Purification and immobilization of rabbit liver aldehyde oxidase

Aldehyde oxidase (E.C. 1.2.3.1) was isolated from rabbit liver and two potential bioaffinity ligands, i.e., 3‐aminocarbonyl‐1‐benzyl‐6‐methylpyridinium bromide and 3‐aminocarbonyl‐1‐benzyl‐4,6‐dimethylpyridinium chloride, were tested for their applicability in a purification procedure for this enzym...

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Bibliographic Details
Published in:Biotechnology and bioengineering 1985-04, Vol.27 (4), p.447-455
Main Authors: Angelino, Steven A. G. F., Müller, Franz, van der Plast, Henk C.
Format: Article
Language:English
Subjects:
aldehyde oxidase
Biochemie
Biochemistry
Biological and medical sciences
Biotechnology
Enzyme engineering
Fundamental and applied biological sciences. Psychology
immobilization
Immobilization of enzymes and other molecules
Immobilization techniques
Laboratorium voor Organische chemie
Laboratory for Organic Chemistry
liver
Methods. Procedures. Technologies
Organic Chemistry
Organische Chemie
rabbits
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Summary:Aldehyde oxidase (E.C. 1.2.3.1) was isolated from rabbit liver and two potential bioaffinity ligands, i.e., 3‐aminocarbonyl‐1‐benzyl‐6‐methylpyridinium bromide and 3‐aminocarbonyl‐1‐benzyl‐4,6‐dimethylpyridinium chloride, were tested for their applicability in a purification procedure for this enzyme. Various supports and different coupling methods were investigated for the immobilization of aldehyde oxidase. Adsorption to n‐hexyl‐ and n‐octylamine‐substituted Sepharose 4B and DEAE Sepharose 6B gave the best retention of aldehyde oxidase activity. The storage stability of free enzyme and enzyme immobilized to n‐octylamine‐substituted Sepharose 4B was studied in several buffers at pH 7.8 and 9.0. This showed that the stability of immobilized enzyme was much less than that of free enzyme. The apparent operational stability of the immobilized enzyme preparation, however, improved substantially compared to soluble enzyme, although the corresponding product yield is still very poor. Coimmobilization of catalase and/or superoxide dismutase provided no significant increase of the apparent operational stability and product yield. A positive effect on both parameters was found for aldehyde oxidase‐n‐alkylamine Sepharose 4B preparations by increasing the amount of enzyme adsorbed per unit weight of support, whereas the productivity of these preparations remained about constant.
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.260270409