The influence of moisture content on the thermostability of Aspergillus oryzae α-amylase

Enzyme and Microbial Technology

Volumn 37, Issue 2, 2005, Pages 167-174

  Samborska, K ^a   Guiavarc'h, Y ^b   Van Loey, A ^b   Hendrickx, M ^b  

^a WARSAW UNIVERSITY OF LIFE SCIENCES   (Poland)

^b UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

Amylases; Aspergillus oryzae; Moisture content; Stability; Temperature

Indexed keywords

ACTIVATION ENERGY; MOISTURE; REACTION KINETICS; SALTS; SOLUTIONS; THERMODYNAMIC STABILITY; WATER;

Α-AMYLASE; ASPERGILLUS ORYZAE; BIPHASIC INACTIVATION PATTERN; MALTODEXTRIN;

ENZYMES;

AMYLASE; MALTODEXTRIN; SODIUM CHLORIDE; WATER;

ACCURACY; AQUEOUS SOLUTION; ARTICLE; ASPERGILLUS ORYZAE; ENERGY; FREEZE DRYING; KINETICS; MOISTURE; NONHUMAN; TEMPERATURE MEASUREMENT; THERMOSTABILITY;

ASPERGILLUS ORYZAE;

EID: 18944402729     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2004.06.017     Document Type: Article

References (24)

1. A.M. Klibanov Thermostabilisation of enzymes Adv Appl Microbiol 29 1983 1 29
2. C.Ó. Fágáin Understanding and increasing protein stability Biochim Biophys Acta 1252 1995 1 14
3. J. Fitter, R. Herrmann, T. Hauß, R.E. Lechner, and N.A. Dencher Dynamical properties of α-amylase in the folded and unfolded state: the role of thermal equilibrium fluctuations for conformational entropy and protein stabilisation Physica B 301 2001 1 7
4. M.R. Terebiznik, M.P. Buera, and A.M.R. Pilosof Thermal stability of dehydrated α-amylase in trehalose matrices in relation to its phase transitions Lebensm Wiss Technol 30 1997 513 518
5. W.Q. Sun, P. Davidson, and H.S.O. Chan Protein stability in the amorphous carbohydrate matrix: relevance to anhydrobiosis Biochim Biophys Acta 1425 1998 245 254
6. C. Colaco, S. Sen, M. Thangavelu, S. Pinder, and B. Roser Extraordinary stability of enzymes dried in trehalose: simplified molecular biology Biotechnology 10 1992 1007 1011
7. T.R. Noel, S.G. Ring, and P.A. Whittam Glass transition in low moisture food Trends Food Sci Technol 1 1990 62 67
8. S. Cardona, C. Schebor, M.P. Buera, M. Karel, and J. Chirife The thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state of trehalose J Food Sci 62 1997 105 112
9. M.F. Mazzobre, M.P. Buera, and J. Chirife Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization Lebensm Wiss Technol 30 1997 324 329
10. Y. Roos Glass transition-related physicochemical changes in foods Food Technol 49 10 1995 97 102
11. L. Greenspan Humidity fixed points of binary saturated aqueous solutions J Res Natl Bureau Stand-A, Phys Chem 81A 1 1977 89 96
12. Y.P. Guiavarc'h, V. Deli, A.M. Van Loey, and M.E. Hendrickx Development of an enzymic time temperature integrator for sterilization processes based on Bacillus licheniformis α-amylase at reduced moisture content J Food Sci 67 1 2002 285 291
13. J. Saraiva, J. Oliveira, A. Lemos, and M. Hendrickx Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength Int J Food Sci Technol 31 1996 223 231
14. A.C. Ling, and D.B. Lund Determining kinetic parameters for isothermal inactivation of heat resistant and heat labile isozymes from thermal destruction curves J Food Sci 43 1978 1307 1310
15. A. Van Loey, A. Arthawan, M. Hendrickx, T. Haentjens, and P. Tobback The development and use of an α-amylase-based time-temperature integrator to evaluate in-pack pasteurisation processes Lebensm Wiss Technol 30 1997 94 100
16. W.L. Claeys, L.R. Ludikhuyze, A.M. Loey, and M.E. Hendrickx Inactivation kinetics of alkaline phosphatase and lactoperoxidase, and denaturation kinetics of β-lactoglobulin in raw milk under isothermal and dynamic temperature conditions J Diary Res 68 2001 95 107
17. M.L. Johnson Why, when, and how biochemists should use least squares Anal Biochem 206 1992 215 225
18. J. Saraiva, S. De Cordt, M. Hendrickx, J. Oliveira, and P. Tobback Inactivation of α-amylase from Bacillus amyloliquefaciens at low moisture contents W.J.J. Van den Tweel A. Harder R.M. Buitelaar Stability and stabilisation of enzymes 1992 Elsevier Maastricht 459 466
19. J. Saraiva, J.C. Oliveira, M. Hendrickx, FA.R. Oliveira, and P. Tobback Analysis of the inactivation kinetics of freeze dried α-amylase form Bacillus amyloliquefaciens at different moisture contents Lebensm Wiss Technol 29 1996 260 266
20. T.H. Haentjens, A.M. Van Loey, M.E. Hendrickx, and P.P. Tobback The use of α-amylase at reduced moisture content to develop time temperature integrators for sterilization processes Lebensm Wiss Technol 31 1998 467 472
21. Y. Ross, and M. Karel Phase transitions of mixtures of amorphous polysaccharides and sugars Biotechnol Prog 7 1991 49 53
22. g may contribute to the stability of biological systems Biophys J 79 2000 1119 1128
23. G. Meerdink, and K. Van't Riet Inactivation of a thermostable α-amylase during drying J Food Eng 14 1991 83 102
24. C. Weemaes, S. De Cordt, K. Goossens, L. Ludikhuyze, M. Hendrickx, and K. Heremans High pressure, thermal and combined pressure-temperature stabilities of α-amylase from Bacillus species Biotechol Bioeng 50 1 1993 49 56