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Abstract:

The thermal stability of enzymes lactase and invertase in dried, amorphous matrices of sugars (trehalose, malrose, lactose, sucrose, raffinose) and some other selected systems (casein, PVP, milk) was studied. The glass transition temperature (T(g)) 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 - T(g)). 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 > T(g), 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 T(g) of the matrix, since crystallization of sugars only occurs above T(g). Trehalose model systems (with added invertase) showed an exceptional stability toward 'darkening' (e.g., nonenzymatic browning) when heated in the dried state to elevated temperatures and for long periods of time. 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.

Registro:

Documento: Artículo
Título:Glassy state and thermal inactivation of invertase and lactase in dried amorphous matrices
Autor:Schebor, C.; Burin, L.; Buera, M.P.; Aguilera, J.M.; Chirife, J.
Ciudad:New York, NY, United States
Filiación:Departamento de Industrias, Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, 1428 Buenos Aires, Argentina
Depto. de Ing. Quim. y Bioprocesos, Facultad de Ingeniería, Pont. Univ. Católica de Chile, Santiago, Chile
Palabras clave:Amorphous materials; Casein; Catalyst activity; Crystallization; Enzyme immobilization; Glass transition; Maltose; Sugar (sucrose); Thermal effects; Thermodynamic stability; Invertase; Lactase; Lactose; Raffinose; Trehalose; Enzymes; beta fructofuranosidase; beta galactosidase; casein; disaccharide; glycosidase; lactase; povidone; sucrose; trehalose; animal; article; chemistry; crystallization; desiccation; enzyme stability; heat; kinetics; metabolism; milk; physical chemistry; Animals; beta-Fructofuranosidase; beta-Galactosidase; Caseins; Chemistry, Physical; Crystallization; Desiccation; Disaccharides; Enzyme Stability; Glycoside Hydrolases; Heat; Kinetics; Lactase; Milk; Povidone; Sucrose; Trehalose; Animalia
Año:1997
Volumen:13
Número:6
Página de inicio:857
Página de fin:863
DOI: http://dx.doi.org/10.1021/bp970093x
Título revista:Biotechnology Progress
Título revista abreviado:Biotechnol. Prog.
ISSN:87567938
CODEN:BIPRE
CAS:beta-Fructofuranosidase, EC 3.2.1.26; beta-Galactosidase, EC 3.2.1.23; Caseins; Disaccharides; Glycoside Hydrolases, EC 3.2.1.-; Lactase, EC 3.2.1.108; Povidone, 9003-39-8; Sucrose, 57-50-1; Trehalose, 99-20-7
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_87567938_v13_n6_p857_Schebor

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Citas:

---------- APA ----------
Schebor, C., Burin, L., Buera, M.P., Aguilera, J.M. & Chirife, J. (1997) . Glassy state and thermal inactivation of invertase and lactase in dried amorphous matrices. Biotechnology Progress, 13(6), 857-863.
http://dx.doi.org/10.1021/bp970093x
---------- CHICAGO ----------
Schebor, C., Burin, L., Buera, M.P., Aguilera, J.M., Chirife, J. "Glassy state and thermal inactivation of invertase and lactase in dried amorphous matrices" . Biotechnology Progress 13, no. 6 (1997) : 857-863.
http://dx.doi.org/10.1021/bp970093x
---------- MLA ----------
Schebor, C., Burin, L., Buera, M.P., Aguilera, J.M., Chirife, J. "Glassy state and thermal inactivation of invertase and lactase in dried amorphous matrices" . Biotechnology Progress, vol. 13, no. 6, 1997, pp. 857-863.
http://dx.doi.org/10.1021/bp970093x
---------- VANCOUVER ----------
Schebor, C., Burin, L., Buera, M.P., Aguilera, J.M., Chirife, J. Glassy state and thermal inactivation of invertase and lactase in dried amorphous matrices. Biotechnol. Prog. 1997;13(6):857-863.
http://dx.doi.org/10.1021/bp970093x