TOMATO PEROXIDASE: PURIFICATION VIA HYDROPHOBIC CHROMATOGRAPHY

TOMATO PEROXIDASE: PURIFICATION VIA HYDROPHOBIC CHROMATOGRAPHY ABSTRACT With a large number of isoenzyme species and substrates, peroxidases have been difficult to purify to homogeneity. By including hydrophobic chromatography in the purification scheme, a homogeneous tomato fruit peroxidase isoenzyme was obtained. The isoenzyme had a clean spectrum in the visible region and a Rz (403 nm/280 nm) value of 2.36. It showed up as a single band in disc gel electrophoresis in basic and acidic buffers, in acetate strip electrophoresis, and in both tube and slab gel SDS electrophoresis. Molecular weight estimation of this tomato peroxidase was 43,000 ± 2,000 daltons. The pH optima were at 5.5 and 7.5 with guaiacol and pyrogallol as substrate, respectively. Kinetic studies showed that pyrogallol and hydrogen peroxide could provide substrate inhibition at 5 mM concentration. Hydrophobic chromatography may be useful for purification of other food enzymes similar to tomato peroxidase. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Science Wiley

TOMATO PEROXIDASE: PURIFICATION VIA HYDROPHOBIC CHROMATOGRAPHY

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Publisher
Wiley
Copyright
Copyright © 1980 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-1147
eISSN
1750-3841
D.O.I.
10.1111/j.1365-2621.1980.tb03870.x
Publisher site
See Article on Publisher Site

Abstract

ABSTRACT With a large number of isoenzyme species and substrates, peroxidases have been difficult to purify to homogeneity. By including hydrophobic chromatography in the purification scheme, a homogeneous tomato fruit peroxidase isoenzyme was obtained. The isoenzyme had a clean spectrum in the visible region and a Rz (403 nm/280 nm) value of 2.36. It showed up as a single band in disc gel electrophoresis in basic and acidic buffers, in acetate strip electrophoresis, and in both tube and slab gel SDS electrophoresis. Molecular weight estimation of this tomato peroxidase was 43,000 ± 2,000 daltons. The pH optima were at 5.5 and 7.5 with guaiacol and pyrogallol as substrate, respectively. Kinetic studies showed that pyrogallol and hydrogen peroxide could provide substrate inhibition at 5 mM concentration. Hydrophobic chromatography may be useful for purification of other food enzymes similar to tomato peroxidase.

Journal

Journal of Food ScienceWiley

Published: Jan 1, 1980

References

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