Abstract
Barley germplasm including breeding lines, wild barley accessions and mapping population parents were screened for variation in α-amylase using isoelectric focusing (IEF) in conjunction with activity staining. IEF screening found extensive variation in α-amylase IEF banding patterns with 14 and 49 different α-amylase isoenzymes identified for low- and high-pI groups, respectively. Alpha-amylase enzyme activity assayed at a range of temperatures (40–75 °C) revealed significant variation in the levels of enzyme activity and thermostability between varieties belonging to different IEF groups. The relationship between fermentability and α-amylase activity and thermostability was studied in 30 elite breeding lines and variation in thermostability between IEF groups was found to have a significant impact on fermentability.
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References
Ahokas, H., & Naskali, L. (1990). Geographic variation of a-amylase, b-amylase, b-glucanase, pullulanase and chitinase activity in germinating Hordeum spontaneum barley from Israel and Jordan. Genetica, 82, 73–78.
Ajandouz, E. L. H., Abe, J. I., Svensson, B., & Marchis-Mouren, G. (1992). Barley malt-a-amylase. Purification, action pattern, and subsite mapping of isozyme 1 and two members of the isozyme 2 subfamily using p-nitrophenylated maltooligosaccharide substrates, Biochimica et biophysica acta. Protein Structure and Molecular Enzymology, 2, 193–202.
Bertoft, E., Andtfolk, C., & Kulp, S. (1984). Effects of pH, temperature, and calcium ions on barley malt alpha-amylase isoenzymes. The Journal of The Institute of Brewing & Distilling, 5, 298–302.
Brown, A. H. D., & Jacobsen, J. V. (1982). Genetic basis and natural variation of alpha-amylase isozymes in barley. Genetical Research, 3, 315–324.
Bush, D., Sticher, L., van Huystee, R., Wagner, D., & Jones, R. (1989). The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone alpha-amylase. The Journal of Biological Chemistry, 264, 19392–19398.
EBC. (1997). Analytica-EBC (European Brewery Convention). Nürnberg: Fachverlag Hans Karl.
Eglinton, J. K., Langridge, P., & Evans, D. E. (1998). Thermostability variation in alleles of barley beta-amylase. Journal of Cereal Science, 28, 301–309.
Evans, D. E., MacLeod, L. C., Eglinton, J. K., Gibson, C. E., Zhang, X., Wallace, W., Skerritt, J. H., & Lance, R. C. M. (1997). Measurement of beta-amylase in malting barley (Hordeum vulgare L.). I. Development of a quantitative ELISA for beta-amylase. Journal of Cereal Science, 26, 229–239.
Evans, E., Van Wegen, B., Ma, Y., & Eglinton, J. (2003). The impact of the thermostability of alpha-amylase, beta-amylase, and limit dextrinase on potential wort fermentability. Journal of the American Society of Brewing Chemists, 61, 210–218.
Evans, D. E., Collins, H. M., Eglinton, J. K., & Wilhelmson, A. (2005). Assessing the impact of the level of diastatic power enzymes and their thermostability on the hydrolysis of starch during wort production to predict malt fermentability. Journal of the American Society of Brewing Chemists, 63, 195–198.
Filner, F., & Varner, J. E. (1967). A test for the de novo synthesis of enzyme: density labeling with H2018 of barley alpha-amylase induced by gibberellic acid. Proceedings of the National Academy of Sciences of the United States of America, 58, 1520–1526.
Frydenberg, O., & Nielsen, G. (1965). Amylase isozymes in germinating barley seeds. Hereditas, 54, 123–139.
Frydenberg, O., Nielsen, G., & Sandfaer, J. (1969). The inheritance and distribution of alpha-amylase types and DDT responses in barley. Journal of Plant Breeding, 61, 201–215.
Henry, R. (1984). A rapid method for the determination of diastatic power. Journal of the Institute of Brewing, 90, 37–39.
Henson, C., & Stone, J. (1988). Variation in alpha-amylase and alpha-amylase inhibitor activities in barley malts. Journal of Cereal Science, 8, 39–46.
Jacobsen, J. V., & Higgins, T. J. V. (1982). Characterization of the {alpha}-amylases synthesized by aleurone layers of Himalaya barley in response to gibberellic acid. Plant Physiology, 70, 1647–1653.
Jensen, M. T., Gottschalk, T. E., & Svensson, B. (2003). Differences in conformational stability of barley alpha-amylase isozymes 1 and 2. Role of charged groups and isozyme 2 specific salt-bridges. Journal of Cereal Science, 38, 289–300.
Khursheed, B., & Rogers, J. (1988). Barley alpha-amylase genes. Quantitative comparison of steady state mRNA levels from individual members of the two different families expressed in aleurone cells. The Journal of Biological Chemistry, 263, 18953–18960.
Kihara, M., Kaneko, T., & Ito, K. (1998). Genetic variation of beta-amylase thermostability among varieties of barley, Hordeum vulgare L., and relation to malting quality. Plant Breeding, 117, 425–428.
Knox, C., Sonthayanon, B., Chandra, G., & Muthukrishnan, S. (1987). Structure and organization of two divergent aamylase genes from barley. Plant Molecular Biology, 9, 3–17.
Mundy, J. (1984). Hormonal regulation of α-amylase inhibitor synthesis in germinating barley. Carlsberg Research Communications, 49, 439–444.
Mundy, J., Svendsen, I., & Hejgaard, J. (1983). Barley alpha-amylase/subtilisin inhibitor I. Isolation and characterization. Carlsberg Research Communications, 48, 81–90.
Muthukrishnan, S., Gill, B., Swegle, M., & Chandra, C. (1984). Structural genes for alpha-amylases are located on barley chromosomes 1 and 6. The Journal of Biological Chemistry, 259, 13637–13639.
Nevo, E., Zohary, D., Brown, A. H. D., & Haber, M. (1979). Genetic diversity and environmental associations of wild barley, Hordeum spontaneum, in Israel. Evolution, 3, 815–833.
Roumeliotis, S., & Tansing, P. (2004). SA barley improvement program barley quality report 2001 and 2002 seasons. Adelaide: Waite Barley Quality Evaluation Laboratory, The University of Adelaide.
Vallée, F., Kadziola, A., Bourne, Y., Juy, M., Rodenburg, K. W., Svensson, B., & Haser, R. (1998). Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 å resolution. Structure, 6, 649–659.
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The authors would like to acknowledge GRDC for funding this project (UA00108).
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© 2013 Zhejiang University Press and Springer Science+Business Media Dordrecht
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Cu, S., Roumeliotis, S., Eglinton, J. (2013). Alpha-Amylase Allelic Variation in Domesticated and Wild Barley. In: Zhang, G., Li, C., Liu, X. (eds) Advance in Barley Sciences. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4682-4_5
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DOI: https://doi.org/10.1007/978-94-007-4682-4_5
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