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Effect of temperature on the actomyosin‐paramyosin structure from giant squid mantle (Dosidicus gigas)
Journal of the science of food and agriculture, 2019-09, Vol.99 (12), p.5377-5383
Tolano‐Villaverde, Ivan J
Santacruz‐Ortega, Hisila
Rivero‐Espejel, Ignacio A
Torres‐Arreola, Wilfrido
Suárez‐Jiménez, Guadalupe M
Márquez‐Ríos, Enrique
2019
Volltextzugriff (PDF)
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
Sprache
Englisch
Identifikatoren
ISSN: 0022-5142
eISSN: 1097-0010
DOI: 10.1002/jsfa.9797
Titel-ID: cdi_proquest_miscellaneous_2231908306
Format
–
Schlagworte
Actin
,
Actomyosin
,
Actomyosin - chemistry
,
actomyosin‐paramyosin
,
Animals
,
Circular dichroism
,
Decapodiformes - chemistry
,
Dichroism
,
Dosidicus gigas
,
Gelation
,
Giant squids
,
Hydrophobic and Hydrophilic Interactions
,
Hydrophobicity
,
infrared
,
Mantle
,
Muscles
,
Myosin
,
Myosins - chemistry
,
Organic chemistry
,
Protein interaction
,
Protein structure
,
Protein Structure, Secondary
,
Protein Unfolding
,
Proteins
,
Seafood - analysis
,
Secondary structure
,
Structural behavior
,
Temperature
,
Temperature effects
,
Tropomyosin - chemistry
,
Viscosity
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