Abstract
An investigation was conducted on the adhesive and water-resistance properties of soy protein isolates that were modified by varying solutions of urea (1, 3, 5, and 8 M) or guanidine hydrochloride (GH) (0.5, 1, and 3 M) and applied on walnut, cherry, and pine plywoods. Soy proteins modified by 1 and 3 M urea showed greater shear strengths than did unmodified protein. The 3 M urea modification gave soy protein the highest shear strength. Soy proteins modified with 0.5 and 1 M GH gave greater shear strengths than did the unmodified protein. The 1 M GH-modified soy protein gave the highest shear strength. Compared to the unmodified protein, the modified proteins also exhibited higher shear strengths after incubating with two cycles of alternating relative humidity, zero delamination, and higher remaining shear strengths after three cycles water soaking and drying. These results indicate that soy proteins modified with urea and GH enhance water resistance as well as adhesive strength. Secondary structures of globule proteins may enhance adhesion strength, and the exposure of hydrophobic amino acids may enhance water resistance. Proteins modified by 3 M urea or 1 M GH may have higher content of secondary structure and more exposed hydrophobic amino acids, compared with other modifications or unmodified proteins.
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References
Lambuth, A.L., Protein Adhesives for Wood, in Advanced Wood Adhesive Technology, edited by A. Pizzi and K.L. Mittal, Marcel Dekker, Inc., New York, 1994, pp. 259–281.
Johnson, L.A., D.J. Myers, and D.J. Burden, Early Uses of Soy Protein in Far East, INFORM 3:282–284 (1984).
O’Brien, D.J., and J.A. Olofsson, Phenol Leachability from Phenolic Resin Materials, Abstract in Proceedings of Industrial Waste Conference, Engineering Information, Inc., Hoboken, 1980, pp. 155–159.
Henderson, J.T., Volatile Emissions from the Curing of Phenolic Resins, Tappi J. 62:93–96 (1979).
Myers, D.J., Industrial Applications for Soy Protein and Potential for Increased Utilization, Cereal Foods World 38:355–358 (1993).
Wolf, W.J., Soybean Proteins: Their Functional, Chemical, and Physical Properties, J. Agric. Food Chem. 18:969–976 (1970).
Kinsella, J.E., Functional Properties of Soy Proteins for Food Applications, J. Am. Oil Chem. Soc. 56:242–258 (1979).
Wu, Y.V., and G.E. Inglet, Denaturation of Plant Proteins Related to Functionality and Food Applications. A Review, J. Food Sci. 39:218–225 (1974).
Hettiarachchy, N.S., U. Kalapathy, and D.J. Myers, Alkali-Modified Soy Protein with Improved Adhesive and Hydrophobic Properties, J. Am. Oil Chem. Soc. 72:1461–1465 (1995).
Sun, X., and K. Bian, Shear Strength and Water Resistance of Modified Soy Protein Adhesives, Ibid. 76:977–980 (1999).
Tanford, C., Protein Denaturation, in Advanced in Protein Chemistry, edited by C.B. Anfinsen, M.L. Anson, J.T. Edsall, and F.M. Richards, Academic Press, Inc, New York, 1968, pp. 121–283.
Chandra, B.R.S., A.G.A. Rao, and M.S.N. Rao, Effect of Temperature on the Conformation of Soybean Glycinin in 8 M Urea and 6 M Guanidine Hydrochloride Solution, J. Agrie. Food Chem. 32:1402–1405 (1984).
Tanford, C., K. Kawahara, and S. Lapanie, Proteins as Random Coils, J. Am. Chem. Soc. 89:729–734 (1967).
Tanford, C., K. Kawahara, S. Lapanie, T. Hooker, and M. Zarlengo, Protein as Random Coils. III. Optical Rotatory Dispersion in 6M Guanidine Hydrochloride, Ibid. 89:5023–5028 (1967).
Pace, C.N., The Stability of Globular Proteins, CRC Crit. Rev. Biochem 3:1–43 (1975).
ASTM Standards for Wood and Adhesives, American Society of Testing and Materials, Philadelphia, 1981, pp. 407–409, Methods D-1183.
Kalapathy, U., N.S. Hettiarachchy, D. Myers, and M.A. Hanna, Modification of Soy Proteins and Their Adhesive Properties on Woods, J. Am. Oil Chem. Soc. 72:507–510 (1995).
Mackay, C.D., Good Adhesive Bonding Starts with Surface Preparation, Adhesive Age 41:30–32 (1998).
Ptitsyn, O.B., Protein Folding: Hypotheses and Experiments, J. Protein Chem. 6:273–293 (1987).
Wang, K.P., and C.D. Tanford, Denaturation of Bovine Carbonic Anhydrase B by Guanidine Hydrochloride, J. Biol. Chem. 248:8518–8523 (1973).
Nazaka, M., K. Kuwajima, K. Nitta, and S. Sugai, Detection and Characterization of the Intermediate on the Folding Pathway of Human Alpha-Lactalbuman, Biochem. 17:3752–3758 (1978).
Dolgikh, D.A., R.I. Gilmanshin, E.V. Brazhnikov, V.E. Bychkova, G.V. Semisotnov, S.Y. Venyaminov, and O.B. Ptitsyn, Alpha-Lactalbumin: Compact State with Fluctuating Tertiary Structure? FEBS Lett. 136:311–315 (1981).
Dolgikh, D.A., A.R. Kolomietz, I.A. Bolotina, and O.B. Ptitsyn, ‘Molten-Globule’ State Accumulates in Carbonic Anhydrase Folding, Ibid. 165:88–92 (1984).
Pfeil, W., V.E. Bychkova, and O.B. Ptitsyn, Physical Nature of the Phase Transition in Globular Proteins, FEBS Lett. 198:287–290 (1986).
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Huang, W., Sun, X. Adhesive properties of soy proteins modified by urea and guanidine hydrochloride. J Amer Oil Chem Soc 77, 101–104 (2000). https://doi.org/10.1007/s11746-000-0016-6
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DOI: https://doi.org/10.1007/s11746-000-0016-6