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1.
Nanoscale Res Lett ; 9(1): 281, 2014.
Artículo en Inglés | MEDLINE | ID: mdl-24948898

RESUMEN

In this work, we have demonstrated that amorphous ZnO nanobranches (a-ZnO NBs) could spontaneously react from the crystalline ZnO NWs (c-ZnO NWs) at specific humid environment. The spontaneous reaction mechanism and result can be analyzed by humidity controlling and optical microscope (OM)/scanning electron microscope (SEM)/Kelvin probe force microscopy (KPFM)/transmission electron microscopy (TEM) system. We can make the c-ZnO NWs spontaneous reaction happen at different humid environments and suppress the a-ZnO NBs spontaneous reaction by oxygen/hydrogen plasma surface passivation. The hydrogen plasma surface treatment also can improve the UV sensing sensitivity more than twofold. This work provides the mechanism and methods of the a-ZnO NBs spontaneous growth and offers the passivation treatment for strengthening and enhancing ZnO-based nanodevice application in humid environment and UV light detection, respectively.

2.
Anal Chem ; 81(7): 2737-44, 2009 Apr 01.
Artículo en Inglés | MEDLINE | ID: mdl-19267482

RESUMEN

Analysis of immobilized enzyme in situ is a crucial step to embed an enzyme onto the planar technology of standard integrated circuit (IC) and microelectromechanical systems (MEMS) for a bioreactor or enzyme-coupled biosensor. A surface reaction limited model, based on a systematized and standardized approach, mathematically derived from mass transfer dynamics and the Michaelis-Menten equation for the measuring the apparent K*(m) (Michaelis-Menten constant) and V*(max) (maximum reaction rate per unit surface area of catalyst) of an immobilized enzyme on a planar surface was developed. The derived equations for the kinetic model were simulated and experimentally confirmed. A platform of a microflow bioreactor with a one-sided planar catalytic surface that contained immobilized enzyme was constructed. The microfluidic bioreactor was designed to possess a channel height less than that of the diffusion layer thickness in a semi-infinite diffusion process, and K*(m) and V*(max) of rat phenol sulfotransferase (PST) immobilized on the silicon oxide surface were successfully determined in situ. Variation in kinetic constants and the possible differences in performance between free and immobilized PST are discussed.


Asunto(s)
Enzimas Inmovilizadas/análisis , Enzimas Inmovilizadas/química , Modelos Químicos , Animales , Arilsulfotransferasa/análisis , Arilsulfotransferasa/química , Arilsulfotransferasa/metabolismo , Reactores Biológicos , Estabilidad de Enzimas , Enzimas Inmovilizadas/metabolismo , Cinética , Modelos Moleculares , Conformación Proteica , Ratas , Análisis de Regresión , Silicio/química , Silicio/metabolismo , Propiedades de Superficie
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