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Abstract:

The purpose of this study was to investigate the combined effects of trehalose and cations on the preservation of β-galactosidase in freeze-dried systems and their relationship to physical properties. Differential scanning calorimetry was employed to measure the glass transition temperature (T(g)) and the endothermal peak area, related to the amount of crystalline trehalose dihydrate present in the samples. In systems in which the trehalose matrix was humidified to conditions which allowed a high proportion of trehalose to crystallize, the enzyme was rapidly inactivated upon heating at 70°C. In these conditions the addition of CsCl, NaCl and particularly KCl or MgCl2, improved the enzyme stability with respect to that observed in matrices containing only trehalose. For a given moisture content, addition of salts produced very little change on the glass transition temperature; therefore the protective effect could not be attributed to a higher T(g) value. The crystallization of trehalose dihydrate in the humidified samples was delayed in the trehalose/salt systems (principally in the presence of Mg2+) and a parallel improvement of enzyme stability was observed. Copyright (C) 1999 Elsevier Science B.V.

Registro:

Documento: Artículo
Título:Combined effects of trehalose and cations on the thermal resistance of β-galactosidase in freeze-dried systems
Autor:Mazzobre, M.F.; Del Pilar Buera, M.
Filiación:Departamento de Industrias, Fac. Cie. Exact. Y Nat., Univ. B., Buenos Aires, Argentina
Palabras clave:β-Galactosidase; Cation; Crystallization; Enzyme stabilization; Freeze-drying; Trehalose; beta galactosidase; cation; cesium chloride; magnesium chloride; potassium chloride; sodium chloride; trehalose; article; crystallization; differential scanning calorimetry; enzyme stability; freeze drying; heat tolerance; moisture; priority journal; X ray diffraction; beta-Galactosidase; Calorimetry, Differential Scanning; Cesium; Chlorides; Crystallization; Enzyme Stability; Freeze Drying; Heat; Lactase; Magnesium Chloride; Potassium Chloride; Sodium Chloride; Trehalose
Año:1999
Volumen:1473
Número:2-3
Página de inicio:337
Página de fin:344
DOI: http://dx.doi.org/10.1016/S0304-4165(99)00207-X
Título revista:Biochimica et Biophysica Acta - General Subjects
Título revista abreviado:Biochim. Biophys. Acta Gen. Subj.
ISSN:03044165
CODEN:BBGSB
CAS:beta-Galactosidase, EC 3.2.1.23; cesium chloride, 7647-17-8; Cesium, 7440-46-2; Chlorides; Lactase, EC 3.2.1.108; Magnesium Chloride, 7786-30-3; Potassium Chloride, 7447-40-7; Sodium Chloride, 7647-14-5; Trehalose, 99-20-7
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03044165_v1473_n2-3_p337_Mazzobre

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Citas:

---------- APA ----------
Mazzobre, M.F. & Del Pilar Buera, M. (1999) . Combined effects of trehalose and cations on the thermal resistance of β-galactosidase in freeze-dried systems. Biochimica et Biophysica Acta - General Subjects, 1473(2-3), 337-344.
http://dx.doi.org/10.1016/S0304-4165(99)00207-X
---------- CHICAGO ----------
Mazzobre, M.F., Del Pilar Buera, M. "Combined effects of trehalose and cations on the thermal resistance of β-galactosidase in freeze-dried systems" . Biochimica et Biophysica Acta - General Subjects 1473, no. 2-3 (1999) : 337-344.
http://dx.doi.org/10.1016/S0304-4165(99)00207-X
---------- MLA ----------
Mazzobre, M.F., Del Pilar Buera, M. "Combined effects of trehalose and cations on the thermal resistance of β-galactosidase in freeze-dried systems" . Biochimica et Biophysica Acta - General Subjects, vol. 1473, no. 2-3, 1999, pp. 337-344.
http://dx.doi.org/10.1016/S0304-4165(99)00207-X
---------- VANCOUVER ----------
Mazzobre, M.F., Del Pilar Buera, M. Combined effects of trehalose and cations on the thermal resistance of β-galactosidase in freeze-dried systems. Biochim. Biophys. Acta Gen. Subj. 1999;1473(2-3):337-344.
http://dx.doi.org/10.1016/S0304-4165(99)00207-X