Trehalose at 10-30% (w/w) greatly stabilized bovine serum albumin (BSA) against thermal denaturation. The highest stabilization was reached in 30% trehalose at 65 degrees C, when the protein's half life was increased from 72 to 335 min. A kinetic analysis based on the Lumry-Eyring mechanism of inactivation showed that BSA denaturation can be described by a first-order rate expression with an apparent activation energy ranging from 238.1 to 246.4 kJ mol(-1).
Effect of Trehalose on Thermal Stability of Bovine Serum Albumin / Lavecchia, Roberto; Zuorro, Antonio. - In: CHEMISTRY LETTERS. - ISSN 0366-7022. - STAMPA. - 39:1(2010), pp. 38-39. [10.1246/cl.2010.38]
Effect of Trehalose on Thermal Stability of Bovine Serum Albumin
LAVECCHIA, Roberto;ZUORRO, ANTONIO
2010
Abstract
Trehalose at 10-30% (w/w) greatly stabilized bovine serum albumin (BSA) against thermal denaturation. The highest stabilization was reached in 30% trehalose at 65 degrees C, when the protein's half life was increased from 72 to 335 min. A kinetic analysis based on the Lumry-Eyring mechanism of inactivation showed that BSA denaturation can be described by a first-order rate expression with an apparent activation energy ranging from 238.1 to 246.4 kJ mol(-1).I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
