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- W2000947445 abstract "The polysaccharide O ‐carboxymethyl‐poly‐β‐cyclodextrin was synthesized (molecular mass 13000 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. 1.0 mol of polymer/mol of enzyme. The optimum temperature for trypsin activity was increased by 10°C after this transformation. Thermostability of the polymer–enzyme complex was increased by about 14°C over 10 min incubation. The conjugate was also more resistant to thermal inactivation at different temperatures, ranging from 45 to 60°C, demonstrating the influence of supramolecular and polymer–protein electrostatic interactions on trypsin thermostabilization. Additionally, the conjugate was 36‐fold more resistant to the action of the anionic surfactant SDS. This modification also protected the enzyme from autolysis at alkaline pH." @default.
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- W2000947445 date "2005-06-01" @default.
- W2000947445 modified "2023-10-13" @default.
- W2000947445 title "Chemical glycosidation of trypsin with O-carboxymethyl-poly-β-cyclodextrin: catalytic and stability properties" @default.
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- W2000947445 doi "https://doi.org/10.1042/ba20040115" @default.
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