Changes in catalase activities during malting of some improved Nigerian sorghum grain varieties.
Main Article Content
Abstract
The catalase activities of ten germinating improved sorghum varieties were monitored over a 4-day period to determine the effect of malting on them. This was done using standard methods that involved catalase assay at the appropriate experimental intervals. Results obtained showed that the different varieties of sorghum differed in their expression of catalase, a difference that was also reflected across the different stages of the malting process. The highest overall catalase activity (20.54 ± 0.74 U) was given by variety SK5912 after 72 hours of germination followed in second place by that from variety Nafelen (18.65 ± 0.99 U) obtained after steeping. The third and fourth highest value (17.88 ± 1.24 U and 17.08 ± 1.64 U) were given by KSV8 and Boboje after 72 and 48 hours of germination respectively. These values are probably indications that no single stage of malting was best for catalase expression among all the varieties. However, the fact that most of them (varieties ICSV 400, SK5912 and KSV 8, CSRO2 and ICSV III) all expressed their highest catalase activities after 72 hours of germination showed that 72 hours is probably the best germination stage for the elicitation of catalase among sorghum grains. The next best stage should be after 48 hours during which point three varieties (Boboje, NRL 3 and KAT 487) had their highest catalase activities. As a unity, all the sorghum varieties had their lowest catalase expression after 24 hours of germination, followed by those obtained after 96 hours germination.
Downloads
Article Details

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
References
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. (2009). Current perspectives on the role of enzymes in brewing. Journal of Cereal Science 50: 353–357.
Bamforth, C.W. (2002) Standards of Brewing: A Practical Approach to Consistency and Excellence. Brewers Publications, Boulder.
Chapman, G. W. (1987). A proteinaceous competitive inhibitor of lipase isolated from Helianthus annum seeds. Phytochemistry 26: 3127-3131.
Choon, S. Y., Ahmad, S. H., Ding, P., Sinniah, U. R. and Hamid, A. A. (2010). Morphological and chemical characteristics of Black gram (Vigna
mungo L.) sprouts produced in a modified atmosphere chamber at four seeding densities. Pertanika Journal of Tropical Agricultural Sciences 33: 179 –191.
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.
Dicko, M. H., Gruppen, H., Zouzouho, O. C., Traore, A. S., van Berkel, W. J. H. and Voragen, A. G. J. (2006). Effects of germination on the activities of amylases and phenolic enzymes in sorghum varieties grouped according to food end-use properties. Journal of the Science of Food and Agriculture 86: 953-963.
Dicko, M. H., Hilhorst, R., Gruppen, H., Traore, A. S., Laane, C., van Berkel, W. J. H. and Voragen, A. G. J. (2002). Comparison of content in phenolic
compounds, polyphenol oxidase and peroxidase in grains of fifty sorghum varieties from Burkina Faso. Journal of Agricultural and Food Chemistry 50: 3780-3788.
Dunford, H. B. (2010). Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology, 2nd Edition. John Wiley and Sons, Hoboken, New Jersey.
Ejeta, G. and J.E. Knoll, 2007. Marker-assisted selection in sorghum. In: Varshney, R.K. and R. Tuberosa (eds.), Genomic-assisted Crop Improvement Genomics Applications in Crops, Vol. 2, pp: 187–205, Springer books.
Elliot, J. (2006): Antioxidant Enzymes. Available at http://www.webcontent.com/articles/86/1/Antioxidant-Enzyme/Page1.html. (last accessed 15 March 2012).
Ezeogu, L.I. and Okolo, B.N. (1994) Effects of final warm water steep and air-rest cycles on malt properties of three improved Nigeian sorghum cultivars. Journal of the Institute of Brewing 100: 335 – 338.
Farkas, G. L., Dezsi. l., Horvath. M., Kisban, K. and Udvardy, J (1963). Common pattern of enzymatic changes in detached leaves and tissues attacked by parasites. Phytopathologia Zeit. 49: 343-354.
Frederiksen, A. M., Festersen, R. M. and Andersen, M. L. (2008). Oxidative reactions during early stages of beer brewing studied by electron spin
resonance and spin trapping. Journal of Agricultural and Food Chemistry 56: 8514 – 8520.
Halliwell, B. and Gutteridge, J. M. C. (1989). Free Radicals in Biology and Medicine (4th Edition). Oxford University Press, New York.
Harb, A., Awad, D. and Samarah, N. (2015). Gene expression and activity of antioxidant enzymes in barley (Hordeum vulgare L.) under controlled severe drought. Journal of Plant Interactions 10: 109 – 116.
Haywood, G., W. and Large, P., J. (1981). Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source. Biochemical Journal 199: 187-201.
Hiraga, S., Sasaki, K., Ito, H., Ohashi, Y. and Matsui, H. (2001). A large family of class III plant peroxidases. Plant Cell Physiology 42: 462 – 468.
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 Signaling and Behavior 3: 183-188.
Ito, S. and Hayashi, S. (1961). Effect of limited oxygen supply on activities of catalase, peroxidase and cytochrome oxidase in germinating rice seeds. Nippon Sakumotsu Gakkai Kiji 30: 97-100.
Kar, M. and Mishra, D. (1976). Catalase, Peroxidase, and Polyphenoloxidase Activities during Rice Leaf Senescence. Plant Physiology 57: 315-319.
Kisban, G., Horvath. M., Dezsi, L., Udvardy. J., and Farkas. G. L. (1964). Role of root system in the regulation of enzyme levels in leaf tissues. Acta Botan. Acad. Sci. Hung. 10: 275-287.
Kruger, J. E. (1977). Changes in the catalases of wheat during kernel growth and maturation. Cereal Chemistry 54: 820 – 826.
Maneemegalai, S. and Nandakumar, S. (2018). Studies on the influence of germination on the activity of antioxidant enzymes of Vigna radiata, Vigna mungo and Pennisetum typhoides seeds. International Journal of Research in Biosciences 7: 30 – 36.
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 1(7): 44-58.
Nout, M.J.R. and Ngoddy, P.O. (1997). Technological aspects of preparing affordable fermented complementary foods. Food Control 8: 279-287.
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). Protein modification in malting sorghum. World J. Microbiol. Biotechnol. 19: 495-503.
Palmiano, E. P. and Juliano, B. O. (1973). Changes in the Activity of Some Hydrolases, Peroxidase, and Catalase in the Rice Seed during Germination. Plant Physiology 52: 274 – 277.
Parish. R. W. (1968). Studies on senescing tobacco leaf disks with special reference to peroxidase. I. The effects of cutting and of inhibition of nucleic acid and protein synthesis. Planta 82: 1-13.
Purselove, J. W. (1972). Tropical Crops: Monocotyledons. Longman Ltd, UK.
Scandalios, J.G., Tsaftaris, A.S., Chandlee, J.M. and Skadsen, R.M. (1984). Expression of the developmentally regulated catalase (Cat) genes in maize. Developmental Genetics 4: 281 – 293.
Siminis, C., Kanellis, A. K. and Roubelakis-Angelakis, K. A. (1994). Catalase 1s Differentially Expressed in Dividing and Nondividing Protoplasts. Plant Physiology 105: 1375-1383.
Sooch, B. S., Kauldhar, B. S. and Puri, M. (2016). Catalases: types, structure, applications and future outlook. In: Microbial Enzyme Technology in Food Applications, First Edition (Ray, R.C and Rosell C.M. Editors). CRC Press, Taylor and Francis Group.
Switala, J. and Loewen, P. C. (2002). Diversity of properties among catalases. Archives of Biochemistry and Biophysics 15: 45 – 54.
Taylor, J. R. N., Schober, T. J. and Bean, S. R. (2006). Novel food and non-food uses for sorghum and millets. Journal of Cereal Science 44: 252 – 271.
Taylor, J.R.N., Noveille, L. and Liebenberg, N.W. (1985). Protein body degradation in the starchy endosperms of germinating sorghum. Journal of Experimental Biology 36: 1287-1295.
Traore, T., Mouquet, C., Icard-Verniere, C., Traore, A.S. and Treche, S. (2004). Changes in nutrient composition, phytate and cyanide contents and
amylase activity during cereal malting in small production units in Ouagadougou (Burkina Faso). Food Chemistry 88: 105-114.
USDA (2011): US Department of Agriculture, Foreign Agricultural Service (Circular Series FG 12-11). Grain: World Market and Trades, 2011. Pg 25
Wong, J. H., Lau, T., Cai, N., Singh, J., Pedersen, J. F., Vensel, W., Hurkman, W. J., Wilson, J. D., Lemaux, P. G. and Buchanan, B. B. (2009). Digestibility of protein and starch from sorghum (Sorghum bicolor) is linked to biochemical and structural features of grain endosperm. Journal of Cereal
Science 49: 73–82.
Yoruk, I.H., Demir, H., Ekici, K. and Savran, A. (2005). Purification and properties of catalase from Van Apple (Golden Delicious). Pakistan Journal of Nutrition, 4: 8-10.