Effect of CaCl2 on denaturation and aggregation of silver carp myosin during setting

Jia, Dan; You, Juan; Hu, Yang; Liu, Ru; Xiong, Shanbai

doi:10.1016/j.foodchem.2015.03.130

Cited by 99 publications

(38 citation statements)

References 33 publications

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“…Silver carp ( Hypophthalmichthys molitrix ), a widely cultivated and processed freshwater fish, has been used to produce surimi and surimid products in China . However, silver carp surimi does not have good gelling capability, which limits its processing and utilization to a great extent .…”

Section: Introductionmentioning

confidence: 99%

Effect of hydrocolloids on gel properties and protein secondary structure of silver carp surimi

et al. 2020

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BACKGROUND Hydrocolloids are the most commonly used additive in the processing of surimi products. However, the effect of hydrocolloids on surimi protein conformation has not been reported, and the level of hydrocolloids may be a key factor influencing the quality of surimi. Therefore, this study investigated the effect of curdlan, xanthan gum, κ‐carrageenan, and gelatin at various levels on gel properties and protein conformation of surimi from silver carp. RESULTS Addition of curdlan, κ‐carrageenan, or gelatin at lower level could significantly promote gel strength, textural profiles, and water holding capacity (WHC) of the surimi gels. However, gel strength and WHC gradually decreased with increasing amount of xanthan gum added. The addition of curdlan or κ‐carrageenan remarkably increased the whiteness of surimi gel, but the whiteness decreased when the concentration of κ‐carrageenan reached 5 g kg−1. Along with the increase of curdlan, κ‐carrageenan, or gelatin concentration, the index of hydrophobic interaction and hydrogen bonds first increased and then decreased, whereas index of ionic bonds first decreased and then increased. According to Raman spectroscopy data, a small content of curdlan or κ‐carrageenan promoted the conformational transition of surimi protein from α‐helix to β‐sheet, leading to the changes in gel properties of surimi gels. Scanning electron microscopy photographs showed surimi gels added with 4 g kg−1 curdlan or 2 g kg−1 κ‐carrageenan had a finer and denser network structure. CONCLUSION Curdlan or κ‐carrageenan at an appropriate concentration is a potential modifier to effectively improve the quality of surimi products. © 2020 Society of Chemical Industry

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Section: Introductionmentioning

confidence: 99%

Effect of hydrocolloids on gel properties and protein secondary structure of silver carp surimi

et al. 2020

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“…In our previous study, HIU was found to lead to the exposure of SH groups in myosin . Jia et al . and Lund et al .…”

Section: Resultsmentioning

confidence: 80%

“…d), which indicated that the peak width was much lower in the hydrated particle size of myosin with 100 mmol L −1 Ca 2+ than that of the other samples. Ca 2+ could promote proteins to form aggregates . It was presumed that Ca 2+ could also enhance the uniformity of myosin as a result of the aggregation of some smaller myosin particles induced by Ca 2+ .…”

Section: Resultsmentioning

confidence: 99%

“…The rate of G′ development in the range 50–70 °C ( R 50–70 ) was indicated by the slope of G′ versus time, and was estimated according to Jia et al . using:

R_{50 - 70} ((), normalPa {min}^{−1}) = ((), G_{70}^{'} - G_{50}^{'}) false/ 10

where G ′ 70 and G ′ 50 are storage modulus at 70 °C and 50 °C, respectively, and ‘10’ refers to the time for an increase of the temperature from 50 °C to 70 °C.…”

Section: Methodsmentioning

confidence: 99%

“…However, the activity of endogenous transglutaminase in surimi is Ca 2+ ‐dependent, such that calcium salt is usually added to improve the gelation properties of surimi . Calcium salt, a destabilizing salt in the Hofmeister series, can reduce the Gibbs free energy required for transfer of non‐polar groups into water, weaken the intramolecular hydrophobic interaction and promote protein unfolding . Furthermore, Ca 2+ can enhance the hydrophobic interaction between myosin and promote myosin cross‐linking via ‘salt bridges’ …”

Section: Introductionmentioning

confidence: 99%

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Aggregation and conformational changes of silver carp myosin as affected by the ultrasound–calcium combination system

Liu

Xie

et al. 2018

J Sci Food Agric

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The combination system reported in the present study was beneficial for myosin unfolding, facilitating intermolecular interactions between Ca and myosin. Ultrasound treatment promoted myosin aggregation via the induction of Ca and reduced the critical concentration of Ca required to aggregate myosin. In the fish processing industry, this combination system can enhance the gelation properties of surimi-based products. © 2018 Society of Chemical Industry.

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Effect of heat treatment duration on the interaction between fish myosin and selected flavor compounds

Wang

Zhao

et al. 2020

J Sci Food Agric

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BACKGROUNDInteractions between flavor compounds and proteins during food processing are critical to flavor perception of the final product. Here, we investigated the effect of the duration of heat treatment on the interaction between bighead carp myosin and selected flavor compounds including hexanal, heptanal, octanal, nonanal, (E)‐2‐heptenal, and 1‐octen‐3‐ol.RESULTSThe binding of flavor compounds to native myosin was strong and decreased in the order nonanal > octanal > (E)‐2‐heptenal > heptanal > hexanal >1‐octen‐3‐ol. The aldehydes, especially trans‐2‐undecenal, were more conducive to hydrophobic binding to myosin than alcohols. Within the initial 5 min of heating, the surface hydrophobicity and total sulfhydryl exposure increased, while α‐helix turned into β‐sheets, β‐turns, and random coils. However, upon further heating, the hydrophobicity and sulfhydryl contents declined, β‐sheets, β‐turns and random coils shifted to α‐helix. Throughout the heating process, the particle size increased, and the absolute zeta potential decreased continuously, indicating that thermal aggregation of myosin occurred simultaneously. Changes in binding capacities of flavor compounds to myosin were consistent with changes in hydrophobicity and sulfhydryl contents.CONCLUSIONThe initial enhancement of the flavor‐binding capacity of myosin was attributed to the unfolding of secondary structures by exposing more hydrophobic bonding sites and hydrogen bonding sites. The rebuilding and aggregating of myosin was enhanced upon prolonged heating, thus favoring hydrophobic protein–protein interactions and weakening the resultant flavor binding capacity of myosin.

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Effect of CaCl2 on denaturation and aggregation of silver carp myosin during setting

Cited by 99 publications

References 33 publications

Effect of hydrocolloids on gel properties and protein secondary structure of silver carp surimi

Effect of hydrocolloids on gel properties and protein secondary structure of silver carp surimi

Aggregation and conformational changes of silver carp myosin as affected by the ultrasound–calcium combination system

Effect of heat treatment duration on the interaction between fish myosin and selected flavor compounds

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