Bioprocess and Biosystems Engineering

, Volume 26, Issue 2, pp 123–132 | Cite as

Monte Carlo simulation of the α-amylolysis of amylopectin potato starch. 2. α-amylolysis of amylopectin

  • L. M. Marchal
  • R. V. Ulijn
  • C. D. de Gooijer
  • G. T. Franke
  • J. Tramper
Original Paper

Abstract

A model is presented that describes all the saccharides that are produced during the hydrolysis of starch by an α-amylase. Potato amylopectin, the substrate of the hydrolysis reaction, was modeled in a computer matrix. The four different subsite maps presented in literature for α-amylase originating from Bacillus amyloliquefaciens were used to describe the hydrolysis reaction in a Monte Carlo simulation. The saccharide composition predicted by the model was evaluated with experimental values. Overall, the model predictions were acceptable, but no single subsite map gave the best predictions for all saccharides produced. The influence of an α(1→6) linkage on the rate of hydrolysis of nearby α(1→4) linkages by the α-amylase was evaluated using various inhibition constants. For all the subsites considered the use of inhibition constants led to an improvement in the predictions (a decrease of residual sum of squares), indicating the validity of inhibition constants as such. As without inhibition constants, no single subsite map gave the best fit for all saccharides. The possibility of generating a hypothetical subsite map by fitting was therefore investigated. With a genetic algorithm it was possible to construct hypothetical subsite maps (with inhibition constants) that gave further improvements in the average prediction for all saccharides. The advantage of this type of modeling over a regular fit is the additional information about all the saccharides produced during hydrolysis, including the ones that are difficult to measure experimentally.

Keywords

Monte Carlo Starch Hydrolysis Alpha-amylase Saccharides 

References

  1. 1.
    Marchal LM, Zondervan J, Bergsma J, Beeftink HH, Tramper J (2001) Monte Carlo simulation of the α-amylolysis of amylopectin potato starch. 1. Modeling of the structure of amylopectin. Bioproc Biosys Eng 24:163–170Google Scholar
  2. 2.
    Allen JD, Thoma JA (1976) Subsite mapping of enzymes. Application of the depolymerase computer model to two α-amylases. Biochem J 159:121–132PubMedGoogle Scholar
  3. 3.
    Torgerson EM, Brewer LC, Thoma JA (1979) Subsite mapping of enzymes. Use of subsite map to simulate complete time course of hydrolysis of a polymer substrate. Archs Biochem Biophys 196:13–22Google Scholar
  4. 4.
    Iwasa S, Aoshima H, Hiromi K, Hatano H (1974) Subsite affinities of bacterial liquefying α-amylase evaluated from the rate parameters of linear substrates. J Biochem 75:969–978PubMedGoogle Scholar
  5. 5.
    Marchal LM, van der Laar AMJ, Goetheer E, Schimmelpennink EB, Bergsma J, Beeftink HH, Tramper J (1999) The effect of temperature on the saccharide composition obtained after α-amylolysis of starch. Biotechnol Bioeng 63:344–355PubMedGoogle Scholar
  6. 6.
    Thoma JA, Rao CV, Brothers CE, Spradlin JE (1971) Subsite mapping of enzymes. Biochem J 246:5621–5635Google Scholar
  7. 7.
    Thoma JA, Brothers CE, Spradlin JE (1970) Subsite mapping of enzymes. Studies on Bacillus subtilis amylase. Biochemistry 9:1768–1775PubMedGoogle Scholar
  8. 8.
    MacGregor EA, MacGregor AW, Macri LJ, Morgan JE (1994) Models for the action of barley alpha-amylase isozymes on linear substrates. Carbohydr Res 257:249–268PubMedGoogle Scholar
  9. 9.
    Allen JD, Thoma JA (1976) Subsite mapping of enzymes. depolymerase computer modelling. Biochem J 159:105–120PubMedGoogle Scholar
  10. 10.
    Hiromi K (1970) Interpreatation of dependency of rate parameters of the degree of polymerization of substrate in enzyme-catalysed reactions. Evaluation of subsite affinities of exo-enzyme. Biochem Biophys Res Commun 40:1–6PubMedGoogle Scholar
  11. 11.
    Chipman DM, Sharon N (1970) Mechanism of lysozyme action. Science. 165:454–465Google Scholar
  12. 12.
    Gurney RW (1953) Ionic processes in solution. McGraw-Hill, LondonGoogle Scholar
  13. 13.
    Thoma JA, Allen JD (1976) Subsite mapping of enzymes: collecting and processing experimental data—a case study of an amylase–malto–oligosaccharide system. Carbohydr Res 48:105–124PubMedGoogle Scholar
  14. 14.
    Marchal LM, Tramper J (1999) Hydrolytic gain during hydrolysis reactions: implications and correction procedures. Biotechnol Tech 13:325–328Google Scholar
  15. 15.
    Hizukuri S (1996) Starch: analytical aspects. In: Eliasson AC (ed) Carbohydrates in food. Marcel Dekker, New York, pp 347–429Google Scholar
  16. 16.
    French D, Smith EE, Whelan WJ (1972) The structural analysis and enzymatic synthesis of a pentasaccharide alpha-limit dextrin formed from amylopectin by Bacillus substilis alpha-amylase. Carbohydr Res 22:123–134PubMedGoogle Scholar
  17. 17.
    Banzhaf W, Nordin P, Keller RE, Francone FD (1998) Genetic programming, an introduction. Morgan Kaufmann, San FranciscoGoogle Scholar
  18. 18.
    Gidley MJ (1985) Quantification of the structural features of starch polysaccharides by NMR spectroscopy. Carbohydr Res 139:85–93Google Scholar

Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  • L. M. Marchal
    • 1
  • R. V. Ulijn
    • 2
  • C. D. de Gooijer
    • 2
  • G. T. Franke
    • 3
  • J. Tramper
    • 2
  1. 1.Basic Supply GroupCE EmmenThe Netherlands
  2. 2.Department of Food Technology and Nutritional Sciences, Food and Bioprocess Engineering GroupWageningen Agricultural UniversityHD WageningenThe Netherlands
  3. 3.Avebe Research and DevelopmentAA VeendamThe Netherlands

Personalised recommendations