Physicochemical characterization of actomyosin–paramyosin from giant squid mantle (<scp><i>Dosidicus gigas</i></scp>)

Tolano-Villaverde, I. J.; Ocaño‐Higuera, Víctor Manuel; Ezquerra‐Brauer, Josafat Marina; Santos‐Sauceda, Irela; Santacruz‐Ortega, Hisila; Cárdenas-López, José Luis; Rodríguez‐Olibarria, Guillermo; Márquez‐Ríos, Enrique

doi:10.1002/jsfa.8653

Cited by 7 publications

(12 citation statements)

References 43 publications

(66 reference statements)

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“…On the other hand, the SoANS of MP in comparison with API are not clearly observed, because it is a more complex system with the three muscle‐protein groups: sarcoplasmic, stromal, and myofibrillar, which prevent better unfolding due to physical–chemical factors. Mantle protein systems therefore do not demonstrate sharp SoANS peaks compared to the API system.…”

Section: Resultsmentioning

confidence: 99%

“…However, from 45–85 °C, API acquires a greater structural order (absorbance, 0.67–0.73), presenting the most significant changes between 45 and 75 °C. Within this temperature range, the unfolding of myosin and paramyosin occurs . Both of these fold again, forming new interactions that promote greater ordering at 90 °C.…”

Section: Resultsmentioning

confidence: 99%

“…This could be due to the types of proteins and functional groups of each system because API does not contain sarcoplasmic and stromal proteins, whereas MP contains all of the mantle's proteins. It is known that fibrous proteins, such as myosin (38% in API), have a greater capacity to interact with water and other proteins, in addition to the higher concentration of sulfhydryl groups, which could form disulfide bridges, promoting a more rigid system and, in turn, a system with higher viscosity …”

Section: Resultsmentioning

confidence: 99%

“…Finally, the third peak of SoANS is observed at 80 °C. This can be associated with actin unfolding and the exposure of its hydrophobic groups . The reason that there is a greater intensity of SoANS in paramyosin with respect to myosin (55% α ‐helix) and actin (30% α ‐helix) may be due to the fact that paramyosin presents a 100% α ‐helix structure, which is more susceptible to unfolding as a result of the thermal effect, thus exposing a greater number of functional groups, among which hydrophobic amino acids could be found …”

Section: Resultsmentioning

confidence: 99%

“…A heating scan was performed from 10 to 95 °C at a heating rate of 5 °C min −1 . Results were expressed as viscosity (Pa.s) versus temperature (°C) …”

Section: Methodsmentioning

confidence: 99%

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

et al. 2019

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BACKGROUND: The secondary structure of a protein determines its functional properties, such as its gelling capacity. The -helix and -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 -helix, because actin, paramyosin, and myosin constitute 30%, 100%, and 55% of the -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 -helix structure to 100% -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.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…A heating scan was performed from 10 to 95 °C at a heating rate of 5 °C min −1 . Results were expressed as viscosity (Pa.s) versus temperature (°C) …”

Section: Methodsmentioning

confidence: 99%

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

et al. 2019

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The drip loss inhibitory mechanism of nanowarming in jumbo squid (Dosidicus gigas) mantles: protein structure and molecular dynamics simulation

Guo

et al. 2022

J Sci Food Agric

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BACKGROUND The magnetic nanoparticles plus microwave thawing (MNPMT), a new rewarming technology entitled ‘nanowarming’, can serve as an effective method to achieve rapid and uniform thawing, thus reducing drip loss. The purpose of this study was to decipher the drip loss inhibitory mechanism of MNPMT in jumbo squid (Dosidicus gigas) from the perspectives of protein structure and ice crystal recrystallization. A number of different techniques such as dynamic rheology, Raman spectra, intrinsic fluorescence measurement, and ultraviolet (UV) absorption spectra were conducted to analyze myofibrillar protein conformation and stability of jumbo squid. Scanning electron microscopy (SEM) and myofibrillar fragmentation index (MFI) were used to observe the growth of ice crystals. The interaction between magnetic nanoparticles (MNPs) and ice crystals was studied by using molecular dynamic (MD) simulation. RESULTS MNPMT exhibited the highest storage modulus (G') value at 90 °C, suggesting the protein conformation was more stable. The increase in α‐helices, fluorescence intensity and characteristic absorption peak of MNPMT illustrated that MNPMT can effectively maintain the secondary and tertiary structure of the protein. Compared with cold storage thawing (CST) and microwave thawing (MT), the MFI value of MNPMT was significantly decreased (P < 0.01). The result of MD simulation showed that MNPs displayed a tendency to gradually approach the surface of ice crystals, and induced a certain degree of damage to the ice crystal surface, thereby markedly inhibiting ice crystal recrystallization. CONCLUSION MNPMT can reduce the drip loss by keeping the protein conformation stable and inhibiting the recrystallization of ice crystals during the thawing process. © 2022 Society of Chemical Industry.

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Effect of ultrasonication time on the functional properties of giant squid (Dosidicus gigas) mantle protein concentrate

et al. 2019

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Physicochemical characterization of actomyosin–paramyosin from giant squid mantle (Dosidicus gigas)

Abstract: The higher percentage of actin in relation to myosin, the presence of paramyosin, as well as the low content of sulfhydryl groups, could comprise the main causes of the low technological functional property of proteins from D. gigas mantle. © 2017 Society of Chemical Industry.

Cited by 7 publications

References 43 publications

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

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

The drip loss inhibitory mechanism of nanowarming in jumbo squid (Dosidicus gigas) mantles: protein structure and molecular dynamics simulation

Effect of ultrasonication time on the functional properties of giant squid (Dosidicus gigas) mantle protein concentrate

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