D- AMINOACID OXIDASE BIO FUNCTIONALIZED PLATTAFORM: TOWARDS AND ENHANCED ENZYMATIC BIO ACTIVITY

ELISA HERRERA; JAVIER VALDEZ TAUBAS; CARLA E. GIACOMELLI

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2015 vol. 356 p. 679 - 679

he purpose of this work is to study the adsorption process and surface bio-activity of His-tagged d-amino acid oxidase (DAAO) from Rhodotorula gracilis (His6-RgDAAO) as the first step for the development of an electrochemical bio-functionalized platform. With such a purpose this work comprises: (a) the His6-RgDAAO bio-activity in solution determined by amperometry, (b) the adsorption mechanism of His6-RgDAAO on bare gold and carboxylated modified substrates in the absence (substrate/COO−) and presence of Ni(II) (substrate/COO− + Ni(II)) determined by reflectometry, and (c) the bio-activity of the His6-RgDAAO bio-functionalized platforms determined by amperometry. Comparing the adsorption behavior and bio-activity of His6-RgDAAO on these different solid substrates allows understanding the contribution of the diverse interactions responsible for the platform performance. His6-RgDAAO enzymatic performance in solution is highly improved when compared to the previously used pig