Effects of nanowarming on water holding capacity, oxidation and protein conformation changes in jumbo squid (Dosidicus gigas) mantles

Zhu, Wenhui; Li, Yue; Bu, Ying; Lǐ, Jiànróng; Li, Xuepeng

doi:10.1016/j.lwt.2020.109511

Cited by 19 publications

(23 citation statements)

References 39 publications

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“…SDS-PAGE was used to characterize the effect of dehydration treatment on the degradation of MFP by determining the molecular weight ( Figure 5 D). The appearance of myosin heavy chains (MHC, bout 200 kDa) may be due to cross-linking and aggregation of myofibril proteins, and the appearance of myosin light chains (MLC, 14–21 kDa) may be caused by the degradation of heavy chains [ 39 ]. As shown in Figure 5 D, the protein molecules of the croaker samples frozen and dehydrated for 18 h did not change significantly.…”

Section: Resultsmentioning

confidence: 99%

Exploring the Effect of Dehydration on Water Migrating Property and Protein Changes of Large Yellow Croaker (Pseudosciaena crocea) during Frozen Storage

Tan

Xie

2021

Foods

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This study aimed to explore the effect of dehydration on the water migrating property and protein changes of large yellow croaker during frozen storage. A freeze-dryer was used to accelerate experiments, which was isolated from oxygen and excluded the effects of protein oxidation. After dehydration time (3, 9, 18, and 30 h) for both fast- and slow-freezing samples, the results showed that the ice sublimation of samples containing small ice crystals was faster than that of samples containing large ice crystals in the early stages of dehydration, but in the latest stage, there was an opposite trend. The results indicated that dehydration reduced the water freedom degrees and water–protein interaction. At the same time, dehydration had a significant effect on protein secondary and tertiary structures. The significant increase in surface hydrophobicity and particle size indicated that dehydration exacerbated myofibrillar protein aggregation. The ΔH1 values (from 1.275 to 0.834 J/g for slow-freezing group and from 1.129 to 0.855 J/g for fast-freezing group) decreased gradually as the dehydration time extended, indicating the decrease in protein thermal stability. Additionally, significant protein degradation occurred when the water content of the sample decreased to a certain level. This study showed that ice crystal size had an important effect on the rate of ice sublimation, and the occurrence of dehydration during frozen storage accelerated the water loss and the decrease in protein stability.

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Section: Resultsmentioning

confidence: 99%

Exploring the Effect of Dehydration on Water Migrating Property and Protein Changes of Large Yellow Croaker (Pseudosciaena crocea) during Frozen Storage

Tan

Xie

2021

Foods

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“…6(A), CST and MT formed a large number of uneven pores, MNPMT had smaller pores, and these results indicated that MNPMT can inhibit the growth and recrystallization of ice crystals during the thawing process, which is consistent with the previous results of light microscopy. 10 Myofibrillar fragmentation index (MFI) MFI value was performed to evaluate the integrity of myofibrils and skeletal proteins in muscle cell. 35 The higher the MFI value is, the worse the integrity of the internal structure of myofibrils.…”

Section: Analyses Of Protein Conformation Dynamic Rheologicalmentioning

confidence: 99%

“…Magnetic nanoparticles (MNPs) can make the thawing process uniform, and also can inhibit the recrystallization of ice crystals to some extent during the thawing process. 10 For instance, Cao et al found that both MNPMT and magnetic nanoparticles plus far-infrared thawing (MNPFT) both resulted in stable protein secondary and tertiary structures with better WHC. 11 MNPMT utilizes the superparamagnetic traits and biocompatibility of MNPs to facilitate uniform rewarming for the frozen biomaterials.…”

Section: Introductionmentioning

confidence: 99%

“…12 Zhu et al revealed that the effects of MNPMT on WHC and protein oxidation in jumbo squid. 10 However, the changes in protein structure and the mechanism by which MNPs can possibly inhibit the growth and recrystallization of ice crystals remains unclear during the thawing process. Furthermore, it is worth noting that the growth pattern of ice crystals is extremely difficult to observe directly.…”

Section: Introductionmentioning

confidence: 99%

“…In our previous studies, we have revealed that the magnetic nanoparticles plus microwave thawing (MNPMT), that is nanowarming, can potentially serve as an effective method to achieve a fast and uniform rate of thawing for frozen jumbo squid. Magnetic nanoparticles (MNPs) can make the thawing process uniform, and also can inhibit the recrystallization of ice crystals to some extent during the thawing process 10 . For instance, Cao et al .…”

Section: Introductionmentioning

confidence: 99%

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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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Evaluating the effects of graphene nanoparticles combined radio‐frequency thawing on the physicochemical quality and protein conformation in hairtail (Trichiurus lepturus) dorsal muscle

Tian,

Gu,

et al. 2024

J Sci Food Agric

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BACKGROUNDThawing process is an essential step for a frozen marine fish. This study aimed to investigate the effects of graphene magnetic nanoparticles combined radio‐frequency thawing methods on frozen hairtail (Trichiurus lepturus) dorsal muscle. Seven thawing methods were used: air thawing (AT), 4°C cold storage thawing (CT), water thawing (WT), radio‐frequency thawing (RT), radio frequency thawing combined with graphene nanoparticles (G‐RT), radio frequency thawing combined with graphene oxide nanoparticles (GO‐RT), and radio‐frequency thawing combined with graphene magnetic nanoparticles (GM‐RT). The thawing loss and centrifugal loss, electric conductivity (EC), TVB‐N, thiobarbituric acid reactive substances (TBARs), and colour of thawed hairtail dorsal muscle were determined. The carbonyl content, total sulfhydryl groups, Ca2+‐ATPase activity, raman spectroscopy measurements, and fourier transform infrared (FTIR) spectrometry measurements were determined using myofibrillar extracted from the dorsal muscle of hairtail. The water distribution was determined by using low‐field NMR techniques.RESULTSThe results demonstrated that the RT, G‐RT, GO‐RT, and GM‐RT could significantly shorten the thawing time. Moreover, GO‐RT and GM‐RT efficiently preserved the colour of fish dorsal muscle and reduced the impact of thawing on fish quality by reducing lipid and protein oxidation. Meanwhile, the myofibrillar protein structure thawed by GO‐RT and GM‐RT were more stable and had a more stable secondary structure, which maintained strong systemic stability while slowing down protein oxidation.CONCLUSIONThe results showed that GO‐RT and GM‐RT can significantly improve the thawing efficiency while effectively maintaining and improving the color and texture of thawed fish, slowing down the oxidation of proteins and lipids, and maintaining good quality of thawed fish meat.This article is protected by copyright. All rights reserved.

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Effects of nanowarming on water holding capacity, oxidation and protein conformation changes in jumbo squid (Dosidicus gigas) mantles

Cited by 19 publications

References 39 publications

Exploring the Effect of Dehydration on Water Migrating Property and Protein Changes of Large Yellow Croaker (Pseudosciaena crocea) during Frozen Storage

Exploring the Effect of Dehydration on Water Migrating Property and Protein Changes of Large Yellow Croaker (Pseudosciaena crocea) during Frozen Storage

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

Evaluating the effects of graphene nanoparticles combined radio‐frequency thawing on the physicochemical quality and protein conformation in hairtail (Trichiurus lepturus) dorsal muscle

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