Thermal analysis combined with other experimental techniques has shown how the activity and stability of lipase from Candida cylindracea are related to protein hydration and how the water is bonded with varying strength and energy to the enzyme surface. It was observed by DSC (differential scanning calorimetry) that the thermal denatulation is the result of two simultaneous events, dehydration and unfolding, and that this endothermic process becomes reversible at temperatures less than T-m (T-m = 86 degrees C, maximum peak temperature) and irreversible at temperatures higher than T-m leading to a partially or totally deactivated physico-chemical aggregate.
Thermal stability and activity of Candida cylindracea lipase / Gentili, Alessandra; Curini, Roberta; Cernia, Enrico; D'Ascenzo, Giuseppe. - In: JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC. - ISSN 1381-1177. - STAMPA. - 3:1-4(1997), pp. 43-49. (Intervento presentato al convegno International Workshop on Lipases in the Biocatalysis tenutosi a ROME, ITALY nel APR 11-13, 1996) [10.1016/s1381-1177(96)00042-2].
Thermal stability and activity of Candida cylindracea lipase
GENTILI, Alessandra;CURINI, Roberta;CERNIA, Enrico;D'ASCENZO, Giuseppe
1997
Abstract
Thermal analysis combined with other experimental techniques has shown how the activity and stability of lipase from Candida cylindracea are related to protein hydration and how the water is bonded with varying strength and energy to the enzyme surface. It was observed by DSC (differential scanning calorimetry) that the thermal denatulation is the result of two simultaneous events, dehydration and unfolding, and that this endothermic process becomes reversible at temperatures less than T-m (T-m = 86 degrees C, maximum peak temperature) and irreversible at temperatures higher than T-m leading to a partially or totally deactivated physico-chemical aggregate.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
