Thermal Stability of Invertase in Reduced-Moisture Amorphous Matrices in Relation to Glassy State and Trehalose Crystallization |
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| Authors: | SILVIA CARDONA,CAROLINA SCHEBOR,MARÍ A P. BUERA,MARCUS KAREL,JORGE CHIRIFE |
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| Affiliation: | Authors Cardona, Schebor, Buera and Chirife are with the Depto. de Industrias, Facultad de Ciencias Exactas y Naturales, Univ. de Buenos Aires, (1428) Buenos Aires, Argentina. Author Schebor is a CONICET Research Fellow and author Buera is a member of CONICET, Argentina. Author Karel is with the Dept. of Food Science and Center for Advanced Food Technology, Rutgers Univ., New Brunswick, NJ 08903. Direct inquiries to Dr. Jorge Chirife. |
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| Abstract: | The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvynilpyrrolidone (PVP; MW 40,000) and trehalose heated at 90°C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass transition temperature (Tg), 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 Tg of model systems. |
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| Keywords: | invertase thermal inactivation glass transition trehalose crystallization |
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