A stochastic model for predicting dextrose equivalent and saccharide composition during hydrolysis of starch by α-amylase

Biotechnology and Bioengineering

Volumn 100, Issue 4, 2008, Pages 684-697

  Besselink, Tamara ^a   Baks, Tim ^a   Janssen, Anja E M ^a   Boom, Rernko M ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

amylase; Amylopectin structure; Modeling; Starch hydrolysis; Stochastic model; Subsite mapping

Indexed keywords

BACTERIOLOGY; BIOMOLECULES; CARBOHYDRATES; DEXTROSE; EQUIVALENCE CLASSES; FORECASTING; GLUCOSE; HYDROLYSIS; MAPS; MATHEMATICAL MODELS; ORGANIC COMPOUNDS; STARCH; STOCHASTIC CONTROL SYSTEMS; STOCHASTIC PROGRAMMING; SUBSTRATES; TWO DIMENSIONAL;

ABSOLUTE VALUES; BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS; BREAKDOWN (BD); DEPOLYMERASE; EXPERIMENTAL DATA; EXPERIMENTAL VALUES; HEPTASACCHARIDES; MALTOHEXAOSE; MODEL DATA; MODEL INPUT; ORDER-OF MAGNITUDES; SIMULATED DATA; STARCH HYDROLYSIS; SUBSTRATE MODELING; TWO-DIMENSIONAL (2D); WEIGHT FRACTIONS;

STOCHASTIC MODELS;

AMYLASE; AMYLOPECTIN; GLUCOSE; STARCH;

ACCURACY; ARTICLE; BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS; ENZYME ACTIVITY; HYDROLYSIS; PREDICTION; REACTION ANALYSIS; SIMULATION; STOCHASTIC MODEL;

ALPHA-AMYLASE; BACILLUS; BINDING SITES; GLUCOSE; HYDROLYSIS; KINETICS; MODELS, BIOLOGICAL; MONTE CARLO METHOD; OLIGOSACCHARIDES; POLYSACCHARIDES, BACTERIAL; PROTEIN BINDING; REFERENCE VALUES; STARCH; STOCHASTIC PROCESSES; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

BACILLUS AMYLOLIQUEFACIENS; BACILLUS LICHENIFORMIS;

EID: 46249107660     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21799     Document Type: Article

References (36)

1. Allen JD, Thoma JA. 1976a. Subsite mapping of enzymes: Depolymerase computer modelling. Biochem J 159:105-120.
2. Allen JD, Thoma JA. 1976b. Subsite mapping of enzymes: Application of the depolymerase computer model to two α-amylases. Biochem J 159:121-132.
3. Baks T, Janssen AEM, Boom RM. 2006. A kinetic model to explain the maximum in α-amylase activity measurements in the presence of small carbohydrates. Biotechnol Bioeng 94:431-440.
4. Baks T, Kappen FHJ, Janssen AEM, Boom RM. 2007. Towards an optimal process for gelatinisation and enzymatic hydrolysis of highly concentrated starch-water mixtures. J Cereal Sci, in press. DOI: 10.1016/j.jcs. 2007.03.011.
5. Brandam C, Meyer XM, Proth J, Strehaiano P, Pinguad H. 2003. An original kinetic model for the enzymatic hydrolysis of starch during mashing. Biochem Eng J 13:43-52.
6. Davies GJ, Wilson KS, Henrissat B. 1997. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 321:557-559.
7. De Cordt S, Vanhoof K, Hu J, Maesmans G, Hendrickx M, Tobback P. 1992. Thermostability of soluble and immobilized α-amylase from Bacillus licheniformis. Biotechnol Bioeng 40:396-402.
8. De Cordt S, Hendrickx M, Maesmans G, Tobback P. 1994. The influence of polyalcohols and carbohydrates on the thermostability of α-amylase. Biotechnol Bioeng 43:107-114.
9. Declerck N, Machius M, Chambert R, Wiegand G, Huber R, Gaillardin C. 1997. Hyperthermostable mutants of Bacillus licheniformis α-amylase: Thermodynamic studies and structural interpretation. Protein Eng 10:541-549.
10. Dobreva E, Ivanova V, Emanuilova E. 1994. Effect of temperature on some characteristics of the thermostable α-amylase from Bacillus licheniformis. World J Microbiol Biotechnol 10:547-550.
11. Ellis RP, Cochrane MP, Dale MFB, Duffus CM, Lynn A, Morrison IM, Prentice RDM, Swanston JS, Tiller SA. 1998. Starch production and industrial use. J Sci Food Agric 77:289-311.
12. Fitter J, Herrmann R, Dencher NA, Blume A, Hauss T. 2001. Activity and stability of a thermostable α-amylase compared to its mesophilic homologue: Mechanisms of thermal adaptation. Biochemistry 40: 10723-10731.
13. French D, Smith EE, Whelan WJ. 1972. The structural analysis and enzymatic synthesis of a pentasaccharide alpha-limit dextrin formed from amylopectin by Bacillus subtilis alpha-amylase. Carbohydr Res 22:123-134.
14. Hanashiro I, Takeda Y. 1998. Examination of number-average degree of polymerization and molar-based distribution of amylose by fluorescent labelling with 2-aminopyridine. Carbohydr Res 306:421-426.
15. Hizukuri S, Maehara Y. 1990. Fine structure of wheat amylopectin: The mode of A to B chain binding. Carbohydr Res 206:145-159.
16. Ivanova VN, Dobreva EP, Emanuilova EI. 1993. Purification and characterization of a thermostable alpha-amylase from Bacillus licheniformis. J Biotechnol 28:277-289.
17. Kandra L, Gyémánt G, Remenyik J, Hovánzski G, Lipták A. 2002. Action pattern and subsite mapping of Bacillus licheniformis α-amylase (BLA) with modified maltooligosaccharide substrates. FEBS Lett 518:79-82.
18. Kiser DL, Hagy RL. 1979. Estimation of dextrose equivalent value of starch hydrolysates from liquid chromatographic. In: Charalambous G, editor. Liquid chromatographic analysis of food and beverages, Vol. 2. New York: Academic Press, pp. 363-378.
19. Komolprasert V, Ofoly RY. 1991. Starch hydrolysis kinetics of Bacillus licheniformis α-amylase. J Chem Tech Biotechnol 51:209-223.
20. Kusunoki K, Kawakami K, Shiraishi F, Kato K, Kai M. 1982. A kinetic expression for hydrolysis of soluble starch by glucoamylase. Biotechnol Bioeng 24:347-354.
21. MacGregor EA, MacGregor AW. 1985. A model for the action of cereal alpha amylases on amylose. Carbohydr Res 142:223-236.
22. Marchal LM, van de Laar AMJ, Goetheer E, Schimmelpennink EB, Bergsma J, Beeftink HH, Tramper J. 1999. Effect of temperature on the saccharide composition obtained after α-amylolysis of starch. Biotechnol Bioeng 63:344-355.
23. Marchal LM, Zondervan J, Bergsma J, Beeftink HH, Tramper J. 2001. Monte Carlo simulation of the α-amylolysis of amylopectin potato starch. Part I: Modelling of the structure of amylopectin. Bioprocess Biosyst Eng 24:163-170.
24. Marchal LM, Ulijn RV, de Gooijer CD, Franke GTh, Tramper J. 2003. Monte Carlo simulation of the α-amylolysis of amylopectin potato starch. Part II: α-Amylolysis of amylopectin. Bioprocess Biosyst Eng 26:123-132.
25. Nakatani H. 1996. Monte Carlo simulation of multiple attack mechanism of ct-amylase. Biopolymers 39:665-669.
26. R enzyme. Biotechnol Bioeng 68:71-77.
27. Park JT, Rollings JE. 1994. Effects of substrate branching characteristics on kinetics of enzymatic depolymerization of mixed linear and branched polysaccharides: I. Amylose/amylopectin α-amylolysis. Biotechnol Bioeng 44:792-800.
28. Rodríguez VB, Alameda EJ, Gallegos JFM, Requena AR, López AIG. 2006a. Enzymatic hydrolysis of soluble starch with an α-amylase from Bacillus licheniformis. Biotechnol Prog 22:718-722.
29. Rodríguez VB, Alameda EJ, Gallegos JFM, Requena AR, López AIG. 2006b. Thermal deactivation of a commercial α-amylase from Bacillus licheniformis used in detergents. Biochem Eng J 27:299-304.
30. Rollings JE, Thompson RW. 1984. Kinetics of enzymatic starch liquefaction: Simulation of the high- molecular-weight product distribution. Biotechnol Bioeng 26:1475-1484.
31. Saito N. 1973. A thermophilic extracellular a-amylase from Bacillus licheniformis. Arch Biochem Biophys 155:290-298.
32. Thompson DB. 2000. On the non-random nature of amylopectin branching. Carbohydr Polym 43:223-239.
33. Tomazic SJ, Klibanov AM. 1988. Why is one Bacillus α-amylase more resistant against irreversible thermoinactivation than another? J Biol Chem 263:3092-3096.
34. Torgerson EM, Brewer LC, Thoma JA. 1979. Subsite mapping of enzymes. Use of subsite map to simulate complete time course of hydrolysis of a polymeric substrate. Arch Biochem Biophys 196: 13-22.
35. Violet M, Meunier JC. 1989. Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylase. Biochem J 263:665-670.
36. Wojciechowski PM, Koziol A, Noworyta A. 2001. Iteration model of starch hydrolysis by amylolytic enzymes. Biotechnol Bioeng 75:530-539.