title: Promotion and suppression effects of cationic polymer ε-poly-L-lysine on the glucose oxidase reaction with ferrocene derivatives as oxidants with different charges.
abstract: The effects of the cationic polymer ε-poly-L-lysine (εPL) on the enzymatic reaction rate of glucose oxidase (GOD) with ferrocene derivatives having different ionic charges have been investigated by measuring the ferrocene derivative-mediated catalytic current of oxidation by GOD. When negatively charged ferrocenes were used, the bioelectrocatalytic current, which is related to the enzymatic reaction rate, was increased by the addition of εPL. On the other hand, the reaction rates with positively charged ferrocenes were decreased by εPL. These promotion and suppression effects of εPL were remarkable at a certain pH range, where εPL and GOD were charged positively and negatively, respectively. Within this range, the polycationic εPL would be adsorbed onto the GOD surface to enhance the electrostatic interactions of the enzyme with negatively charged substrates, and repulsion with positively charged ones. These findings should be important for practical applications of enzymes.
authors: Faculty of Biotechnology, Fukui Prefectural University.
authors: Kohei
authors: K
authors: Uematsu
authors: Yuto
authors: Y
authors: Minami
authors: Shu
authors: S
authors: Taira
authors: Hajime
authors: H
authors: Katano
mesh_terms: D001234:Aspergillus niger / Q000201:enzymology; D055162:Biocatalysis; D004553:Electric Conductivity; D004563:Electrochemistry; D005296:Ferrous Compounds / Q000737:chemistry*; D005949:Glucose Oxidase / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D000075163:Metallocenes; D016877:Oxidants / Q000737:chemistry*; D011107:Polylysine / Q000737:chemistry*; D011485:Protein Binding; D055672:Static Electricity
chemical_list: D005296:Ferrous Compounds; D000075163:Metallocenes; D016877:Oxidants; D011107:Polylysine; D005949:Glucose Oxidase; C004998:ferrocene