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Krafft temperature and enthalpy of solution of N-acyl amino acid surfactants and their racemic modifications: Effect of the amino acid residue
http://hdl.handle.net/2297/1830
http://hdl.handle.net/2297/183015a7d961-7ce0-49ed-8c21-f0d85a450f97
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
2003CPS281_363.pdf (399.2 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-10-03 | |||||
| タイトル | ||||||
| タイトル | Krafft temperature and enthalpy of solution of N-acyl amino acid surfactants and their racemic modifications: Effect of the amino acid residue | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
Ohta, Akio
× Ohta, Akio× Ozawa, Noriaki× Nakashima, Satoru× Asakuwa, Tsuyoshi× Miyagishi, Shigeyoshi |
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| 提供者所属 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 金沢大学工学部 | |||||
| 書誌情報 |
Colloid and Polymer Science 巻 281, 号 4, p. 363-369, 発行日 2003-04-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0303-402X | |||||
| DOI | ||||||
| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1007/s00396-002-0784-y | |||||
| 出版者 | ||||||
| 出版者 | Springer Verlag | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The Krafft temperatures and the enthalpies of solution of six kinds of N-hexadecanoyl amino acid surfactant (Gly, Ala, Val, Leu, Ile, and Phe) were obtained from both solubility measurements and differential scanning calorimetry. It was shown that the Krafft temperature of N-hexadecanoyl amino acid surfactant increased with decreasing size of the amino acid residue except for the case of phenylalanine. On the other hand, the enthalpy of solution was endothermic and increased with decreasing size of the amino acid residue except for the cases of glycine and phenylalanine. It was found from these results that the D-L interaction was superior to the L-L interaction in solid state of N-hexadecanoyl amino acid surfactant salt for both the alanine and phenylalanine systems. It was suggested by ab initio calculations that the difference of the magnitude of the peptide-peptide hydrogen bonding was the dominant factor for the chiral effect. | |||||
| 著者版フラグ | ||||||
| 出版タイプ | AM | |||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
