Rheological Properties of Mixed Agar Gels and Collagen-Peptide from Tilapia Scales
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- Onodera Makoto
- School of Human Science and Environment, University of Hyogo
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- Fukae Ryohei
- School of Human Science and Environment, University of Hyogo
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- Eguchi Satomi
- School of Human Science and Environment, University of Hyogo
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- Nishinari Katsuyoshi
- Graduate School of Human Life Science, Osaka City University
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- Yoshimura Miki
- School of Human Science and Environment, University of Hyogo
Bibliographic Information
- Other Title
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- 寒天と魚鱗由来コラーゲンペプチド混合ゲルから調製したゲルの物性
- カンテン ト ギョリン ユライ コラーゲンペプチド コンゴウ ゲル カラ チョウセイ シタ ゲル ノ ブッセイ
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Abstract
The effects of the concentration and molecular weight (Mw) of collagen-peptide (CP) from tilapia scales on the rheological and thermal properties of agar gel (AG) were examined by gel permeation chromatography, dynamic viscoelasticity, rupture properties, syneresis and differential scanning calorimetry. Three kinds of CP from tilapia scales (CP1000, CP5000 and CP10000) with Mw=7.4×102, 4.5×103 and 1.0×104, respectively, were investigated. The results showed that CP1000 had the highest rupture stress, Young’s modulus and syneresis of the AGs tested. For CP5000 and CP10000, rupture stress and Young’s modulus were lower, syneresis was repressed and enthalpy was decreased. Therefore, it was suggested that higher molecular weight CP hindered cross-linking formation in AGs. Also, a comparison of CP from porcine skin and tilapia scales suggested that viscosity and enthalpy of CP solutions and gel strength were influenced by molecular weight and amino acids composition.
Journal
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- Nippon Shokuhin Kagaku Kogaku Kaishi
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Nippon Shokuhin Kagaku Kogaku Kaishi 59 (1), 22-33, 2012
Japanese Society for Food Science and Technology
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Keywords
Details 詳細情報について
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- CRID
- 1390001206409178112
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- NII Article ID
- 10030333647
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- NII Book ID
- AN10467499
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- ISSN
- 18816681
- 1341027X
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- NDL BIB ID
- 023402942
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- Text Lang
- ja
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed