Isolation and partial characterization of thermostable isoperoxidases from potato (Solanum tuberosum L.) tuber sprouts.
Peroxidases (POD; EC 1.11.1.7) can cross-link cell wall polymers and may have an impact on the final textural quality of potato tubers. Because heat treatments are important during processing, the thermal properties of isoPODs from soluble and ionically and covalently bound fractions were studied from both potato tubers and sprouts. For both tissues, the ionically bound fraction was the most thermostable; approximately 20% of POD activity remained after a heat treatment of 10 min at 90 degrees C (for sprouts). The temperature profile of the ionically bound sprout fraction appeared to be nonlinear and suggested the presence of a very thermostable POD, which still showed activity after a heat treatment at 100 degrees C. Visualization by using isoelectric focusing confirmed the occurrence of a thermostable isoPOD with an IEP of 9.5, which displayed regeneration of activity after heat inactivation. This cationic POD was further purified by chromatography techniques, and by SDS-PAGE its molecular mass was estimated at 38 kDa.
Boucoiran
C F
CF
Department of Agrofibres and Cellulose, Agrotechnological Research Institute (ATO-DLO), P.O. Box 17, 6700 AA Wageningen, The Netherlands. c.f.s.boucoiran@plant.wag-ur.nl
Kijne
J W
JW
Recourt
K
K
D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification*; D010544:Peroxidases / Q000737:chemistry* / Q000302:isolation & purification*; D018520:Plant Shoots; D011198:Solanum tuberosum / Q000201:enzymology*; D013696:Temperature
D007527:Isoenzymes; D010544:Peroxidases