Characteristics of silver carp surimi gel under high temperature (≥100 °C): quality changes, water distribution and protein pattern

Jiang, Qixing; Wu, Weiming; Han, Jie; Chung, Hau Yin; Gao, Pei; Yu, Dawei; Yu, Peipei; Xu, Yanshun; Xia, Wenshui

doi:10.1111/ijfs.15799

Cited by 11 publications

(5 citation statements)

References 70 publications

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“…In this study, a Gaussian function fitting method was used to fit the deconvoluted spectra to compare the changes in protein secondary structure during storage at 4 °C and 10 °C, respectively. The results showed that the content of α-helix and β-sheet in the protein secondary structure gradually decreased with increasing storage time, while the content of the content and β-turn gradually increased, and the findings are consistent with those of previous authors [27,28]. As a result, the molecular structure of egg proteins changes in response to storage conditions, and FTIR-based techniques can provide a clearer picture of the exact changes that occur.…”

Section: Discussionsupporting

confidence: 89%

“…Journal of Food Processing and Preservation temperatures indicates a weakening of the hydrogen bonds and a gradual unfolding of the protein molecules. decrease in α-helix content with increasing storage temperature and time in the test is therefore due to the weakening of intermolecular hydrogen bonding in egg albumin as a result of the high temperature over time [27][28][29].…”

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confidence: 99%

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Study of the Molecular Structure of Proteins in Eggs under Different Storage Conditions

Ren

Yang

et al. 2023

Journal of Food Processing and Preservation

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The aim of this study is to reveal the relationship between changes in the physical and chemical characterization of eggs during storage and to provide a new way to assess egg freshness at the molecular chemical level. In this study, the Fourier transform infrared (FTIR) spectra of egg albumin from 60 fresh eggs (ISA Brown layer) stored for 1, 10, 20, 30, and 40 days at 4°C and 10°C were measured ( n = 6 ), and the amide I band of the egg albumin spectra was quantified by Fourier deconvolution and curve fitting to obtain the composition of the protein molecular structure. The results showed that different storage temperatures and storage times led to protein denaturation, resulting in changes in the conformation of the protein secondary structure. With increasing storage temperature and storage time, the content of the ordered structures β-sheet and α-helix in the egg protein secondary structure decreased significantly ( p < 0.05 ), and the content of the disordered structure β-turn and random coil increased significantly ( p < 0.05 ). Based on the pattern of protein secondary structure changes during storage, it was found that fresh eggs were better stored at 4°C for up to 15 days. Spearman’s correlation analysis of egg protein height, Haugh unit, egg weight, and protein secondary structure in eggs stored at 4°C showed a significant positive correlation between β-sheet and α-helix and egg weight, protein height, and Haugh unit. And a significant negative correlation between random coil and egg weight, protein height, and Haugh unit. Therefore, a curve fitting method based on Fourier transform infrared spectroscopy of deconvoluted spectra is an effective method for evaluating egg quality and freshness.

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Section: Discussionsupporting

confidence: 89%

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confidence: 99%

Study of the Molecular Structure of Proteins in Eggs under Different Storage Conditions

Ren

Yang

et al. 2023

Journal of Food Processing and Preservation

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“…Thiobarbituric acid reactive substances Thiobarbituric acid reactive substances analysis was according to the method of Jiang et al (2022aJiang et al ( , 2022b with slight modification. Chopped samples (5 g) were dispersed in three times the volume of 7.5% trichloroacetic acid (containing 0.1% propyl gallate and 0.1% EDTA) and then homogenised.…”

Section: Peroxide Value (Pov)mentioning

confidence: 99%

“…Jiang et al . (2022a, 2022b) studied the effects of high‐temperature treatments (100–125 °C) on the properties of silver carp surimi gel, and found that high‐temperature heating resulted in protein denaturation, aggregation, crosslinking and degradation, based on the increase in trichloroacetic acid (TCA) soluble peptides and the changes in protein secondary structure.…”

Section: Introductionmentioning

confidence: 99%

“…Shi et al (2020) found that high-temperature treatments (≥100 °C) significantly reduced the content of myosin and actin, resulting in poor water-holding capacity. Jiang et al (2022aJiang et al ( , 2022b studied the effects of hightemperature treatments (100-125 °C) on the properties of silver carp surimi gel, and found that hightemperature heating resulted in protein denaturation, aggregation, crosslinking and degradation, based on the increase in trichloroacetic acid (TCA) soluble peptides and the changes in protein secondary structure.…”

Section: Introductionmentioning

confidence: 99%

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Effects of acidification and sterilisation on the quality of channel catfish (Ietalurus punctatus) fillets

Zhang

Tang

et al. 2022

Int J of Food Sci Tech

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This study aims to investigate the effects of acidification and sterilisation on the quality of channel catfish, based on the texture, colour, physical and chemical properties, protein composition and water migration of channel catfish fillets. The results showed that the hardness, chewiness and colour of acidified and sterilised (AS) groups were significantly better than unacidified and sterilised (NAS) groups. The content of TCA soluble peptide in NAS was significantly higher than AS groups, indicating that high-temperature sterilisation induced more protein degradation. Electrophoresis analysis also showed that the protein bands in the unacidified and sterilised (NAS) groups weakened or disappeared. There was no significant difference in the fat oxidation index of peroxide value and thiobarbituric acid value indicating that little effect on oxidation was induced by acidification and sterilisation. After sterilisation, the water transferred from immobilised water to free water, and the weight loss rate of acidified non-sterilised (ANS) groups was significantly higher than AS. On the whole, acidified channel catfish could be sterilised at a lower temperature, thus having better texture, colour and lower weight loss rate. The sterilisation temperature of 91-95 °C was recommended to maintain a better quality of ready-to-eat acidified fish fillets.

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Kinetics and mechanisms of thermal deterioration in silver carp (Hypophthalmichtys molitrix) surimi gel quality under high‐temperature sterilization

Wu,

Gao,

Jiang

et al. 2024

J Sci Food Agric

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BACKGROUNDThe gelation properties of surimi gel under various high temperatures (115, 118, and 121 °C) and sterilization intensities (F0 values of 3–7 min) were systematically investigated. A kinetic model detailed quality changes during heat treatment through mathematical analysis, elucidating mechanisms for gel quality degradation.RESULTSIncreased sterilization intensity significantly reduced the quality characteristics of surimi gel. Compared to the gel without sterilization treatment, when the sterilization intensity was increased to 7 min, the gel strength of the groups treated at 115 °C, 118 °C, and 121 °C decreased by 68.35%, 51.4%, and 51.71%, respectively, and the water‐holding capacity decreased by 24.87%, 16.85%, and 22.5%, respectively. The hardness, chewiness, and whiteness of the gel also significantly decreased, and the changes in these indicators all conformed to a first‐order kinetic model. Activation energy of 291.52 kJ mol−1 highlighted gel strength as the least heat‐resistant. At equivalent sterilization intensities, 115 °C exhibited the poorest gel quality, followed by 121 °C, with 118 °C showing relatively better gel quality. Increased T22 and decreased PT22 suggested heightened water mobility and transition of immobilized water within the gel into free water. Protein degradation, weakened disulfide bonds and hydrophobic interaction, and protein conformation changes collectively led to a rough and incoherent gel network structure with large fissures, as verified by the results of scanning electron microscopy. Correlation analysis indicated potential for precise control over surimi gel quality by modulating physicochemical attributes.CONCLUSIONThe outcomes may be beneficial to improve the production and quality control of ready‐to‐eat surimi‐based products. © 2024 Society of Chemical Industry.

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Characteristics of silver carp surimi gel under high temperature (≥100 °C): quality changes, water distribution and protein pattern

Cited by 11 publications

References 70 publications

Study of the Molecular Structure of Proteins in Eggs under Different Storage Conditions

Study of the Molecular Structure of Proteins in Eggs under Different Storage Conditions

Effects of acidification and sterilisation on the quality of channel catfish (Ietalurus punctatus) fillets

Kinetics and mechanisms of thermal deterioration in silver carp (Hypophthalmichtys molitrix) surimi gel quality under high‐temperature sterilization

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