Studies on thiaminase of fungi-1-Thiaminase of Lentinus edodes(Berg,)Sing

DOI Web Site PubMed
  • 小野 忠義
    Osaka Agricultural Research Center Department of Applied Chemistry, Faculty of Science and Engineering, Kinki University
  • 川崎 正弘
    Osaka Agricultural Research Center Department of Applied Chemistry, Faculty of Science and Engineering, Kinki University

書誌事項

タイトル別名
  • Studies on Thiaminase of Fungi
  • I. Thiaminase of <i>Lentinus edodes</i> (Berg.) Sing

この論文をさがす

抄録

1. It was confirmed that thiaminase and thermostable factor existed in “Shiitake”, Lentinus edodes (Berg.) Sing. by chemical and microbiological methods. 2. The optimum pH of the enzyme was 6.5, and the optimum temperature 20°. It was inactivated by heating at 45° for 10 minutes. Organic bases such as pyridine, aniline, quinoline and P-aminobenzoic acid activated the activity, as was the case with thiaminase I. Pyrichrome was produced by ferricyanide oxidation in the presence of pyridine. 3. The thermostable factor was active at pH 6 or above, and at 60° or above. 4. The enzyme activity in the fungus was greatest in the gillus, followed by the stipe and the pileus. 5. The content of thiamine in the fungus was greatest in the gillus, followed by the pileus, and the stipe, and about 70% of the vitamin was in the esterified form.

収録刊行物

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ