Changes in Molecular Size and Chemical Properties of Gelatin Caused by the Reaction with Oxidizing Methyl Linoleate
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概要
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Gelatin, soy protein, lysozyme, succinyl-casein and succinyl-egg albumin were allowed to react with methyl linoleate (ML) at a relative humidity (RH) of 0% at 50°C for 7 days (protein : ML=1:1). Gel filtration indicated that only gelatin was extensively fragmented. The gelatin was then incubated with ML under various conditions, and changes in the molecular sizes, the gel forming abilities and the chemical characteristics were investigated. The fragmentation of gelatin was increased by decreasing the RH and with the increase in the ratio of ML to protein. The melting point of gel in heating and cooling gelatin was decreased by increasing the fragmentation. The contents of amide and carbonyl groups increased and that of amino group decreased as the reaction progressed at RH 0%, but no change in C-terminal amino acids was observed. Following the reaction at RH 0%, many kinds of amino acid residues of gelatin were damaged, although in our previous paper[Matoba et al., Agric. Biol. Chem., 46, 979 (1982)] such was not detected in casein and egg albumin. From the above results, we conclude that gelatin is susceptible to fragmentation by reaction with oxidizing lipids and one possible mechanism of the degradationmay be the-N-C-scission ofpeptide bonds as proposed by Zirlin and Karel [J. Food Sci., 34, 160(1969)]. Complex reactions other than this scission may also occur.
- 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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KURITA Osamu
Research Institute for Food Science, Kyoto University
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YONEZAWA Daizo
Research Institute for Food Science, Kyoto University
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