Skip to main content
Log in

Influence of the malting parameters on the haze formation of beer after filtration

  • Original Paper
  • Published:
European Food Research and Technology Aims and scope Submit manuscript

Abstract

Malting changes the chemical and enzymatical composition of barley. During malting, enzymes are synthesized, cell walls (pentosans, proteins, etc.) degraded and starch becomes available for enzymatic attack. The progress of germination defines the final beer quality and processability in several aspects: mouthfeel, foam and haze formation (different proteins), processability (viscosity caused by certain substances, like β-glucan), fermentation progress (FAN, sugar content), etc. The objective of this research was to study the influence of different modified malt on turbidity in beer after filtration. This was achieved by analyzing selected malts at different germination stages and afterward studying their influence on the final beer composition, focusing on protein content and composition. Protein fractions were analyzed using a Lab-on-a-Chip technique, which separates the proteins—based on their molecular weight—by capillary electrophoresis. This analysis was supported by the use of two-dimensional gel electrophoresis (2D-PAGE). Additionally, common malt and beer analyses and turbidity and filterability measurements were performed. The protein composition could be followed from malt to beer with both the Lab-on-a-Chip technique and 2D-PAGE. No differences in protein composition could be seen in the final protein composition of the beer. However, it could be observed, with Lab-on-a-Chip technique, that high amounts of a protein fraction with a size of 25–28 kDa caused increased turbidity in the beer.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2

Similar content being viewed by others

Abbreviations

EBC:

European Brewing Convention

MEBAK:

Mitteleuropäische Brautechnische Analysenkommission

References

  1. Curioni A et al (1995) Major proteins of beer and their precursors in barley: electrophoretic and immunological studies. J Agric Food Chem 43(10):2620–2626

    Article  CAS  Google Scholar 

  2. Hejgaard J, Kaersgaard P (1983) Purification and properties of the major antigenic beer protein of barley origin. J Inst Brew 89 (6):402–410

    Google Scholar 

  3. Evans DE, Sheehan MC (2002) Don’t be fobbed off: the substance of beer foam. J Am Soc Brew Chem 60(2):47–57

    Google Scholar 

  4. Van Nierop SNE et al (2004) Impact of different wort boiling temperatures on the beer foam stabilizing properties of lipid transfer protein 1. J Agric Food Chem 52(10):3120–3129

    Article  Google Scholar 

  5. Bamforth CW (1999) Beer haze. J Am Soc Brew Chem 57(3):81–90

    CAS  Google Scholar 

  6. Kaersgaard P, Hejgaard J (1979) Antigenic beer macromolecules: an experimental survey of purification methods. J Inst Brew 85(2):103–111

    Google Scholar 

  7. Nadzeyka A et al (1979) The significance of beer proteins in relationship to cold break and age-related haze formation. Brauwissenschaft 32(6):167–172

    CAS  Google Scholar 

  8. Siebert KJ et al (1996) Formation of protein-polyphenol haze in beverages. J Agric Food Chem 44(8):1997–2005

    Article  CAS  Google Scholar 

  9. Asano K et al (1982) Characterization of haze-forming proteins of beer and their roles in chill haze formation. J Am Soc Brew Chem 40(4):147–154

    CAS  Google Scholar 

  10. Siebert KJ (1999) Protein-polyphenol haze in beverages. Food Technol (Chicago) 53(1):54–57

    CAS  Google Scholar 

  11. Siebert KJ (1999) Effects of protein-polyphenol interactions on beverage haze, stabilization, and analysis. J Agric Food Chem 47(2):353–362

    Article  CAS  Google Scholar 

  12. Kreisz S (2002) Der Einfluss von Polysacchariden aus Malz. Hefe und Bakterien auf die Filtrierbarkeit von Würze und Bier, TU-München, Freising

    Google Scholar 

  13. Cach N, Annemüller G (1995) Ein Beitrag über die Pentosane im Prozess der Bierherstellung–sind sie wichtig oder technologisch unbedeutend? = Contribution on pentosans in the beer brewing process, are they important or insignificant technologically? Monatsschrift für Brauwissenschaft 48(7–8):232–241

    Google Scholar 

  14. Narziß L (2005) Abriss der Bierbrauerei, vol 7. Wiley, VCH

  15. Shewry PR (1993) Barley seed proteins. Barley:131–197

  16. Leiper KA et al (2003) Beer polypeptides and silica gel. Part II. Polypeptides involved in foam formation. J Inst Brew 109 (1):73–79

    Google Scholar 

  17. Leiper KA et al (2003) Beer polypeptides and silica gel. Part I. Polypeptides involved in haze formation. J Inst Brew 109(1):57–72

    Google Scholar 

  18. Leiper KA et al (2005) Optimising beer stabilisation by the selective removal of tannoids and sensitive proteins. J Inst Brew 111(2):118–127

    Google Scholar 

  19. MEBAK (2002) Brautechnische Analysenmethoden, vol 2nd Volume. 4th edn. Methodensammlung der Mitteleuropäischen Brautechnischen Analysenkommission

  20. McMurrough I et al (1992) Effect of the removal of sensitive proteins and proanthocyanidins on the colloidal stability of lager beer. J Am Soc Brew Chem 50(2):67–76

    CAS  Google Scholar 

  21. Siebert KJ (2006) Haze formation in beverages. LWT–Food Sci Technol 39(9):987–994

    Google Scholar 

  22. Siebert KJ et al (1996) Nature of polyphenol-protein interactions. J Agric Food Chem 44(1):80–85

    Article  CAS  Google Scholar 

  23. McManus JP et al (1985) Polyphenol interactions 1. Introduction; some observation on the reversible complexation of polyphenols with proteins and polysaccharides. J Chem Soc Perkin Trans 11:1429–1438

    Google Scholar 

  24. McMurrough I et al (1996) The role of flavanoid polyphenols in beer stability. J Am Soc Brew Chem 54(3):141–148

    CAS  Google Scholar 

  25. Okada Y et al (2008) The influence of barley malt protein modification on beer foam stability and their relationship to the barley dimeric alpha -amylase inhibitor-I (BDAI-I) as a possible foam-promoting protein. J Agric Food Chem 56(4):1458–1464

    Article  CAS  Google Scholar 

  26. Nursten H (2005) The Maillard reaction: chemistry, biochemistry and implications. Royal Society of Chemistry, Cambridge

    Google Scholar 

  27. Esslinger HM (ed) (2009) Handbook of brewing: processes, technology, markets. Wiley, London

    Google Scholar 

  28. Kunze W (2007) Technologie Brauer und Mälzer, vol 9. VLB Berlin

  29. Shewry PR et al (1978) Comparison of methods for extraction and separation of hordein fractions from 29 barley varieties. J Sci Food Agric 29(5):433–441

    Article  CAS  Google Scholar 

  30. Shewry PR, Miflin BJ (1985) Seed storage proteins of economically important cereals. Adv Cereal Sci Technol 7:1–83

    CAS  Google Scholar 

  31. Jin B et al (2009) Proteomics study of silica eluent proteins in beer. J Am Soc Brew Chem 67(4):183–188

    Google Scholar 

  32. Jin B et al (2009) Structural changes of malt proteins during boiling. Molecules 14(3):1081–1097

    Article  CAS  Google Scholar 

  33. Sheehan M, Skerritt J (1997) Identification and characterisation of beer polypeptides derived from barley hordeins. J Inst Brew 103(5):297–306

    CAS  Google Scholar 

  34. Jones BL (2005) Endoproteases of barley and malt. J Cereal Sci 42(2):139–156

    Article  CAS  Google Scholar 

  35. Jones BL (2005) The endogenous endoprotease inhibitors of barley and malt and their roles in malting and brewing. J Cereal Sci 42(3):271–280

    Article  CAS  Google Scholar 

  36. Jones BL, Budde AD (2005) How various malt endoproteinase classes affect wort soluble protein levels. J Cereal Sci 41(1):95–106

    Article  CAS  Google Scholar 

  37. Zhang NY, Jones BL (1995) Characterization of germinated barley endoproteolytic enzymes by 2-dimensional gel-electrophoresis. J Cereal Sci 21(2):145–153

    Article  CAS  Google Scholar 

  38. Poulle M, Jones BL (1988) A proteinase from germinating barley. I. Purification and some physical properties of a 30 kD cysteine endoproteinase from green malt. Plant Physiol 88(4):1454–1460

    Article  CAS  Google Scholar 

  39. Finnie C et al (2004) Aspects of the barley seed proteome during development and germination. Biochem Soc Trans 32(3):517–519

    Article  CAS  Google Scholar 

  40. Finnie C et al (2002) Proteome analysis of grain filling and seed maturation in barley. Plant Physiol 129(3):1308–1319

    Article  CAS  Google Scholar 

  41. Finnie C et al (2003) Barley proteome analysis, starch degrading enzymes and proteinaceous inhibitors. J Appl Glycosci 50(2):277–282

    CAS  Google Scholar 

  42. Finnie C, Svensson B (2009) Barley seed proteomics from spots to structures. J Proteomics 72 (3):315–324

    Google Scholar 

  43. Jones BL (1997) Malt endoproteinases; their synthesis and inactivation during malting and mashing. Proc 1st Eur Symp Enzym Grain Process, pp 54–64

  44. Jones BL, Budde AD (1999) Endoproteinases and the hydrolysis of malt proteins during mashing. Proc Congr—Eur Brew Conv 27th:611–618

    Google Scholar 

  45. Asano K, Hashimoto N (1980) Isolation and characterization of foaming proteins of beer. J Am Soc Brew Chem 38(4):129–137

    CAS  Google Scholar 

  46. Iimure T et al (2009) Identification of novel haze-active beer proteins by proteome analysis. J Cereal Sci 49(1):141–147

    Article  CAS  Google Scholar 

  47. Bamforth CW (2001) A brewer's biochemistry. Brew int 1(3):21–25

    Google Scholar 

  48. Djurtoft R (1965) Composition of the protein and polypeptide fraction of EBC beer haze preparations. J Inst Brew 71(4):305–315

    CAS  Google Scholar 

  49. Mussche R (1990) Physico-chemical stabilization of beer using new generation gallotannins. Proc 21st Conv—Inst Brew (Aust NZ Sect), pp 136–140

  50. Osman AM (2003) Barley and malt proteins and proteinases: II. The purification and characterisation of five malt endoproteases, using the highly degradable barley protein fraction (HDBPF) substrate. J Inst Brew 109(2):142–149

    Google Scholar 

  51. Osman AM (2003) Barley and malt proteins and proteinases: I. Highly degradable barley protein fraction (HDBPF), a suitable substrate for malt endoprotease assay. J Inst Brew 109(2):135–414

    Google Scholar 

  52. Osman AM (2003) Barley and malt proteins and proteinases: III. A simple method for estimating the combined actions of malt proteinases and the extent of prtein degradation during malting. J Inst Brew 109(2):150–153

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Elisabeth Steiner.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Steiner, E., Arendt, E.K., Gastl, M. et al. Influence of the malting parameters on the haze formation of beer after filtration. Eur Food Res Technol 233, 587–597 (2011). https://doi.org/10.1007/s00217-011-1547-0

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00217-011-1547-0

Keywords

Navigation