Effect of curing temperature on properties and solvent welding strength of ovalbumin

Abstract

Effect of curing temperature on properties of ovalbumin has been investigated. Functional basis, crosslinking degree, tensile strength, and hardness increases with rising curing temperature. The increase of visible transmittance and the decrease of absorption accompany with increasing wavelength. The absorptive peak shows at 440-450 nm and the wavelength of the absorptive peak increases with the rising curing temperature. The relationship of joint strength with solvent welded joints of ovalbumin to their microstructure is also investigated. Ovalbumin can promote joint strength after the treatment of distilled water and curing. Comparing joint strength with fracture morphology, the smoother fracture surface morphology is related to the maximum tensile and shear joint strength, respectively. The joint strength is increasing with curing temperature and compressive stress, and the joint strength of treatment with 150 C curing temperature and 0.12 kgf/mm 2 compressive stresses are larger than its original tensile fracture strength of cured ovalbumin at same curing temperature.

The Glass Transition Temperature and Temperature Dependence of Activation Energy of Viscous Flow of Ovalbumin

“…Study of ovalbumin by X-ray crystallography showed that the ovalbumin molecule is approximately a tri-axial ellipsoid with overall dimensions 74.55 nm (Stein et al, 1991). Ovalbumin has been the subject of many physicochemical studies by using different experimental techniques (Kang et al, 2014;Yang et al, 2013;Lin et al, 2012;Khodarahmi et al, 2009;Monkos, 2007;Tani et al, 2004;Renault et al, 2002;Ikeda & Nishinari, 2001;Monkos, 2000 and references therein). As a result many of its physicochemical properties is well known and ovalbumin is widely used as a standard protein in various biophysical studies.…”