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Preparation, characterisation and structure of rabbit (Hyla rabbit) skin gelatine
Author(s) -
Yu Wei,
Wang Xuemeng,
Ma Liang,
Li Hongjun,
He Zhifei,
Zhang Yuhao
Publication year - 2016
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13012
Subject(s) - rabbit (cipher) , hydroxyproline , chemistry , amino acid , amino acid analysis , gelatin , chromatography , lysine , proline , biochemistry , statistics , mathematics
Summary Rabbit skin was used as a raw material to prepare gelatine. The yield of extracted rabbit skin gelatine was 8.49 ± 0.91% based on a wet weight basis. The bloom strength of 6.67% rabbit gelatine was 457.57 ± 3.302 g, and its gelling and melting temperatures were 27.8 and 34.4 °C, respectively. Sodium dodecyl sulphate‐polyacrylamide gel electrophoresis analysis demonstrated that the content of the subunit components (α chain, β and γ components) of the rabbit skin gelatine achieved 97.915%. Amino acid composition analysis indicated that the total amino acid contents (proline plus hydroxyproline) in the rabbit gelatine were 222 residues per 1000 residues. The high content of the subunit components and amino acids could contribute to the gelatine's suitable gel properties. Rabbit gelatine had nearly all of the characteristic absorption peaks of collagen from rabbit skin, and the loss of the triple helical structure and damage to part of the hydrogen bonds occurred during the conversion of collagen to gelatine.

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