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Electrochemical behavior of dye-linked L-proline dehydrogenase on glassy carbon electrode modified by multi-walled carbon nanotubes

Haitao Zheng^{1, 3}, Leyi Lin^{2, 3}, Yosuke Okezaki³ and Shin-ichiro Suye^3, *

(¹School of Environmental Science and Chemical Engineering, Tianjin Polytechnic University, Tianjin 300160, P.R. China; ²College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, P.R. China; ³Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, Fukui 910-8507, Japan.)

Purpose

As an essential component, L-proline is important for proper functioning of joints and tendons. It not only implicates some disorders in human body, but also a practical subject in food and pharmaceutical industries.

An electrochemical biosensor based on nanotube-modified electrode was constructed in this research.

Experimental and results

A glassy carbon electrode (GC) was modified by multi-walled carbon nanotubes (MWCNTs), and the cyclic voltammetric behaviors of the modified electrode were investigated. A redox pair of peaks was found clearly, which was owned to the oxygen-containing functional groups on the nanotube surface. Recombinant thermostable dye-linked L-proline dehydrogenase originally from hyperthermophilic archaeon (Thermococcus profundus) was further immobilized, and the modified electrode (GC/MWCNTS/L-proDH) exhibited electrocatalytic properties to L-proline compared to bare GC, GC/L-proDH and GC/MWCNTs electrode, which suggested that the presence of MWCNTs efficiently enhanced the electron transfer between the active center of L-proline dehydrogenase and the electrode surface.

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Enhanced surface functionality of soy globulins through attachment of carbohydrates and fatty acid chains Athanasia O. Matemu, Shigeru Katayama, and Soichiro Nakamura

(Department of Bioscience and Biotechnology, Shinshu University)

Objectives

Soy proteins have been widely used as a source of highly functional proteins in many formulated food products. For further industrial uses, it is desirable to improve their functional properties. Introduction of carbohydrates and fatty acid chains onto the protein molecular can alter its structure facilitating change in physic-chemical and functional properties. The aim of this study is to investigate the effects of glycosylation and lipophilization on the surface functionalities such as emulsion stability (ES), emulsifying ability index (EAI), and water or oil-binding capacities (WBC or OBC) of soy globulins.

Methods and Results

Glycinin (11S) or -conglycinin (7S) were covalently conjugated with carbohydrates such as xyloglucan (XG), chitin and chitosan oligosaccharide, through naturally occurring Maillard-type glycosylation at controlled temperature 60°C, relative humidity 65% and pH 7.0 for 7 days, or acylated with N-hydroxysuccinimide esters of fatty acids (6C-18C). As the result, the XG or chitin oligo conjugates showed almost 3.0-4.5 times improvement in ES but no significant difference in EAI. The EAI of 7S and 11S was increased by acylation with increasing chain length of fatty acid. The OBC of 11S was significantly increased by glycosylation with chitosan oligo but the OBC of 7S and the WBC of 7S and 11S were not improved. In contrast, the WBC and OBC of soy globulins were improved upon acylation, except for the WBC of 11S. In conclusion, it is revealed that covalent attachment of carbohydrates and fatty acid chains to soy globulin, 7S and 11S, resulted in enhancement of the surface functional properties.

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