- 【Updated on May 12, 2025】 Integration of CiNii Dissertations and CiNii Books into CiNii Research
- Trial version of CiNii Research Knowledge Graph Search feature is available on CiNii Labs
- Suspension and deletion of data provided by Nikkei BP
- Regarding the recording of “Research Data” and “Evidence Data”
-
- TAKAYAMA Naoko
- 平安女学院短期大学
-
- ENDO Kinji
- 奈良女子大学家政学部
-
- YAMAMOTO Yoshio
- 奈良女子大学家政学部
Bibliographic Information
- Other Title
-
- あわび肉コラーゲンとそのテクスチャーについて
- アワビ ニク コラーゲン ト ソノ テクスチャー ニ ツイテ
Search this article
Description
The identification of a collagen in abalone muscles was made. The changes in abalone collagen and the texture of abalone muscles during heating were investigated.<BR>Results obtained are summarized as follows : <BR>1) There was a larger NaOH-insoluble fraction in abalone muscles than in other kinds of muscles and about 80% of it was a collagen.<BR>2) The abalone collagen was gradually gelatinized upon being heated at 100°C, but the amount gelatinized in 3 hour heating was only 7% of the collagen used.<BR>3) On heating at 100°C orange-G-binding site and safranin-O-binding site of the collagen rapidly increased to some extent, and ammonia was gradually generated from the collagen. On these bases it was assumed that, on heating at 100°C, collagen fiber rapidly unfolded and amide group was degraded.<BR>4) Of various muscles tested, only abalone muscle became soft on heating. This characteristic phenomenon was assumed to correlate with the unfolding and the degradation of amide group in abalone collagen.
Journal
-
- Journal of Home Economics of Japan
-
Journal of Home Economics of Japan 23 (6), 376-379, 1972
The Japan Society of Home Economics
- Tweet
Details 詳細情報について
-
- CRID
- 1390001206330307584
-
- NII Article ID
- 130003868372
-
- NII Book ID
- AN00041468
-
- ISSN
- 18847870
- 04499069
-
- NDL BIB ID
- 9325416
-
- Data Source
-
- JaLC
- NDL Search
- CiNii Articles
-
- Abstract License Flag
- Disallowed