Chemical glycosidation of trypsin with O-carboxymethyl-poly-beta-cyclodextrin: catalytic and stability properties.

The polysaccharide O-carboxymethyl-poly-beta-cyclodextrin was synthesized (molecular mass 13,000 Da, 40% carboxy groups) and attached to the surface of bovine pancreatic trypsin. The resulting neoglycoenzyme retained high proteolytic and esterolytic activity and contained approx. 1.

Metal-induced stabilization of trypsin modified with alpha-oxoglutaric acid.

Alpha-oxoglutaric acid was attached to trypsin via reductive alkylation with NaBH4 thereby introducing metal-chelating groups at the protein surface. The thermostability of the modified enzyme was increased by 6.5-13 degrees C and its resistance to autolytic degradation was improved 2- to 4-fold in 5 mM ZnCl2, MnCl2 or MgCl2.