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Isolation, purification and properties of the peroxidase from the hull ofGlycine max var HH2

✍ Scribed by Liu, Wen; Fang, Jing; Zhu, Wen-Miao; Gao, Pei-Ji

Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
177 KB
Volume
79
Category
Article
ISSN
0022-5142

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✦ Synopsis

Soybean hull peroxidase (EC 1.11.1.7), an acidic peroxidase isolated from soybean (Glycine max var HH2) hulls was puriüed 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 ültration. The speciüc activity of puriüed 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 45ÄC, and was stable in the pH range 2.5-11.5. The enzyme could tolerate heating for 10 min at 75ÄC without being inactivated, and at 85ÄC, it took 40 min to inactivate the enzyme 50% , conürming that the peroxidase was a novel thermostable enzyme. Fe2', Fe3', Sn2', CN-and N 3 inhibited enzyme activity, while Hg2', Ag', Pb2', Cr3', EDTA and SDS were not signiücantly inhibitory.

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