Isolation, purification and properties of the peroxidase from the hull ofGlycine max var HH2
| Autor: | Wen-Miao Zhu, Jing Fang, Pei-Ji Gao, Wen Liu |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
chemistry.chemical_classification
Gel electrophoresis Nutrition and Dietetics Chromatography biology Size-exclusion chromatography Enzyme assay Gel permeation chromatography Isoelectric point Enzyme chemistry Affinity chromatography biology.protein Agronomy and Crop Science Food Science Biotechnology Peroxidase |
| Zdroj: | Journal of the Science of Food and Agriculture. 79:779-785 |
| ISSN: | 1097-0010 0022-5142 |
| Popis: | Soybean hull peroxidase (EC 1.11.1.7), an acidic peroxidase isolated from soybean (Glycine max var HH2) hulls was purified to electrophoretic homogeneity by a combination of ammonium sulphate fractionation, DEAE-Sephadex A-50 chromatography, concanavalin A-Sepharose 4B affinity chromatography and Bio-Gel P-60 gel filtration. The specific activity of purified peroxidase was about 57-fold higher than that of crude extract. The yield was about 16.4%. The molecular weight of the enzyme was estimated to be 38 000 by SDS-polyacrylamide gel electrophoresis. The peroxidase was a glycoprotein containing about 18.7% carbohydrate, approximately one-quarter of which was shown to be glucosamine residues. It was found to have an isoelectric point of 3.9. The enzyme was most active at pH 4.6 and 45°C, and was stable in the pH range 2.5–11.5. The enzyme could tolerate heating for 10 min at 75°C without being inactivated, and at 85°C, it took 40 min to inactivate the enzyme 50%, confirming that the peroxidase was a novel thermostable enzyme. Fe 2+, Fe3+, Sn2+, CN − and N3− inhibited enzyme activity, while Hg2+, Ag+, Pb 2+, Cr3+, EDTA and SDS were not significantly inhibitory. © 1999 Society of Chemical Industry |
| Databáze: | OpenAIRE |
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