Dextransucrase-catalyzed elongation of polysaccharide brushes with immobilized mono-/di-saccharides as acceptors.
A quartz crystal microbalance (QCM) was used to monitor dextransucrase (DSase)-catalyzed polysaccharide elongation on the glucose-/maltose-ended self-assembly monolayer (SAM) surfaces. Kinetic parameters of the enzymatic elongation indicate that maltose is a promising substrate acceptor for DSase.
MOE Key Laboratory of Macromolecular Synthesis and Functionalization, Department of Polymer Science and Engineering, Zhejiang University, Hangzhou 310027, China. xuzk@zju.edu.cn.
Yan
Y
Fang
Jian
J
Wu
Zhi-Kang
ZK
Xu
D055162:Biocatalysis; D005964:Glucosyltransferases / Q000378:metabolism*; D007103:Immobilization; D007700:Kinetics; D007934:Leuconostoc / Q000201:enzymology; D008320:Maltose / Q000737:chemistry / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism*; D058525:Quartz Crystal Microbalance Techniques; D013379:Substrate Specificity; D013499:Surface Properties
D011134:Polysaccharides; D008320:Maltose; D005964:Glucosyltransferases; C020025:dextransucrase