Biospecific immobilisation of mannan-modified α-amylase on Concanavalin A Sepharose
by Yunel Perez, Reynaldo Villalonga
International Journal of Biotechnology (IJBT), Vol. 6, No. 4, 2004

Abstract: 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.

Online publication date: Tue, 12-Oct-2004

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