Changes in Casein and Egg Albumin due to Reactions with Oxidizing Methyl Linoleate in Dehydrated Systems
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概要
- 論文の詳細を見る
Casein and egg albumin were allowed to react with methyl linoleate (ML) at a relative humidity (RH) of 0% or 80% at 50°C for 10 days (protein : ML=1:0.2 or 1:1, w/w). Changes in the molecular sizes of the reacting proteins were examined by gel filtration and gel electrophoresis. Both proteins showed similar changes, whereas the reaction at RH 80% (protein: ML=1:1) resulted in insolubilization because of polymerization. Changes in the amino acid residues of the reacting proteins were investigated after acid (6 N HCl) and enzymatic (pepsin-pancreatin, followed by aminopeptidase-prolidase) hydrolyses. Insignificant changes were observed in the amino acid composition of proteins reacted at RH 0%. After reaction at RH 80% (protein: ML=1:1), Lys, His and Met were the only amino acids affected. The percentage loss of these amino acids after acid hydrolysis was Lys (22%), His (41%), Met (9%) for casein and Lys (22%), His (31%), Met (1%) for egg albumin. This percentage loss after enzymatic hydrolysis was Lys (41%), His (49%), Met (94%) for casein and Lys (37%), His (42%), Met (88%) for egg albumin. Some differences between our results and other researchers were also discussed.
- 社団法人 日本農芸化学会の論文
著者
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Matoba Teruyoshi
Research Institute For Food Science Kyoto University
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YOSHIDA Hozumi
Food Technical High School of Osaka Prefecture
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YONEZAWA Daizo
Research Institute for Food Science, Kyoto University
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