TY - JOUR
T1 - Physicochemical changes of pepsin-solubilized and insoluble collagen in jumbo squid (Dosidicus gigas) muscle after cooking process
AU - Ezquerra-Brauer, Josafat M.
AU - Márquez-Ríos, Enrique
AU - López-Corona, Betzabe E.
AU - Ocaño-Higuera, Víctor M.
AU - Ramírez-Guerra, Hugo E.
AU - Cota-Arriola, Octavio
AU - Torres-Arreola, Wilfrido
PY - 2018/1/1
Y1 - 2018/1/1
N2 - © 2018 Josafat M. Ezquerra-Brauer Enrique Márquez-Ríos Betzabe E. López-Corona Víctor M. Ocaño-Higuera Hugo E. Ramírez-Guerra Octavio Cota-Arriola and Wilfrido Torres-Arreola. Collagen is the major connective tissue (CT) protein and one of the main constituents of the jumbo squid (Dosidicus gigas). Therefore, physicochemical changes of pepsin-solubilized collagen (PSC) and insoluble collagen (IC) were studied after cooking (100°C/30 min) of muscle (mantle, fins, and arms). Different pyridinoline (Pyr) contents (the major cross-linking molecule in collagen fibers) were found in the fresh muscle of the three anatomical regions. After the cooking process, a decrease from 10 to 30% in the thermal resistance of collagen was observed, depending on the anatomical region and fraction evaluated. Furthermore, the electrophoretic profile, Fourier transform infrared (FTIR) spectroscopy, and the amino-acid profile revealed that structural changes occurred in the two different collagen fractions caused by the thermal process, and the changes were greater in the mantle. Under the conditions applied in this study, collagen fractions from the squid arms showed more stability during the cooking process due to the high cross-linking degree of their fibers.
AB - © 2018 Josafat M. Ezquerra-Brauer Enrique Márquez-Ríos Betzabe E. López-Corona Víctor M. Ocaño-Higuera Hugo E. Ramírez-Guerra Octavio Cota-Arriola and Wilfrido Torres-Arreola. Collagen is the major connective tissue (CT) protein and one of the main constituents of the jumbo squid (Dosidicus gigas). Therefore, physicochemical changes of pepsin-solubilized collagen (PSC) and insoluble collagen (IC) were studied after cooking (100°C/30 min) of muscle (mantle, fins, and arms). Different pyridinoline (Pyr) contents (the major cross-linking molecule in collagen fibers) were found in the fresh muscle of the three anatomical regions. After the cooking process, a decrease from 10 to 30% in the thermal resistance of collagen was observed, depending on the anatomical region and fraction evaluated. Furthermore, the electrophoretic profile, Fourier transform infrared (FTIR) spectroscopy, and the amino-acid profile revealed that structural changes occurred in the two different collagen fractions caused by the thermal process, and the changes were greater in the mantle. Under the conditions applied in this study, collagen fractions from the squid arms showed more stability during the cooking process due to the high cross-linking degree of their fibers.
U2 - 10.1080/10942912.2018.1477159
DO - 10.1080/10942912.2018.1477159
M3 - Article
SP - 821
EP - 834
JO - International Journal of Food Properties
JF - International Journal of Food Properties
SN - 1094-2912
ER -