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Thermal Stability of Invertase in Reduced‐Moisture Amorphous Matrices in Relation to Glassy State and Trehalose Crystallization
Author(s) -
CARDONA SILVIA,
SCHEBOR CAROLINA,
BUERA MARÍA P.,
KAREL MARCUS,
CHIRIFE JORGE
Publication year - 1997
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1997.tb04378.x
Subject(s) - trehalose , invertase , glass transition , crystallization , thermal stability , moisture , maltodextrin , chemistry , amorphous solid , sucrose , materials science , sugar , chemical engineering , food science , chromatography , polymer , biochemistry , crystallography , spray drying , organic chemistry , engineering
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 (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.