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

Authors: Yunel Perez, Reynaldo Villalonga

Addresses: Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, Autopista a Varadero Km 3 1/2, Matanzas, C.P. 44740, Cuba. ' Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, Autopista a Varadero Km 3 1/2, Matanzas, C.P. 44740, Cuba

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.

Keywords: lectin; α-amylase; mannan; enzyme immobilisation; enzyme stability; biocatalyst immobilisation.

DOI: 10.1504/IJBT.2004.005521

International Journal of Biotechnology, 2004 Vol.6 No.4, pp.385 - 392

Published online: 12 Oct 2004 *

Full-text access for editors Full-text access for subscribers Purchase this article Comment on this article