Thiophilic interaction chromatography of sweet potato β-amylase

The affinity of sweet potato β-amylase toward two kinds of thiophilic adsorbents [the so-called thiophilic or T-gel and 3-(2-pyridylsulphido)-2- hydroxypropylagarose or PyS-gel] was demonstrated. Enzyme adsorption on both gels was promoted by antichaotropic salts. Lower salt requirements and higher...

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Bibliographic Details
Published in:Journal of Chromatography A 1992-06, Vol.604 (1), p.103-107
Main Authors: Franco-Fraguas, Laura, Batista-Viera, Francisco
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
beta-amylase
Biological and medical sciences
chromatography
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
purification
sweet potatoes
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Summary:The affinity of sweet potato β-amylase toward two kinds of thiophilic adsorbents [the so-called thiophilic or T-gel and 3-(2-pyridylsulphido)-2- hydroxypropylagarose or PyS-gel] was demonstrated. Enzyme adsorption on both gels was promoted by antichaotropic salts. Lower salt requirements and higher protein recoveries were observed for the PyS gel, even though its ligand concentration was half that of T-gel. For the former gel, the effectiveness series for sulphates was Na 2SO 4 > (NH 4) 2SO 4 > K 2SO 4 > MgSO 4. Based on the thiophilic character exhibited by the pure sweet potato β-amylase and the reversibility of the salt effects, a new method for its purification from crude extracts was developed.
ISSN:0021-9673
DOI:10.1016/0021-9673(92)85534-Z