大豆トリプシンインヒビターに関する研究　ＩＩ　　大豆トリプシンインヒビターの熱失活におよぼすタンパク質の影響

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書誌事項

タイトル別名
  • Studies on soybean trypsin inhibitor. Part II. Effects of soybean protein on thermal stability of soybean trypsin inhibitor.
  • ダイズ トリプシン インヒビター ノ ネツ シッカツ ニ オヨボス タンパクシ
  • Studies on Soybean Trypsin Inhibitor Part II
公開日
1988
DOI
  • 10.3136/nskkk1962.35.8_534
公開者
社団法人 日本食品科学工学会

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説明

In the previous paper, it was reported that addition of soybean protein inactivate trypsin inhibitor (TI) remarkably. In this paper, effects of soybean protein on thermal stability of TI was investigated. Changes of thermal stability of TI by adding soybean protein components, such as 7S, 11S and 15S, were examined first of all. As a result, TI heated with llS indicated the remarkable reduction of anti-tryptic activity and thermal stability. 11S has 2 mol of SH group in its molecule, but 7S and 15S hardly have. Accordingly, effects of the SH group on thermal stability of TI were investigated by addition of some amino acids. As a result, only addition of cysteine showed the same effect as the addition of llS. When llS and cysteine were added to TI after modification of the SH with p-chloro-mercuribenzoate (PCMB), and heated, remarkable inactivation of TI was not observed. When TI was heated with PCMB, the absorbancy at 250nm (mercaptide) increasedremarkably. This indicates the reduction of SS bonds in TI molecule, and also suggests that the heat inactivation of TI was due to the exchange reduction of the SH and SS between llS and TI. For above reasons, effects of llS on thermal stability of TI fractions obtained from chinese soybean were compared. TI activities were declined 30-60% with llS against the remaining activities without 11S.

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