Details

Autor(en) / Beteiligte

• Tolano‐Villaverde, Ivan J
• Santacruz‐Ortega, Hisila
• Rivero‐Espejel, Ignacio A
• Torres‐Arreola, Wilfrido
• Suárez‐Jiménez, Guadalupe M
• Márquez‐Ríos, Enrique

Titel

Effect of temperature on the actomyosin‐paramyosin structure from giant squid mantle (Dosidicus gigas)

Ist Teil von

• Journal of the science of food and agriculture, 2019-09, Vol.99 (12), p.5377-5383

Ort / Verlag

Chichester, UK: John Wiley & Sons, Ltd

Erscheinungsjahr

2019

Quelle

Wiley Blackwell Single Titles

Beschreibungen/Notizen

• BACKGROUND The secondary structure of a protein determines its functional properties, such as its gelling capacity. The α‐helix and β‐sheet comprise its main structures. Myofibrillar proteins from jumbo squid are composed mainly of the actomyosin‐paramyosin complex; this complex contains a high percentage of α‐helix, because actin, paramyosin, and myosin constitute 30%, 100%, and 55% of the α‐helix, respectively. It is important to elucidate the role of the secondary structures in the gelation of giant squid proteins as they form gel. The role of the secondary structures in the gelation of giant squid proteins is therefore very important. For this reason, the objective of this work was to evaluate the effect of temperature on the structural behavior of actomyosin‐paramyosin isolate (API) from Dosidicus gigas. RESULTS The unfolding of the API system, which is composed of the actomyosin‐paramyosin complex, was clarified by studying surface hydrophobicity and viscosity. Three characteristic peaks were found, associated with myosin, paramyosin, and actin. Infrared and circular dichroism corroborated the view that API undergoes major structural changes, because it proceeds from mostly an α‐helix structure to 100% β‐sheet. CONCLUSION The structural rearrangement favors gelation by cross‐linking, generating new protein–protein and water‐protein interactions, which create a more stable structure compared to mantle proteins (MP). Likewise, the presence of sarcoplasmic and stromal proteins in D. gigas muscle prevents the unfolding of myofibrillar proteins, favoring gelation by agglomeration, decreasing the ability to trap water and thus its gelling capacity. © 2019 Society of Chemical Industry