Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The thermal stability of enzymes lactase and invertase in dried, amorphous matrices of sugars (trehalose, maltose, lactose, sucrose, raffinose) and some other selected systems (casein, PVP, milk) was studied. The glass transition temperature (Tg) was limited as a threshold parameter for predicting enzyme inactivation because (a) enzyme inactivation was observed in glassy matrices, (b) a specific effect of enzyme stabilization by certain matrices particularly trehalose was observed, and (c) enzyme stability appeared to depend on heating temperature (T) "per se" rather than (T-Tg). For these reasons, a protective mechanism by sugars related to the maintenance of the tertiary structure of the enzyme was favored. A rapid loss of enzyme (lactase) activity was observed in heated sucrose systems at T > Tg, and this was attributed to sucrose crystallization since it is known that upon crystallization the protective effect of sugars is lost. Thus, the stabilizing effect could be indirectly affected by the Tg of the matrix, since crystallization of sugars only occurs above Tg. Trehalose model systems (with added invertase) showed an exceptional stability toward "darkening" (e.g., non-enzymatic browning) when heated in the dried state to elevated temperatures and for long periods of time.
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PMID:Glassy state and thermal inactivation of invertase and lactase in dried amorphous matrices. 941 44

Research continues to differentiate the impact of water activity (a(W)) and the glass transition temperature (T(g)) on chemical reactions. Invertase with and without sucrose was incorporated into low and high molecular weight poly(vinylpyrrolidone) model systems (PVP-LMW and PVP-K30, respectively). Invertase activity and sucrose hydrolysis were monitored during storage at a(W) = 0.32-0.75 and 30 degrees C. Pseudo-first-order rate constants for activity loss in PVP-K30 were not different, regardless of the system being glassy or rubbery. In PVP-LMW, invertase stability decreased with increasing a(W). An a(W) > 0.62 was required for sucrose hydrolysis to occur in PVP-LMW. PVP molecular weight appeared to affect invertase stability and reactivity. No dramatic change around T(g) was found in either invertase stability or sucrose hydrolysis, suggesting that T(g)-dictated mobility has a minimal effect on these reactions in amorphous solids.
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PMID:Invertase storage stability and sucrose hydrolysis in solids as affected by water activity and glass transition. 1056 24