Kulthida KaewprapanPatoomratana TuchindaEmmanuelle MarieAlain DurandPranee InprakhonMahidol UniversityLaboratoire de Chimie Physique Macromoleculaire2018-08-242018-08-242007-07-02Journal of Molecular Catalysis B: Enzymatic. Vol.47, No.3-4 (2007), 135-142138111772-s2.0-34447250841https://repository.li.mahidol.ac.th/handle/20.500.14594/24166The application of enzymatic catalysis for the synthesis of polysaccharide-based surfactants was investigated. The polysaccharide dextran, a neutral bacterial polysaccharide consisting of α-1,6 linked glucose units, was chemically modified by the attachment of hydrophobic groups through a transesterification reaction with a vinyl decanoate. A screening of commercially available lipases and protease for the synthesis of amphiphilic polysaccharides in DMSO suggested that lipase AY from Candida rugosa modified dextran T-40 with vinyl decanoate at the highest conversion. A pH-adjustment in a phosphate buffer at pH 7.5 prior to use is crucial to make this enzyme active in DMSO. The effect of enzyme concentration and mole ratio of fatty ester to dextran T-40 on the conversion and the rate of reaction were studied. Finally, investigation of the kinetics and regioselectivity of lipase AY-catalyzed modification offer a possibility to regulate the position and the extent of hydrophobic group attached to dextran. These two properties are fundamental for controlling the physico-chemical properties of the final polymeric surfactants. © 2007 Elsevier B.V. All rights reserved.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyChemical EngineeringArticleSCOPUS10.1016/j.molcatb.2007.04.006