Skip to main content

Alpha-Amylase Allelic Variation in Domesticated and Wild Barley

  • Conference paper
  • First Online:
Book cover Advance in Barley Sciences

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.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

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.

    Article  CAS  Google Scholar 

  • 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.

    Article  Google Scholar 

  • 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.

    Google Scholar 

  • Brown, A. H. D., & Jacobsen, J. V. (1982). Genetic basis and natural variation of alpha-amylase isozymes in barley. Genetical Research, 3, 315–324.

    Article  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • EBC. (1997). Analytica-EBC (European Brewery Convention). Nürnberg: Fachverlag Hans Karl.

    Google Scholar 

  • Eglinton, J. K., Langridge, P., & Evans, D. E. (1998). Thermostability variation in alleles of barley beta-amylase. Journal of Cereal Science, 28, 301–309.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • 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.

    CAS  Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Frydenberg, O., & Nielsen, G. (1965). Amylase isozymes in germinating barley seeds. Hereditas, 54, 123–139.

    Article  CAS  Google Scholar 

  • 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.

    Google Scholar 

  • Henry, R. (1984). A rapid method for the determination of diastatic power. Journal of the Institute of Brewing, 90, 37–39.

    CAS  Google Scholar 

  • Henson, C., & Stone, J. (1988). Variation in alpha-amylase and alpha-amylase inhibitor activities in barley malts. Journal of Cereal Science, 8, 39–46.

    Article  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • Mundy, J. (1984). Hormonal regulation of α-amylase inhibitor synthesis in germinating barley. Carlsberg Research Communications, 49, 439–444.

    Article  CAS  Google Scholar 

  • Mundy, J., Svendsen, I., & Hejgaard, J. (1983). Barley alpha-amylase/subtilisin inhibitor I. Isolation and characterization. Carlsberg Research Communications, 48, 81–90.

    Article  CAS  Google Scholar 

  • 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.

    PubMed  CAS  Google Scholar 

  • 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.

    Article  Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Article  PubMed  Google Scholar 

Download references

Acknowledgement

The authors would like to acknowledge GRDC for funding this project (UA00108).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Suong Cu .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2013 Zhejiang University Press and Springer Science+Business Media Dordrecht

About this paper

Cite this paper

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

Download citation

Publish with us

Policies and ethics