2004年
The solubilization of unheated cattle achilles tendon with actinidin under neutral and acidic conditions
Food Science and Technology Research
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- 巻
- 10
- 号
- 1
- 開始ページ
- 35
- 終了ページ
- 37
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.3136/fstr.10.35
- 出版者・発行元
- S. Karger AG
The solubilization of cattle achilles tendon with actinidin was investigated under neutral and acidic conditions. 1.43 to 1.92 and 0.97 to 3.19% of collagen were solubilized by treating the cattle achilles tendon with actinidin at 20°C at pH 6.0 and 3.3, respectively. Furthermore, SDS-polyacrylamide gel electrophoresis of reaction mixtures with actinidin demonstrated that actinidin degraded the tendon into collagen subunit chain, β- and α-chain and peptide fragments of various sizes at 20°C at pH 6.0 and 3.3. These results indicated that actinidin could solubilize the insoluble collagen in unheated cattle achilles tendon at 20°C at pH 6.0 and 3.3 and that a large proportion of the resulting peptide fragments by actinidin seemed to be actinidin digests against elastin with a small contribution of hydroxyproline.
- リンク情報
- ID情報
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- DOI : 10.3136/fstr.10.35
- ISSN : 1344-6606
- SCOPUS ID : 2342631166