Keywords: lectin, &, #945, -amylase, mannan, enzyme immobilisation, enzyme stability, biocatalyst immobilisation
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.