Abstract

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 glycosidated 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.