Characterisation of three starch degrading enzymes: Thermostable β-amylase, maltotetraogenic and maltogenic α-amylases

被引:74
作者
Derde, L. J. [1 ]
Gomand, S. V. [1 ]
Courtin, C. M. [1 ]
Delcour, J. A. [1 ]
机构
[1] Katholieke Univ Leuven, Lab Food Chem & Biochem, Leuven Food Sci & Nutr Res Ctr LFoRCe, B-3001 Louvain, Belgium
关键词
Amylase; Action pattern; Hydrolysis; Malto-oligosaccharide forming alpha-amylase; PSEUDOMONAS-STUTZERI; BACILLUS-STEAROTHERMOPHILUS; RHEOLOGICAL PROPERTIES; FORMING AMYLASE; ACTION PATTERN; PURIFICATION; SACCHAROPHILA; IMPACT; SUGARS;
D O I
10.1016/j.foodchem.2012.05.031
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Maltogenic alpha-amylase from Bacillus stearothermophilus (BStA) is widely used as bread crumb anti-firming enzyme. A maltotetraose-forming alpha-amylase from Pseudomonas saccharophila (PSA) was recently proposed as alternative, hence the need to compare both exo-acting enzymes with some endo-action component. A purely exo-acting thermostable beta-amylase from Clostridium thermosulfurogenes (CTB) was included for reference purposes. Under the experimental conditions used, temperature optima of the enzymes are rather similar (60-65 degrees C), but temperature stability decreased in the order BStA, PSA and CTB. The action of the enzymes on different substrates and their impact on the rheological behaviour of maize starch suspensions demonstrated that, while CTB acts exclusively through an exo-action mechanism, BStA displayed limited endo-action which became more pronounced at higher temperatures. PSA has more substantial endo-action than BStA, which is rather temperature independent. This is important for their impact in processes such as breadmaking, where temperature is gradually increased. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:713 / 721
页数:9
相关论文
共 32 条
  • [1] Temperature impacts the multiple attack action of amylases
    Bijttebier, Annabel
    Goesaert, Hans
    Delcour, Jan A.
    [J]. BIOMACROMOLECULES, 2007, 8 (03) : 765 - 772
  • [2] Hydrolysis of amylopectin by amylolytic enzymes: structural analysis of the residual amylopectin population
    Bijttebier, Annabel
    Goesaert, Hans
    Delcour, Jan A.
    [J]. CARBOHYDRATE RESEARCH, 2010, 345 (02) : 235 - 242
  • [3] Amylase action pattern on starch polymers
    Bijttebier, Annabel
    Goesaert, Hans
    Delcour, Jan A.
    [J]. BIOLOGIA, 2008, 63 (06) : 989 - 999
  • [4] Bowles L.K., 1996, BAKED GOODS FRESHNES, P105
  • [5] Christophersen C, 1998, STARCH-STARKE, V50, P39, DOI 10.1002/(SICI)1521-379X(199801)50:1<39::AID-STAR39>3.0.CO
  • [6] 2-S
  • [7] X-ray structure of Novamyl, the five-domain "maltogenic" α-amylase from Bacillus stearothermophilus:: Maltose and acarbose complexes at 1.7 Å resolution
    Dauter, Z
    Dauter, M
    Brzozowski, AM
    Christensen, S
    Borchert, TV
    Beier, L
    Wilson, KS
    Davies, GJ
    [J]. BIOCHEMISTRY, 1999, 38 (26) : 8385 - 8392
  • [8] Hydrolysis of β-limit dextrins by α-amylases from porcine pancreas, Bacillus subtilis, Pseudomonas saccharophila and Bacillus stearothermophilus
    Derde, L. J.
    Gomand, S. V.
    Courtin, C. M.
    Delcour, J. A.
    [J]. FOOD HYDROCOLLOIDS, 2012, 26 (01) : 231 - 239
  • [9] A COLORIMETRIC METHOD FOR THE DETERMINATION OF SUGARS
    DUBOIS, M
    GILLES, K
    HAMILTON, JK
    REBERS, PA
    SMITH, F
    [J]. NATURE, 1951, 168 (4265) : 167 - 167
  • [10] Wheat flour constituents: how they impact bread quality, and how to impact their functionality
    Goesaert, H
    Brijs, K
    Veraverbeke, WS
    Courtin, CM
    Gebruers, K
    Delcour, JA
    [J]. TRENDS IN FOOD SCIENCE & TECHNOLOGY, 2005, 16 (1-3) : 12 - 30