The effect of egg white protein and β-cyclodextrin mixture on structural and functional properties of silver carp myofibrillar proteins during frozen storage

Walayat, Noman; Xiong, Zhouyi; Xiong, Hanguo; Moreno, Helena M.; Nawaz, Asad; Niaz, Nadia; Chun, Ho-Kyung; Taj, Muhammad Imran; Mushtaq, Bilal Sajid; Khalifa, Ibrahim

doi:10.1016/j.lwt.2020.109975

Cited by 58 publications

(34 citation statements)

References 34 publications

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“…In addition, these results are totally in agreement with Zhang et al [ 36 ] who reported that addition of KC (3%) significantly restricted the increase in dityrosine content than the KC (1%) and control shrimp protein samples during frozen storage. Meanwhile, these results, which indicated the formation of new cross-linking in shrimp proteins after the incorporation of oligosaccharides are consistent with the Walayat et al [ 9 ]. Moreover, Colombo, et al [ 37 ] stated that the MP oxidative changes increased in similar ways, such as increased dityrosine, formation of disulfide bindings and protein denaturation.…”

Section: Resultssupporting

confidence: 91%

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Ovalbumin and Kappa-Carrageenan Mixture Suppresses the Oxidative and Structural Changes in the Myofibrillar Proteins of Grass Carp (Ctenopharyngodon idella) during Frozen Storage

et al. 2021

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This study was done to analyze the cryoprotective influence of ovalbumin (OVA) with kappa-carrageenan (KC) in grass carp myofibrillar proteins during frozen storage. Ca2+-ATPase activity of MP was significantly reduced due to protein denaturation and showed a direct association with decreased sulphydryl (SH) contents and tertiary structural properties. Besides that, an increase in carbonyl, surface hydrophobicity, and dityrosine contents was observed. The addition of OVA-KC significantly restricted the decline in Ca2+-ATPase and SH groups, which were further confirmed by the retarded increase in carbonyls. Furthermore, the addition of OVA-KC increased the stability of α-helix contents. Moreover, MP treated with 6% OVA-KC also improved intermolecular interaction forces linked with gelling and water holding properties of MP. Therefore, it can be concluded that OVA-KC could be used as an effective cryoprotectant in fish and related products for preservation and commercialization.

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Section: Resultssupporting

confidence: 91%

“…Myofibrillar proteins (MP), which include myosin, actin, troponin, and other proteins, are the main components of fish muscles, covering 65–75% of total proteins [ 9 ]. MP are susceptible to temperature fluctuations and can be quickly oxidized during frozen storage.…”

Section: Introductionmentioning

confidence: 99%

Ovalbumin and Kappa-Carrageenan Mixture Suppresses the Oxidative and Structural Changes in the Myofibrillar Proteins of Grass Carp (Ctenopharyngodon idella) during Frozen Storage

et al. 2021

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“…A porous protein network is formed during the two-stage thermal processing of surimi, which determines many important quality attributes of the gel products, such as texture, shelf life and digestion etc. [42,43]. Therefore, SEM was applied to observe the microstructure of gels prepared from frozen surimi.…”

Section: Effect Of Cmco On the Microstructure Of Gels Prepared From F...mentioning

confidence: 99%

Cryoprotective Roles of Carboxymethyl Chitosan during the Frozen Storage of Surimi: Protein Structures, Gel Behaviors and Edible Qualities

Zhu

et al. 2022

Foods

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Carboxymethyl chitosan (CMCh) is an ampholytic chitosan derivative that manifests versatile applications in food industry, such as antibacterial ingredients and nutritional additives. However, its use as a cryoprotectant remains under-researched. In this study, the cryoprotective effect of CMCh oligosaccharide (CMCO) on frozen surimi (silver carp) was systematically investigated in terms of protein structures, gelling behaviors, and sensory qualities. CMCO (0.6%) was incorporated in the surimi before frozen storage (−18 °C for 60 days) while the commercial cryoprotectant (4% sucrose, 4% sorbitol) was used as a positive control. Results indicated that CMCO could inhibit the freezing-induced denaturation of myofibrillar protein, whose values of solubility, Ca2+-ATPase and sulfhydryl content were 24.8%, 64.7%, and 17.1% higher than the nonprotected sample, respectively, while the surface hydrophobicity was 21.6% lower. Accordingly, CMCO stabilized microstructure of the surimi gels associated with improved gel strength, viscoelasticity, water-holding capacities, and whiteness. Moreover, the cryoprotective effect of CMCO with higher degree of carboxymethyl substitution (DS: 1.2) was more pronounced than that of low-DS-CMCO (DS: 0.8). Frozen surimi treated with high-DS-CMCO achieved competitive gelling properties and sensory acceptability to those with the commercial counterpart. This study provided scientific insights into the development of ampholytic oligosaccharides as food cryoprotectants.

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“…Fluorescence intensity (FI) can be adopted to determine the tertiary structural changes in myofibrils because of tryptophan (Trp) residue's sensitivity to microenvironmental polarity (Walayat et al, 2021). In…”

Section: Fluorescence Analysismentioning

confidence: 99%

The effect of multiple freeze–thaw cycles on protein oxidation and quality of Trachurus murphyi

Xie

2021

J. Food Process. Preserv.

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Trachurus murphyi is a fish species of the family scad of the suborder percophagus. It is widely distributed in the Northwest Pacific Ocean, including the East China Sea, Yellow Sea, and seawaters of Japan and Korea, and has high economic value. T. murphyi is an underused medium-fat fish, captured in large volumes by countries such as China, Peru, and Chile, and great interest has been accorded to its commercialisation (Zhao et al., 2019). Fresh Trachurus is perishable, and the sensory properties of fish deteriorate with storage because of chemical and biological transformations. Protein oxidation has been deemed as a major contributor to the deterioration of fish (Zhang, Shan, et al., 2020).Deterioration of fish quality may occur under degradation, denaturation, or aggregation of proteins during transportation and storage. Several studies have reported the changes in the structure and physicochemical properties of myofibrillar protein during storage, suggesting that protein denaturation is a major contributor of shelf-life decline, nutrient loss, and structural changes in fish (Alak et al., 2021;Isık et al., 2020). Protein oxidation is a complicated phenomenon that involves amino acid residues, buried hydrophobic exposure, and protein unfolding upon heating (Dericioglu at al., 2019). This process leads to further chemical modifications in amino acid side chains, triggers polymerisation, disruption of peptide backbones, and following aggregation, it involves intermolecular protein

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The effect of egg white protein and β-cyclodextrin mixture on structural and functional properties of silver carp myofibrillar proteins during frozen storage

Cited by 58 publications

References 34 publications

Ovalbumin and Kappa-Carrageenan Mixture Suppresses the Oxidative and Structural Changes in the Myofibrillar Proteins of Grass Carp (Ctenopharyngodon idella) during Frozen Storage

Ovalbumin and Kappa-Carrageenan Mixture Suppresses the Oxidative and Structural Changes in the Myofibrillar Proteins of Grass Carp (Ctenopharyngodon idella) during Frozen Storage

Cryoprotective Roles of Carboxymethyl Chitosan during the Frozen Storage of Surimi: Protein Structures, Gel Behaviors and Edible Qualities

The effect of multiple freeze–thaw cycles on protein oxidation and quality of Trachurus murphyi

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