Yunel Pérez

Improved pharmacological properties for superoxide dismutase modified with mannan

Mannan from Sacharomyces cerevisiae was activated by oxidation with NaIO4 (sodium m‐periodate) and further linked to SOD (superoxide dismutase) via reductive alkylation with NaBH4 (sodium borohydride). The gly‐cosidated enzyme contained an average of 1.2 mol of polysaccharide per mol of protein and retained 52% of its initial activity. The modified enzyme was 560‐fold more resistant to inactivation with H2O2 and acquired a lectin‐recognition capacity in respect of concanavalin A. The anti‐inflammatory activity of SOD was increased 2‐fold and its plasma half‐life time was prolonged from 4.8 min to 1.7 h after glycosylation with the polymer.

Biospecific immobilisation of mannan-modified α-amylase on Concanavalin A Sepharose

Bacillus subtilis α-amylase was chemically modified with yeast mannan, yielding a conjugate containing 1.2 mol of polysaccharide per mol of protein and retaining 60% of the original amylolytic activity. This neoglycoenzyme was immobilised on Concanavalin A Sepharose via a biospecific lectin-carbohydrate recognition mechanism. The immobilised biocatalyst retained high amylolytic activity and its optimum temperature was 10°C higher than the native enzyme. Thermal stability was increased by 12°C for α-amylase after glycosidation-immobilisation.