Hen's egg white, as well as milk, is one of the most valuable foods especially in protein nutrients. However, egg white has not been used sufficiently for the processed goods as compared with milk and it is of limited use for the industrial applications in these days. One of the reasons for this limitation lies a strong thermal coagulation of egg white. If egg White had lost the ability of thermal coagulation, it would be widely utilized not only in food products but also in many culture mediums for microorganisms or animal tissue cells. For a food industrial utilization of egg white, it is required not to coagulate even if heated at 100°C or 120°C, and moreover even under the presence of salts (NaCl etc.). We have studied to find the preparating method of the non-thermal coagulating protein of egg white. In preceding paper, thermal coagulation was found to reduce by foaming native egg white using a hand mixer or an electric foamer and further affected by several kinds of chemical and physical treatments. However, in the presence of salts, the egg white solution treated with above methods strongly coagulated. So that the effect of partial hydrolysis by acid or alkali on thermal coagulation of egg white was studied. After alkali hydorlysis (0.1N NaOH, 120°C, 15min), the egg white solution did not coagulate at all, but it was inappropriate for the nutrients because microorganism (Eremothecium ashbyii) was never grew in this medium of egg white. So we had to study to find the method of preparation of nutritionally valuable and non-thermal coagulating protein of egg white. In this paper, we were fortunately able to find this preparating method.
Hen's egg white was diluted with water five times, and stirred gently with a glass rod. The white fibrous coagulant of protein emerged in the diluted egg white solution. This coagulant, thought to be a very important factor on the thermal coagulation of egg white, was filtered with a filter paper, and the filtrate was heated at 120°C for 10min in an autoclave. This protein solution was not coagulated by heating at 120°C even under the presence of salt (1% NaCl).
Accordingly, this non-thermal coagulating protein of egg white was thought to be widely used for not only food industry, but also microbiological fermentation.
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