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Triple helical structure of acid‐soluble collagen derived from Nile tilapia skin as affected by extraction temperature
Author(s) -
Thuanthong Mantaka,
Sirinupong Nualpun,
Youravong Wirote
Publication year - 2016
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.7572
Subject(s) - extraction (chemistry) , acetic acid , circular dichroism , yield (engineering) , fourier transform infrared spectroscopy , chemistry , nile tilapia , biomaterial , imino acid , chromatography , nuclear chemistry , biochemistry , materials science , amino acid , fish <actinopterygii> , oreochromis , organic chemistry , biology , proline , chemical engineering , fishery , engineering , metallurgy
BACKGROUND Fish skin has become a new source of collagen. It is usually extracted at low temperature. Increasing the extraction temperature can increase the collagen yield. However, high temperature might cause degradation of the triple helical structure of collagen, which is related to its functional biomaterial. This work thus aimed to investigate the effect of extraction temperature on the extraction efficiency and characteristics of acid‐soluble collagen ( ASC ), particularly its triple helical structure. RESULTS ASC was extracted at 5 ± 1, 15 ± 1 and 25 ± 1 °C for 0–24 h with 0.3 or 0.5 mol L −1 acetic acid. The results showed that extraction with 0.5 mol L −1 acetic acid gave a higher extraction efficiency than that in 0.3 mol L −1 acetic acid ( P < 0.5). Extraction at 25 ± 1 °C for 5 h with 0.5 mol L −1 acetic acid gave a higher extraction efficiency (73.73 ± 1.28%), which is higher than that of 5 ± 1 °C by about 1.7‐fold. All ASC obtained were identified as type I collagen and showed similar physicochemical properties. CONCLUSION The results showed that extraction temperature strongly affected extraction efficiency. Extraction at 25 °C did not affect the triple helical structure, which was confirmed by the results of Fourier transform infrared, circular dichroism spectrum and collagen self‐assembly. © 2015 Society of Chemical Industry