アルカリゲル化卵白の溶解性とプロテアーゼによる分解性

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タイトル別名
  • Studies on the Solubility and the Digestibility by Proteases of the Alkali Gelled Egg White
  • アルカリ ゲルカ ランパク ノ ヨウカイセイ ト プロテアーゼ ニヨル ブンカ

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The solubility and the digestibility by proteases of the alkali gelled egg white was determined in order to investigate food qualities of pidan. One hundred mg of freeze dried alkali gelled egg white was dispersed in 10ml of different solvents and shaken at 30°C for 60 min. The undissolved protein was removed by filtration and the protein in the filtrate was determined according to LOWRY et al. In acid or neutral pH range, the alkali gelled egg white was hardly soluble. Its solubility did not increase by adding 1M sodium chloride or by heating at 75°C for 10min, but increased slightly by the addition of 6M guanidine hydrochloride. In alkaline pH range, the alkali gelled egg white was generally more soluble than in acid or neutral solutlon, and the solubility was increased by the addition of 2-6M urea or 6M guanidine hydrochloride and by heating at 75°C for 10min. Freeze dried alkali gelled egg white and heat coagulated egg white were dispersed in 0.1M phosphate or citrate buffer and digested by pepsin (pH 2.4), molsin (protease produced from Aspergillus Saitoi, pH2.4), nagarse (pH7.0), pronase (pH7.0) or trypsin (pH8.0) at 30°C for 120min. The trichloroacetic acid soluble hydrolysis products were determined by FOLIN's method. Alkali gelled egg white was more easily digested than heat coagulated or untreated one by trypsin, nagarse, or pronase. The improvement of the digestibility of alkali treated egg white may result from the inactivation of trypsin inhibitor or ovoinhibitor in egg white by alkali. Alkali gelled egg white was also more digestible than untreated one by pepsin or molsin.

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