Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization

The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvynilpyrrolidone (PVP; MW 40,000) and trehalose heated at 90 degrees C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass tr...

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Bibliographic Details
Published in:Journal of food science 1997-01, Vol.62 (1), p.105-112
Main Authors: Cardona, S. (Univ. de Buenos Aires, Buenos Aires, Argentina.), Schebor, C, Buera, M.P, Karel, M, Chirife, J
Format: Article
Language:English
Subjects:
Biological and medical sciences
CRYSTALLIZATION
Enzymes
Food engineering
Food industries
Food science
Fundamental and applied biological sciences. Psychology
General aspects
GLASS TRANSITION
HEAT
HEAT STABILITY
invertase
TEMPERATURE RESISTANCE
thermal inactivation
Thermodynamics
TREHALOSE
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Summary:The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvynilpyrrolidone (PVP; MW 40,000) and trehalose heated at 90 degrees C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass transition temperature (T(g)), but the enzyme was fairly stable in rubbery trehalose systems. However, at moisture contents which allowed trehalose crystallization rapid thermal inactivation of invertase was observed. Invertase inactivation in heated PVP, MD and trehalose systems of reduced-moisture could not be predicted on the basis of glass transition and this was particularly true for trehalose. Conditions which would allow collapse of the systems and crystallization of trehalose were fairly well predicted based on the estimated T(g) of model systems
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.1997.tb04378.x