Effect of Different Steeping Conditions on the Peroxidase Activities of Some Improved Sorghum Varieties
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Abstract
In order to evaluate the impact of duration and the incorporation or otherwise of air rest during steeping on the peroxidase activities of sorghum grains, five improved varieties were studied. Steeping durations used ranged from 0 (raw grains) to 72 hours, in two formats: with air rest and without air rest. Results obtained showed that among the raw grains which were the control experiment, variety SK5912 gave the highest peroxidase activity, followed by variety KSV 8 while variety CSRO2 had the least peroxidase activity. During steeping, we observed that in almost all cases, higher peroxidase activities were obtained with air rested sorghum grains than those without air rest. In terms of how the different varieties compared during steeping, we found that variety KSV 8 gave the highest peroxidase activity at
both with and without air rest regimes in all the steeping periods used. Also, we observed that in all cases, the highest increase in peroxidase expression was obtained during the first 6 hours of steeping, shown by a steep rise of over 50% increase in activity. The other steeping times following the first 6 hours however showed just gradual increases in peroxidase over the period of sorghum. The major
significance of this result is that although increasing duration showed increased peroxidase activities, such increases were less jumpy than those obtained during the first 6 hours. Therefore, long steeping times may not necessarily be very beneficial, with the added benefit that costs associated with long steeping durations may be avoided.
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References
Anderson, R. G. (2000). Current practice in malting, brewing and distilling. In: Cereal Biotechnology (Morris, B. C. and Byrce J. H. eds.) CRC Press, Woodhead Publishing Limited, Cambridge, England.
Bakalova, S., Nikolova, A. and Wedera, D. (2004). Isoenzyme profiles of peroxidase, catalase and superoxide dismutase as affected by dehydration stress and ABA during germination of wheat seeds. Bulgarian Journal of Plant Physiology, 30: 64–77.
Bamforth, C.W. (2002). Standards of Brewing: A Practical Approach to Consistency and Excellence. Brewers Publications, Boulder.
Bamforth, C.W., Muller, R.E. and Walker, M.D. (1993). Oxygen and oxygen radicals in malting and brewing. Journal of the American Society of Brewing Chemists, 51: 79-88.
Briggs, D. E. (1987). Accelerating malting: A review of some lessons of the past from the United Kingdom. Journal of the American Society of Brewing Chemists, 45: 0001.
Briggs, D. E. (1998). Malts and Malting. Blackie, London.
Clarkson, S.P., Large, P.J. and Bamforth, C.W. (1992). Oxygen-scavenging enzymes in barley and malt and their effects during mashing. Journal of the Institute of Brewing, 98: 111-115.
Dewar, J., Taylor, J.R.N. and Berjak, P. (1997). Determination of improved steeping conditions for sorghum malting. Journal of Cereal Science, 26: 129-136.
Dey, E.S., Staniszewska, M., Pasciak, M., Konopacka, M., Rogolinski, J., Gamian, A. and Danielsson, B. (2005). The cytotoxic and genotoxic effects of conjugated trans-2-nonenal (T2N), an off-flavour compound in beer and heat processed food arising from lipid oxidation. Polish Journal of
Microbiology, 54: 47-52.
Diao, M., Kone, O.H., Quedraogo, N., Bayili, R.G., Bassole, I.H. and Dicko, M.H. (2011). Comparison of peroxidase activities from Allium sativum, Ipomoea batatas, Raphanus sativus and Sorghum bicolor grown in Burkina Faso. African Journal of Biochemistry Research, 5: 124-128.
Dicko, M.H., Gruppen, H., Traore, A.S., Voragen, A.G.J. and van Berkel, W.J.H. (2006). Phenolic compounds and related enzymes as determinants of sorghum for food use. Biotechnology and Molecular Biology Reviews, 1: 21-38.
Dunford, H.B. (1999). Heme Peroxidases, John Wiley and Sons Inc. Chichester.
Dunford, H.B. (2010): Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology, 2nd edn. John Wiley and Sons, New Jersey.
Elliot, J. (2006). Antioxidant Enzymes. Available at http://www.webcontent.com/articles/86/1/Antioxidant-Enzyme/Page1.html. (last accessed 15 March 2012).
French, B.J. and McRuer, G.R. (1990). Malt quality as affected by various steep aeration regimes. MBAA Technical Quarterly, 27: 10-14.
Hilderbrand, D.F. (1992). Genetic engineering of plant foods for altered fatty acid metabolism. Food Technology, 46: 71-74.
Igyor, M. A., Ogbonna, A. C. and Palmer, G. H. (1989). Effect of malting temperature and time on enzyme development and sorghum wort properties. Journal of the Institute of Brewing, 104: 101–104.
Ishibashi, Y., Yamamoto, K., Tawaratsumida, T., Yuasa, T. and Iwaya‑Inoue, M. (2008). Hydrogen peroxide scavenging regulates germination ability during wheat (Triticum aestivum L.) seed maturation. Plant Signalling and Behaviour, 3: 183-188.
Kruger, J.E. (1977). Changes in the catalases of wheat during kernel growth and maturation. Cereal Chemistry, 54: 820 – 82.
Lin, A., Zhang, X., Zhu, Y.G. and Zhao, F.J. (2008). Arsenate-induced toxicity: Effects on antioxidative enzymes and DNA damage in Vicia faba. Environmental and Toxicological Chemistry, 27: 413-419.
Nnamchi, C. I., Okolo, B. N., Moneke, A. N. and Nwanguma, B. C. (2013). Changes in the activities of peroxidases during different stages of sorghum malting. International Journal of Advanced Research (Accepted paper).
McLellan, K.M. and Robinson, D.S. (1981). The heat stability of purified spring cabbage peroxidase isoenzymes. Food Chemistry, 26: 97-107.
Mliki, A. and Zimmermann, W. (1992). Purification and characterization of an intracellular peroxidase from Streptomyces cyaneus. Applied and Environmental Microbiology, 58: 916-919.
Murphy, E.J., Metcalfe, C.L., Nnamchi, C.I, Moody, P.C.E. and Raven, E.L. (2012). Crystal structure of guaiacol and phenol bound to a heme peroxidase. FEBS Journal, 279: 1632–1639.
Nwanguma, B.C. and Eze, M.O. (1995). Heat sensitivity, optimum pH and changes in activity of sorghum peroxidase during malting and mashing. Journal of the Institute of Brewing, 101: 275-276.
Ogbonna, A.C., Obi, S.K.C. and Okolo, B.N. (2003). Modifications of the methods for the extraction of carboxypeptidase and proteinase activities from sorghum malts. Journal of the Institute of Brewing, 109: 51-56.
Passardi, F., Cosio, C., Penel, C. and Dunand, C. (2005). Peroxidases have more functions than a Swiss army knife. Plant Cell Reports, 24: 255–265.
Passardi, F., Longet, D., Penel, C. and Dunand, C. (2004). The class III peroxidase multigenic family in rice and its evolution in land plants. Phytochemistry, 65: 1879-1893.
Santimone, M. (1975). Titration study of guaiacol oxidation by horseradish peroxidase. Can. Journal of Biochemistry, 53: 649–657.
Scialabba, A., Bellani, L.M. and Dell’Aquila, A. (2002). Effects of ageing on peroxidase activity and localization in radish (Raphanus sativus L.) seeds. European Journal of Histochemistry, 46: 351–358.
Sessa, D.J. and Anderson, R.L. (1981). Soybean Peroxidases: Purification and some properties. Journal of Agricultural Food Chemistry, 29: 960-965.
Suzuki, T., Honda, Y., Mukasa, Y. and Kim, S. (2006). Characterization of peroxidase in buckwheat seed. Phytochemistry, 67: 219–224.
Ukwuru, M. U. (2010). Effect of steeping conditions on the amylolytic development of some Nigerian improved sorghum cultivars. Journal of Food Science and Technology, 47: 61–66.
Zmrhal, Z. and Machackova, I. (1978). Isolation and characterization of wheat peroxidase isoenzyme Bl. Phytochemistry 17: 1517-1520.