Increased thermostability and phenol removal efficiency by chemical modified horseradish peroxidase

Horseradish peroxidase was modified by phthalic anhydride and glucosamine hydrochloride. The thermostabilities and removal efficiencies of phenolics by native and modified HRP were assayed. The chemical modification of horseradish peroxidase increased their thermostability (about 10- and 9-fold, res...

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Bibliographic Details
Published inJournal of molecular catalysis. B, Enzymatic Vol. 18; no. 4; pp. 225 - 232
Main Authors Liu, Jian-Zhong, Song, Hai-Yan, Weng, Li-Ping, Ji, Liang-Nian
Format Journal Article
LanguageEnglish
Published Elsevier B.V 23.10.2002
Subjects
Chemical modification
Horseradish peroxidase
Phenol removal
Thermostability
Thermostability
Horseradish peroxidase
Chemical modification
Phenol removal
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Summary:Horseradish peroxidase was modified by phthalic anhydride and glucosamine hydrochloride. The thermostabilities and removal efficiencies of phenolics by native and modified HRP were assayed. The chemical modification of horseradish peroxidase increased their thermostability (about 10- and 9-fold, respectively) and in turn also increased the removal efficiency of phenolics. The quantitative relationships between removal efficiency of phenol and reaction conditions were also investigated using modified enzyme. The optimum pH for phenol removal is 9.0 for both native and modified forms of the enzyme. Both modified enzyme could suffer from higher temperature than native enzyme in phenol removal reaction. The optimum molar ratio of hydrogen peroxide to phenol was 2.0. The phthalic anhydride modified enzyme required lower dose of enzyme than native horseradish peroxidase to obtain the same removal efficiency. Both modified horseradish peroxidase show greater affinity and specificity of phenol.
ISSN:1381-1177
1873-3158
DOI:10.1016/S1381-1177(02)00100-5