Skip to main content
Log in

The Effect of Aqueous Urea on the Processing, Structure and Properties of CGM

  • Original Paper
  • Published:
Journal of Polymers and the Environment Aims and scope Submit manuscript

Abstract

Corn gluten meal (CGM) is potentially a cost-effective raw material for producing a bioderivable thermoplastic. However, CGM disintegrates to a powder subsequent to processing with polar plasticisers, such as water. The hypothesis of this study was that aqueous urea could be used to denature protein within CGM and therefore encourage protein–protein interactions leading to consolidated bioplastics when using water as a plasticiser. To assess this, the effects of aqueous urea on structure and properties of CGM with particular focus on storage were assessed. Processing of CGM with aqueous urea produced consolidated materials. FTIR analysis showed secondary structure was modified during processing, leading to increased amounts of α-helices and random coils and reduction of the amount of intermolecular β-sheets and turns. Above 6 wt% free water, the plasticising efficiency of water in processed CGM increased as the amount of denatured proteins increased. Below 6 wt% free water, protein secondary structure did not have a significant influence on thermal and flexural properties. It was found that storage environment and urea concentration influenced the rate of drying, however, the final water content was constant relative to CGM, and not urea. The materials were resistant to cracking at urea concentrations above 8 M, provided the mass loss during storage did not exceed 15 wt%.

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
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Similar content being viewed by others

References

  1. Shukla R, Cheryan M (2001) Zein: the industrial protein from corn. Ind Crop Prod 13:171–192

    Article  CAS  Google Scholar 

  2. Wang Y, Padua GW (2004) Water sorption properties of extruded zein films. J Agric Food Chem 52:3100–3105

    Article  CAS  Google Scholar 

  3. Di Gioia L, Guilbert S (1999) Corn protein-based thermoplastic resins: effect of some polar and amphiphilic plasticisers. J Agric Food Chem 47:1254–1261

    Article  CAS  Google Scholar 

  4. Richardson JS (1981) The anatomy and taxonomy of protein structure. Adv Protein Chem 34:167–339

    Article  CAS  Google Scholar 

  5. Whitford D (2005) Proteins structure and function. Wiley, Chichester

    Google Scholar 

  6. Nielson HC et al (1970) Extraction and structure studies on corn glutelin proteins. Cereal Chem 47(5):501–512

    Google Scholar 

  7. Danzer LA, Ades H, Rees ED (1975) The helical content of zein, a water insoluble protein, in non-aqueous solvents. Biochim Biophys Acta 389:26–31

    Google Scholar 

  8. Esen A (1987) A proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays L.). J Cereal Chem 5:117–128

    Article  CAS  Google Scholar 

  9. Wall JS, Cooker LA, Bietz JA (1988) Structure and origin of maize endosperm alcohol-insoluble glutelin. J Agric Food Chem 36:722–728

    Article  CAS  Google Scholar 

  10. del Angel SS, Martinez EM, Lopez MAV (2003) Study of denaturation of corn proteins during storage using differential scanning calorimetry. Food Chem 83:531–540

    Article  Google Scholar 

  11. De Graaf L (2000) Denaturation of proteins from a non-food perspective. J Biotechnol 79:299–306

    Article  Google Scholar 

  12. Sears JK, Darby JR (1982) Mechanism of plasticiser action. In: Sears JK, Darby JR (eds) The technology of plasticizers. Wiley, New York, pp 33–77

    Google Scholar 

  13. Creighton TE (1993) Proteins: structure, molecular properties. W. H. Freeman and Company, New york

    Google Scholar 

  14. Creighton TE (1994) The protein folding problem. In: Pain RH (ed) Mechanisms of protein folding. Oxford University Press, New York

    Google Scholar 

  15. Prakash V et al (1981) Interactions of proteins with solvent components in 8 M urea. Arch Biochem Biophys 210(2):455–464

    Article  CAS  Google Scholar 

  16. Frank HS, Franks F (1968) Structural approach to the solvent power of water for hydrocarbons; urea as a structure breaker. J Chem Phys 48(10):4746–4757

    Article  CAS  Google Scholar 

  17. Beauregard DV, Barrett RE (1968) Ultrasonics and water structure in urea solutions. J Chem Phys 49(12):5241–5244

    Article  CAS  Google Scholar 

  18. Dey BP, Lahiri SC (2000) Gibbs free energy of transfer of H+ ion from water to urea-water mixtures. Z Phys Chem 214(1):15–26

    Article  CAS  Google Scholar 

  19. Schiffer CA, Dötsch V (1996) The role of protein-solvent interactions in protein unfolding. Curr Opin Biotechnol 7:428–432

    Article  CAS  Google Scholar 

  20. Bennion BJ, Daggett V (2003) The molecular basis for the chemical denaturation of proteins by urea. Proc Natl Acad Sci USA 100(9):5142–5147

    Article  CAS  Google Scholar 

  21. Idrissi A (2005) Molecular structure and dynamics of liquids: aqueous urea solutions. Spectrochim Acta A 61:1–17

    Article  CAS  Google Scholar 

  22. Tobi D, Elber R, Thirumalai D (2003) The dominant interaction between peptide and urea is electrostatic in nature: a molecular dynamics simulation study. Biopolymers 68:359–369

    Article  CAS  Google Scholar 

  23. Caballero-Herrera A et al (2005) Effect of urea on peptide conformation in water: molecular dynamics and experimental characterisation. Biophys J 89:842–857

    Article  CAS  Google Scholar 

  24. Tanford C (1970) Theoretical models for the mechanism of denaturation. Adv Protein Chem 24:1–95

    Article  CAS  Google Scholar 

  25. Ghosh T, Garde S, Garcia AE (2003) Role of backbone hydration and salt-bridge formation in stability of α-helix in solution. Biophys J 85(5):3187–3193

    Article  CAS  Google Scholar 

  26. Vila JA, Ripoll DR, Scheraga HA (2000) Physical reasons for the unusual α-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides. Proc Natl Acad Sci USA 97(24):13075–13079

    Article  CAS  Google Scholar 

  27. Zou Q, Habermann-Rottinghaus SM, Murphy KP (1998) Urea effects on protein stability: hydrogen bonding and the hydrophobic effect. Proteins Struct Funct Genet 31:107–115

    Article  CAS  Google Scholar 

  28. Di Gioia L, Cuq B, Guilbert S (1999) Plasticization of corn gluten meal and characterisation of the blends. Macromol Symp 144:365–369

    Article  CAS  Google Scholar 

  29. Di Gioia L, Cuq B, Guilbert S (1998) Effect of hydrophilic plasticizers on thermomechanical properties of corn gluten meal. Cereal Chem 75(4):514–519

    Article  CAS  Google Scholar 

  30. Pelton JT, McLean LR (2000) Spectroscopic methods for analysis of protein secondary structure. Anal Biochem 277:167–176

    Article  CAS  Google Scholar 

  31. Kong J, Yu S (2007) Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures. Acta Biochim Biophys Sin 39(8):549–559

    Article  CAS  Google Scholar 

  32. Jackson M, Mantsch HH (1995) The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure. Crit Rev Biochem Mol Biol 30(2):95–120

    Article  CAS  Google Scholar 

  33. Rahmelow K, Hubner W (1996) Fourier self-deconvolution: parameter determination and analytical band shapes. Appl Spectrosc 50(6):795–804

    Article  CAS  Google Scholar 

  34. Mizutani Y et al (2003) Effects of water activity and lipid addition on secondary structure of zein in powder systems. J Agric Food Chem 51:229–235

    Article  CAS  Google Scholar 

  35. From NB, Bowler BE (1998) Urea denaturation of staphylococcal nuclease monitired by Fouries transform infrared spectroscopy. Biochemistry 37:1623–1631

    Article  CAS  Google Scholar 

  36. Constantino HR et al (1998) Effect of excipients on the stability and structure of lyophilized recombinant human growth hormone. J Pharm Sci 87(11):1412–1420

    Article  Google Scholar 

  37. Yu P (2005) Protein secondary structures (a-helix and b-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach. Br J Nutr 94:655–665

    Article  CAS  Google Scholar 

  38. Bai S et al (2005) Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy. J Pharm Sci 94(9):2030–2038

    Article  CAS  Google Scholar 

  39. Griffiths PR, Pariente GL (1986) Introduction to spectral deconvolution. Trends Anal Chem 5(8):209–215

    Article  CAS  Google Scholar 

  40. Page GE (1949) Factors influencing the maximum rate of air drying shelled corn in thin layers. Purdue University, West Lafayette

    Google Scholar 

  41. Matsushima N et al (1997) Three-dimensional structure of maize α-zein proteins studied by small-angle X-ray scattering. Biochim Biophys Acta 1339:14–22

    Article  CAS  Google Scholar 

  42. Forato LA, Bicudo TC, Colnago LA (2003) Conformation of α zein in solid state by Fourier Transform IR. Biopolymers 72:421–426

    Article  CAS  Google Scholar 

  43. Nielsen MN et al (2007) Unfolding of B-sheet proteins in SDS. Biophys J 92:3674–3685

    Article  CAS  Google Scholar 

  44. Ibel K et al (1990) Protein-decorated micelle structure of sodium dodecyl-sulfate-protein complexes as determined by neutron scattering. Eur J Biochem 190:311–318

    Article  CAS  Google Scholar 

  45. Lefevre T, Subirade M, Pezolet M (2005) Molecular description of the formation and structure of plasticized globular protein films. Biomacromolecules 6:3209–3219

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Kim L. Pickering.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Pickering, K.L., Verbeek, C.J.R. & Viljoen, C. The Effect of Aqueous Urea on the Processing, Structure and Properties of CGM. J Polym Environ 20, 335–343 (2012). https://doi.org/10.1007/s10924-011-0411-4

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10924-011-0411-4

Keywords

Navigation