Freezing denaturation of ovalbumin at acid pH.

摘要: The effects of rapid freezing and thawing at acid pH on the physiochemical properties ovalbumin were examined. At low (around 2), UV difference spectra showed microenvironmental changes around aromatic amino residues; elution curves by gel permeation chromatography decreasing numbers monomers after neutralization. These depended incubation temperature (between -196 -10 degrees C) protein concentration (0.5-10 mg/ml), a incubated -40 C suffered most damage to its conformation. With then C, three four sulfhydryl groups in molecule reacted with 2,2'-dithiodipyridine. CD these secondary structure, but they smaller than those when guanidine hydrochloride was used for denaturation. Supercooling -15 or had little no effect conformation molecule. Thus, irreversible conformational caused under critical condition an pH. arose from partial denaturation resembled thermal neutral