Beneficial Effect of Sugar Osmolytes on the Refolding of Guanidine Hydrochloride-Denatured Trehalose-6-phosphate Hydrolase from Bacillus licheniformis

Comparative analysis of chemical and thermal denatured 13-lactoglobu1in A in the presence of sugar osmolytes

Chemical denaturation and thermal denaturation of13-lactoglobulin A (f3 — lgA) in the absenceand presence of various concentrations sugar osmolytes and polyols were measured bymonitoring changes in the absorption coefficients at pH 2.0. It has been observed that AGD°(H20), (Gibbs free energy change in absence of denaturant at 25 °C) of f3-1gA in the presenceof 10% (w/v) Trehalose, Sucrose, Sorb...

Does recovery in the spectral characteristics of GdnHCl-denatured Bacillus licheniformis α-amylase due to added calcium point towards protein stabilization?

Treatment of Bacillus licheniformis α-amylase (BLA) with guanidine hydrochloride (GdnHCl) produced both denatured and aggregated forms of the enzyme as studied by circular dichroism, fluorescence, UV difference spectroscopy, size exclusion chromatography (SEC), and enzymatic activity. The presence of CaCl(2) in the incubation mixture produced significant recovery in spectral signals, being comp...

Effective Parameters on the Partition Coefficient of Guanidine Hydrochloride in the Poly (Ethylene Glycol) +Phosphate +Water System at 298.15 K

Optimizing refolding condition for recombinant tissue plasminogen activator

Low molecular size additives such as L-arginine and the redox compounds have been used both in the culturemedium and in vitro refolding to increase recombinant proteins production. Additives increase proteinrefolding and yield of active proteins by suppressing aggregate formation or enhancing refolding process.In this work, a comparative study was performed on refolding of rec...

REASSOCIATION AND REACTIVATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM STREPTOMYCES AUREOFACIENS AFTER DENATURATION BY 6 M UREA

Glucose 6-phosphate dehydrogenase (G6PD) from Streptomyces aureofaciens was purified and denatured in 6 M urea. Denaturation led to complete dissociation of the enzyme into its inactive monomers, 98% loss of the enzyme activity, about 30% decrease in the protein fluorescence and a 10 nm red shift in the emission maximum. Dilution of urea-denatured enzyme resulted in regaining of the enzyme acti...