):235-242.
    • (2010) Carbohydrate Research , vol.345 , Issue.2 , pp. 235-242
    • Bijttebier, A.1    Goesaert, H.2    Delcour, J.A.3
  • 8
    • 74549169007 scopus 로고    scopus 로고
    • Hydrolysis of amylopectin by amylolytic enzymes: level of inner chain attack as an important analytical differentiation criterion
    • Goesaert H., Bijttebier A., Delcour J.A. Hydrolysis of amylopectin by amylolytic enzymes: level of inner chain attack as an important analytical differentiation criterion. Carbohydrate Research 2010, 345(3):397-401.
    • (2010) Carbohydrate Research , vol.345 , Issue.3 , pp. 397-401
    • Goesaert, H.1    Bijttebier, A.2    Delcour, J.A.3
  • 9
    • 75149175501 scopus 로고    scopus 로고
    • Structural properties and gelatinisation characteristics of potato and cassava starches and mutants thereof
    • Gomand S.V., Lamberts L., Derde L.J., Goesaert H., Vandeputte G.E., Goderis B., et al. Structural properties and gelatinisation characteristics of potato and cassava starches and mutants thereof. Food Hydrocolloids 2010, 24:307-317.
    • (2010) Food Hydrocolloids , vol.24 , pp. 307-317
    • Gomand, S.V.1    Lamberts, L.2    Derde, L.J.3    Goesaert, H.4    Vandeputte, G.E.5    Goderis, B.6
  • 11
    • 0040687034 scopus 로고
    • Polymodal distribution of the chain lengths of amylopectins, and its significance
    • Hizukuri S. Polymodal distribution of the chain lengths of amylopectins, and its significance. Carbohydrate Research 1986, 147(2):342-347.
    • (1986) Carbohydrate Research , vol.147 , Issue.2 , pp. 342-347
    • Hizukuri, S.1
  • 12
    • 0000329882 scopus 로고
    • Multi-branched nature of amylose and the action of debranching enzymes
    • Hizukuri S., Takeda Y., Yasuda M., Suzuki A. Multi-branched nature of amylose and the action of debranching enzymes. Carbohydrate Research 1981, 94(2):205-213.
    • (1981) Carbohydrate Research , vol.94 , Issue.2 , pp. 205-213
    • Hizukuri, S.1    Takeda, Y.2    Yasuda, M.3    Suzuki, A.4
  • 13
    • 0032456747 scopus 로고    scopus 로고
    • Fractionation of high-amylose maize starches by differential alcohol precipitation and chromatography of the fractions
    • Klucinec J.D., Thompson D.B. Fractionation of high-amylose maize starches by differential alcohol precipitation and chromatography of the fractions. Cereal Chemistry 1998, 75(6):887-896.
    • (1998) Cereal Chemistry , vol.75 , Issue.6 , pp. 887-896
    • Klucinec, J.D.1    Thompson, D.B.2
  • 14
    • 0032571577 scopus 로고    scopus 로고
    • Quantitative analysis of amylopectin unit chains by means of high-performance anion-exchange chromatography with pulsed amperometric detection
    • Koch K., Andersson R., Aman P. Quantitative analysis of amylopectin unit chains by means of high-performance anion-exchange chromatography with pulsed amperometric detection. Journal of Chromatography A 1998, 800(2):199-206.
    • (1998) Journal of Chromatography A , vol.800 , Issue.2 , pp. 199-206
    • Koch, K.1    Andersson, R.2    Aman, P.3
  • 17
    • 0027372602 scopus 로고
    • Multiple attack mechanism in the porcine pancreatic alpha-amylase hydrolysis of amylose and amylopectin
    • Mazur A.K., Nakatani H. Multiple attack mechanism in the porcine pancreatic alpha-amylase hydrolysis of amylose and amylopectin. Archives of Biochemistry and Biophysics 1993, 306(1):29-38.
    • (1993) Archives of Biochemistry and Biophysics , vol.306 , Issue.1 , pp. 29-38
    • Mazur, A.K.1    Nakatani, H.2
  • 18
    • 0014140609 scopus 로고
    • Multiple attack hypothesis of alpha-amylase action: action of porcine pancreatic, human salivary and Aspergillus oryzae alpha-amylases
    • Robyt J.F., French D. Multiple attack hypothesis of alpha-amylase action: action of porcine pancreatic, human salivary and Aspergillus oryzae alpha-amylases. Archives of Biochemistry and Biophysics 1967, 122(1):8-16.
    • (1967) Archives of Biochemistry and Biophysics , vol.122 , Issue.1 , pp. 8-16
    • Robyt, J.F.1    French, D.2
  • 19
    • 0001960537 scopus 로고
    • A new reagent for the determination of sugars
    • Somogyi M. A new reagent for the determination of sugars. Journal of Biological Chemistry 1945, 160(1):61-68.
    • (1945) Journal of Biological Chemistry , vol.160 , Issue.1 , pp. 61-68
    • Somogyi, M.1
  • 20
    • 1642367502 scopus 로고    scopus 로고
    • Starch - composition, fine structure and architecture
    • Tester R.F., Karkalas J., Qi X. Starch - composition, fine structure and architecture. Journal of Cereal Science 2004, 39(2):151-165.
    • (2004) Journal of Cereal Science , vol.39 , Issue.2 , pp. 151-165
    • Tester, R.F.1    Karkalas, J.2    Qi, X.3
  • 21
    • 5044220259 scopus 로고    scopus 로고
    • Amylopectin molecular structure reflected in macromolecular organization of granular starch
    • Vermeylen R., Goderis B., Reynaers H., Delcour J.A. Amylopectin molecular structure reflected in macromolecular organization of granular starch. Biomacromolecules 2004, 5(5):1775-1786.
    • (2004) Biomacromolecules , vol.5 , Issue.5 , pp. 1775-1786
    • Vermeylen, R.1    Goderis, B.2    Reynaers, H.3    Delcour, J.A.4
  • 22
    • 0023406022 scopus 로고
    • Assay of reducing sugars in the nanomole range with 2,2'-bicinchoninate
    • Waffenschmidt S., Jaenicke L. Assay of reducing sugars in the nanomole range with 2,2'-bicinchoninate. Analytical Biochemistry 1987, 165(2):337-340.
    • (1987) Analytical Biochemistry , vol.165 , Issue.2 , pp. 337-340
    • Waffenschmidt, S.1    Jaenicke, L.2
  • 23
    • 14744279295 scopus 로고    scopus 로고
    • Maize starch-branching enzyme isoforms and amylopectin structure. In the absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching
    • Yao Y., Thompson D.B., Guiltinan M.J. Maize starch-branching enzyme isoforms and amylopectin structure. In the absence of starch-branching enzyme IIb, the further absence of starch-branching enzyme Ia leads to increased branching. Plant Physiology 2004, 136(3):3515-3523.
    • (2004) Plant Physiology , vol.136 , Issue.3 , pp. 3515-3523
    • Yao, Y.1    Thompson, D.B.2    Guiltinan, M.J.3
  • 24
    • 0024465379 scopus 로고
    • Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila
    • Zhou J.H., Baba T., Takano T., Kobayashi S., Arai Y. Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila. Febs Letters 1989, 255(1):37-41.
    • (1989) Febs Letters , vol.255 , Issue.1 , pp. 37-41
    • Zhou, J.H.1    Baba, T.2    Takano, T.3    Kobayashi, S.4    Arai, Y.5
  • 25
    • 0026513012 scopus 로고
    • Properties of the enzyme expressed by the Pseudomonas saccharophila maltotetrahydrolase gene (Mta) in Escherichia coli
    • Zhou J.H., Baba T., Takano T., Kobayashi S., Arai Y. Properties of the enzyme expressed by the Pseudomonas saccharophila maltotetrahydrolase gene (Mta) in Escherichia coli. Carbohydrate Research 1992, 223:255-261.
    • (1992) Carbohydrate Research , vol.223 , pp. 255-261
    • Zhou, J.H.1    Baba, T.2    Takano, T.3    Kobayashi, S.4    Arai, Y.5
  • 26
    • 79961171052 scopus 로고
    • Cloning of exo-maltotetraohydrolase gene from Pseudomonas saccharophila in Escherichia coli
    • Zhou J.H., Takano T., Kobayashi S. Cloning of exo-maltotetraohydrolase gene from Pseudomonas saccharophila in Escherichia coli. Agricultural and Biological Chemistry 1989, 53(1):301-302.
    • (1989) Agricultural and Biological Chemistry , vol.53 , Issue.1 , pp. 301-302
    • Zhou, J.H.1    Takano, T.2    Kobayashi, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.