TY - JOUR
T1 - Changes in firmness and thermal behavior of ice-stored muscle of jumbo squid (Dosidicus gigas)
AU - Ramírez Olivas, Rosalina
AU - Rouzaud Sández, Ofelia
AU - Haard, Norman F.
AU - Pacheco Aguilar, Ramón
AU - Ezquerra Brauer, Josafat Marina
N1 - Funding Information:
Acknowledgements The authors thank Herlinda Soto Valdez and Jose Luis C rdenas López for their suggestions during the preparation of the manuscript. This study was supported by a UCMEXUS-CONACYT grant given to J.M.E.B and N.F.H.
PY - 2004/9
Y1 - 2004/9
N2 - Changes in firmness, muscle total protease activity, and the thermal behavior of jumbo squid (Dosidicus gigas) were measured throughout 15 days of ice-storage. A significant decrease (p<0.05) in the shear force of raw mantle muscle was observed after 7-days ice-storage. The highest total protease activity detected was 1.24 U/g mantle. The thermograms obtained at day zero showed four transition states. The first three transition states were endothermic and correspond to myosin (50 °C), sarcoplasmic proteins (69 °C), and actin (79 °C). The fourth transition state was exothermic at 107 °C, and was probably associated with protein aggregation. The thermal behavior of the muscle showed a decreasing trend in temperature and enthalpy of transition for myosin, sarcoplasmic proteins, and actin with storage time. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed a change in the myofibrillar protein pattern, which with the shear force, and differential scanning calorimetry data, suggests a partial denaturation of that protein fraction during ice-storage.
AB - Changes in firmness, muscle total protease activity, and the thermal behavior of jumbo squid (Dosidicus gigas) were measured throughout 15 days of ice-storage. A significant decrease (p<0.05) in the shear force of raw mantle muscle was observed after 7-days ice-storage. The highest total protease activity detected was 1.24 U/g mantle. The thermograms obtained at day zero showed four transition states. The first three transition states were endothermic and correspond to myosin (50 °C), sarcoplasmic proteins (69 °C), and actin (79 °C). The fourth transition state was exothermic at 107 °C, and was probably associated with protein aggregation. The thermal behavior of the muscle showed a decreasing trend in temperature and enthalpy of transition for myosin, sarcoplasmic proteins, and actin with storage time. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed a change in the myofibrillar protein pattern, which with the shear force, and differential scanning calorimetry data, suggests a partial denaturation of that protein fraction during ice-storage.
KW - Shear force
KW - Squid
KW - Thermal denaturation
UR - http://www.scopus.com/inward/record.url?scp=21144458662&partnerID=8YFLogxK
U2 - 10.1007/s00217-004-0991-5
DO - 10.1007/s00217-004-0991-5
M3 - Artículo
AN - SCOPUS:21144458662
SN - 1438-2377
VL - 219
SP - 312
EP - 315
JO - European Food Research and Technology
JF - European Food Research and Technology
IS - 4
ER -