Res. Agr. Eng., 2008, 54(4):170-175 | DOI: 10.17221/703-RAE
Effect of heat treatment on re-solubility of potato proteins isolated from industrial potato fruit juice
- Biotechnological centre, Department of Plant Production, Faculty of Agriculture, University of South Bohemia, České Budějovice, Czech Republic
The contribution deals with thermal stability and re-solubility of potato tuber proteins isolated by ethanol precipitation from industrial potato fruit juice. The protein isolate was exposed to the temperatures ranging from 25°C to 70°C. Patatin, the tuber protein with a high nutritious value, was detected by SDS-PAGE in the region of 39-43 kDa. Patatin was evaluated as thermal sensitive - temperatures above 30°C caused its strong insolubility. Potato protease inhibitors were detected in the region from 4.3 to 24 kDa. Thermal stability of potato protease inhibitors (region from 25 to 14 kDa) was higher, although the temperatures above 45°C caused denaturation and insolubility of most of the protease inhibitors. Extremely thermo-stable was potato carboxypeptidase inhibitor with molecular weight of 4.3 kDa that remained soluble even after having been exposed to the highest temperatures.
Keywords: potato proteins thermo-stability; potato fruit water; patatin; protease inhibitors
Published: December 31, 2008 Show citation
References
- Andrews D.L., Beames B., Summers M.D., Park W.D. (1988): Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning and abundant expression in a baculovirus vector. Biochemical Journal, 252: 199-206.
Go to original source...
Go to PubMed...
- Bárta J., Čurn V. (2004): Potato (Solanum tuberosum L.) tuber proteins - classification, characterization, importance. Chemické Listy, 98: 373-378.
- Bárta J., Heřmanová V., Diviš J. (2008): Effect of lowmolecular additives on precipitation of potato fruit juice proteins under different temperature regimes. Journal of Food Process Engineering, 31: 533-547.
Go to original source...
- Bollag D.M., Rozycki M.D., Edelstein S.J. (1996): Protein Methods. 2nd Ed., Willey-Liss, New York.
- Gonzales J.M., Lindamoon J.B., Desai N. (1991): Recovery of protein from potato plant waste effluents by complexation with carboxymethylcellulose. Food Hydrocolloids, 4: 355-363.
Go to original source...
- Hames B.D., Rickwood D. (1987): Gel Electrophoresis of Proteins. A Practical Approach. IRL Press Limited, Oxford.
- Harrison R.G., Todd P., Rudge S.R., Petrides D.P. (2003): Bioseparation Science and Engineering. Oxford University Press, Inc., New York, 303-313.
- Huang D.Y., Swanson B.G., Ryan C.A. (1981): Stability of proteinase inhibitors in potato tuber during cooking. Journal of Food Science, 46: 287-290. RES. AGR. ENG., 54, 2008 (4): 170-175 S.
Go to original source...
- Cabanes J., Garcia-Carmona F. (2001): An octaethylene glycol monododecyl ether-based mixed micellar assay for determining the lipid acyl hydrolase activity of patatin. Lipids, 36: 1169-1174.
Go to original source...
Go to PubMed...
- Kapoor A.C., Desborough S.L., Li P.H. (1975): Potato tuber proteins and their nutritional quality. Potato Research, 8: 469-478.
Go to original source...
- Knorr D. (1978): Protein quality of the potato and potato protein concentrates. Lebensmittel Wissenschaft und Technologie, 11: 109-115.
- Koningsveld van G.A., Gruppen H., Jongh de H.H.J., Wijngaards G., Boekel van M.A.J.S., Wastra P., Voragen A.G.J. (2001): The solubility of potato proteins from industrial potato fruit juice as influenced by pH and various additives. Journal of the Science of Food and Agriculture, 82: 134-142.
Go to original source...
- Laemmli U.K. (1970): Cleavage of structural proteins during the assembly of the head of bacteriophageT4. Nature, 227: 680-685.
Go to original source...
Go to PubMed...
- Lindner P., Keren R., Ben-Gera I. (1981): Precipitation of proteins from potato juice with bentonite. Journal of the Science of Food and Agriculture, 32: 1177-1182.
Go to original source...
Go to PubMed...
- Márquez M.C., Fernandez V., Alonso R. (1998): Effect of dry heat on the in vitro digestibility and trypsin inhibitor activity of chickpea flour. Journal of Food Science and Technology, 33: 527-532.
Go to original source...
- Pots M.A. (1999): Physico-chemical properties and thermal aggregation of patatin, the major potato tuber protein. Wageningen.
- Pouvreau L. (2004): Occurrence and physico-chemical properties of protease inhibitors from potato tuber (Solanum tuberosum). [Ph.D. Thesis.] Wageningen Agricultural University, Wageningen.
- Pouvreau L., Gruppen H., Piersma S.R., Broek van der L.A.M., Koningsvld van G.A., Voragen A.G.J. (2001): Relative abundance and inhibitory distribution of protease inhibitors in potato fruit juice from cv. Elkana. Journal of Agriculture and Food Chemistry, 49: 2864-2874.
Go to original source...
Go to PubMed...
- Ralet M.C., Guéguen J. (2001): Foaming properties of potato raw proteins and isolated fractions. Lebensmittel Wissenschaft und Technologie, 34: 266-269.
Go to original source...
- Senda K., Yoshioka H., Doke N., Kawakita K. (1996): A cytosolic phospholipase A2 from potato tissues appears to be patatin. Plant and Cell Physiology, 37: 347-353.
Go to original source...
Go to PubMed...
- Tonón C., Daleo G., Oliva C. (2002): Isolation of a potato acidic 39 kDa β-1,3-glucanase with antifungal activity against Phytophthora infestans and analysis of its expression in potato cultivars differing in their degrees of field resistance. Journal of Phytopathology, 150: 189-195.
Go to original source...
- Zwijnenberg H.J., Kemperman A.J.B, Boerrigter M.E., Lotz M., Dijksterhuis J.F., Poulsen P.E., Koops G-H. (2002): Native protein recovery from potato fruit juice by ultra-filtration. Desalination, 144: 331-334.
Go to original source...
This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International (CC BY NC 4.0), which permits non-comercial use, distribution, and reproduction in any medium, provided the original publication is properly cited. No use, distribution or reproduction is permitted which does not comply with these terms.