Skip to main content
SpringerLink
Log in

Soy protein biopolymers cross-linked with glutaraldehyde

  • Published:
Journal of the American Oil Chemists' Society

Abstract

Biopolymers from soy protein isolate (SPI) crosslinked with glutaraldehyde (GA) were prepared. Surface hydrophobicities of SPI-GA biopolymers and SPI were 4.4 and 11.5, respectively. The solubility profile of SPI was slightly higher than that of SPI-GA biopolymers. Foaming capacities of SPI-GA biopolymers (23 mL) were higher than that of SPI (19 mL), but similar to egg white (22 mL). Foaming stabilities of SPI-GA biopolymers (120 min) were significantly higher than those of SPI (40 min) and egg white (98 min). The emulsifying properties of SPI-GA biopolymers were lower than those of SPI and bovine serum albumin (P>0.05). Tensile strength (TS) and elongation at break (ETB) of SPI-GA biopolymer films were significantly higher than those of glycerol-plasticized soy protein films. TS and ETB of SPI-GA biopolymer films increased with increasing GA concentrations. GA treatment intensified yellowness of SPI-GA biopolymer films. SPI-GA biopolymers may have potential use for biodegradable packaging materials.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Ly, Y., J. Jane, and L.A. Johnson, Soy Proteins as Biopolymers, in Biopolymers from Renewable Resources, edited by D. Kaplan Springer-Verlag, Heidelberg, 1998, pp. 171–200.

    Google Scholar 

  2. Matsuda, S., H. Iwata, N. Se, and Y. Ikada, Bioadhesion of Gelatin Films Cross-linked with Glutaraldehyde, J. Biomed. Mater. Res. 45:20–27 (1999).

    Article  CAS  Google Scholar 

  3. Huang-Lee, L.L.H., D.T. Cheung, and M.E. Nimni, Biomedical Changes and Cytotoxicity Associated with the Degradation of Polymeric Glutaraldehyde-Derived Cross-links, 24:1185–1201 (1990).

    Article  CAS  Google Scholar 

  4. Ziegler, K., I. Schmitz, and H. Zahn, Introduction of New Crosslinks into Proteins, Adv. Exp. Med. Biol. 86A:345–354 (1974).

    Google Scholar 

  5. Feeney, R.E., G. Blankenhorn, and H.B.F. Dixon, Carbonylamine Reactions in Protein Chemistry, Adv. Protein Chem. 29:135–203 (1975).

    Article  CAS  Google Scholar 

  6. Hood, L.L., Collagen in Sausage Casings, in Advances in Meat Research, edited by A.M. Pearson, T.R. Dutson, and A.J. Bailey, Van Nostrand Reinhold Co., Inc., New York, 1987, Vol. 4, pp. 109–129.

    Google Scholar 

  7. Ghorpade, V.M., H. Li, A. Gennadios, and M.A. Hanna, Chemically Modified Soy Protein Films, Trans. ASAE 38:1805–1809 (1995).

    CAS  Google Scholar 

  8. Wolf, W.J., and J.C. Cowan, Soybeans as a Food Source, revised edition, CRC Press, Inc., Cleveland, 1975, pp. 101–105.

    Google Scholar 

  9. Hayakawa, S., and S. Nakai, Relationships of Hydrophobicity and Net Charge to the Solubility of Milk and Soy Protein, J. Food Sci. 50:486–491 (1985).

    Article  CAS  Google Scholar 

  10. Pearce, K.N., and J.E. Kinsella, Emulsifying Properties of Proteins: Evaluation of Turbidimetric Techniques, J. Agric. Food Chem. 26:716–723 (1978).

    Article  CAS  Google Scholar 

  11. Kato, A., A. Takahashi, N. Matsudomi, and K. Kobayashi, Determination of Foaming Properties of Proteins by Conductivity Measurement. J. Food Sci. 48:62–65 (1983).

    Article  CAS  Google Scholar 

  12. ASTM, Standard Test Method for Tensile Properties of Thin Plastic Sheeting, in Annual Book of American Standard Testing Methods, Philadelphia, 1990, D882-90.

  13. Francis, F.J., and F.M. Clydesdale, Food Colorimetry: Theory and Applications, AVI Publishing, Westport, 1975, pp. 171–181.

    Google Scholar 

  14. SAS Institute Inc., SAS/STAT User's Guide, Statistical Analysis System Institute, Cary, NC, 1994.

    Google Scholar 

  15. Darmodaran, S., Structure-Function Relationship of Food Protein, in Protein Functionality in Food Systems, edited by N.S. Hettiarachchy and G.R. Ziegler, Marcel Dekker Inc., New York, 1994, pp. 1–37.

    Google Scholar 

  16. Chtel, J.C., J.L. Cug, and D. Lorient, Amino Acids, Peptides, and Protein, in Food Chemistry, edited by O.W. Fennema, Marcel Dekker Inc., New York, 1985, pp. 245–370.

    Google Scholar 

  17. Yildirim, M., N.S. Hettiarachchy, and U. Kalapathy, Properties of Biopolymers from Cross-Linking Whey Protein Isolate and Soybean 11S Globulin, J. Food Sci. 61:1129–1131 (1996).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Food Protein R&D Center, Texas A&M University, 77843-2476, Texas, College Station

    S. K. Park & K. C. Rhee

  2. Department of Applied Biology and Chemistry, Konkuk University, 133-701, Seoul, Korea

    D. H. Bae

Authors
  1. S. K. Park
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. D. H. Bae
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. K. C. Rhee
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to S. K. Park.

About this article

Cite this article

Park, S.K., Bae, D.H. & Rhee, K.C. Soy protein biopolymers cross-linked with glutaraldehyde. J Amer Oil Chem Soc 77, 879–884 (2000). https://doi.org/10.1007/s11746-000-0140-3

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11746-000-0140-3

Key Words

Search

Navigation