Artículo
Properties of soluble α-chymotrypsin in neat glycerol and water
Fecha de publicación:
12/2000
Editorial:
Elsevier Science Inc
Revista:
Enzyme and Microbial Technology
ISSN:
0141-0229
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
UV scanning of a-chymotrypsin dissolved in neat glycerol and water showed no significant differences in its spectra at pH 7.8. Fluorescence scanning revealed a strong dependence on pH values (between 5.9 to 10.5) of the maximum wavelength emission in water and no pH-dependence in 99% glycerol supplemented with 1% of appropriate buffers. The profile of a-chymotrypsin activity dissolved in water-glycerol mixtures with phenyl acetate as substrate displayed two maximum: highest peak was found at 100% water, and the second one was observed in 99% glycerol concentration with about 40% of the relative activity. Optimum pH of the soluble a-chymotrypsin in glycerol showed a displacement of 1 pH/U towards the alkaline side compared to water at pH 8.0. Kinetic and thermodynamic analysis using kinetic measurements of the thermal stability of a-chymotrypsin showed a higher inactivation rate in neat glycerol as compared to water in 30 to 45°C range, however, when temperature increases enzyme stability in glycerol is better than water. Thermostability of trypsin and a-chymotrypsin dissolved in glycerol at 100°C showed a half reaction time of approximately 7 and 20 h, respectively, and less than 1 minute in aqueous buffer for both enzymes.
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Articulos(PROIMI)
Articulos de PLANTA PILOTO DE PROC.IND.MICROBIOLOGICOS (I)
Articulos de PLANTA PILOTO DE PROC.IND.MICROBIOLOGICOS (I)
Citación
Castro, Guillermo Raul; Properties of soluble α-chymotrypsin in neat glycerol and water; Elsevier Science Inc; Enzyme and Microbial Technology; 27; 1-2; 12-2000; 143-150
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