Importance of salt and temperature in myosin polymerization during surimi gelation

Núñez-Flores, R.; Cando, Deysi; Borderías, A. Javier; Moreno, Helena M.

doi:10.1016/j.foodchem.2017.07.028

Cited by 87 publications

(36 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In general, the fractions of β ‐turn and random coil also increased gradually with increasing heating time. This is in agreement with previous reports on other fish proteins indicating that a decreased content of α ‐helix and increased content of β ‐sheet is a general feature in translucent‐type proteins during heating and gelation . In the second stage of heat treatments at 90 °C, the α ‐helix content decreased continuously within 1 min and then an obvious increase was observed with subsequent heating ( P < 0.05), whereas the changing tendencies of the β ‐sheet and β ‐turn fractions were contrary to the α ‐helix.…”

Section: Resultssupporting

confidence: 92%

Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Wang

Zhao

et al. 2019

J Sci Food Agric

View full text Add to dashboard Cite

BACKGROUND: The present study investigated the effect of two-step heat treatments on the structure of grass carp myofibrillar proteins (MPs) and their binding ability for selected aldehydes (hexanal, heptanal, octanal and nonanal). RESULTS: Within 30 min of the first heating step at 40 ∘ C and 5-10 min of the second heating step at 90 ∘ C, the enhancement of the flavor-binding ability was likely explained by the increases in surface hydrophobicity and total sulfhydryl content due to the unfolding of secondary structures of MPs through exposure of hydrophobic amino acids and sulfhydryl groups. Nevertheless, lengthy heating at 90 ∘ C accelerated the aggregation of unfolded MPs and reduced the hydrophobic bonding sites, thus weakening the hydrophobic interactions and decreasing the resultant binding ability of MPs with aldehydes.CONCLUSION: The binding ability of aldehydes to MPs was found to be strongly influenced by changes in protein structure and surface during the two-step heating process. The results provided insight into improving the flavor characteristics of freshwater fish surimi products.

show abstract

Section: Resultssupporting

confidence: 92%

Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Wang

Zhao

et al. 2019

J Sci Food Agric

View full text Add to dashboard Cite

show abstract

“…-helical structure probably led to the exposure of active groups, which resulted in heat-induced chemical cross-linking and formed a three-dimensional network. 20 Previous studies 32,33 concerning other proteins have also indicated that a decrease in -helix content and an increase in -sheet content are general features in a translucent type of protein during heating and gelation, which is consistent with our study.…”

Section: Raman Spectrasupporting

confidence: 92%

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Zhao

Wang

et al. 2019

J Sci Food Agric

View full text Add to dashboard Cite

BACKGROUND The influence of heat‐induced structural modifications of grass carp myofibrillar protein (MP) on its ability to bind to selected aldehydes (hexanal, heptanal, octanal and nonanal) was investigated. The interactions of MP and flavor compounds were investigated using HS‐GC‐MS, intrinsic fluorescence spectra, Raman spectra, SDS‐PAGE, turbidity, total sulfhydryl content and surface hydrophobicity. RESULTS The ability to bind to aldehydes was strongly influenced by changes in the structure and surface of proteins during the heating process (0–30 min). During the first 0–10 min of heating, the flavor‐binding ability increased, which is likely attributable to increased surface hydrophobicity and total sulfhydryl content, and to the unfolding of secondary structures of MP by exposure to reactive amino acids, sulfhydryl groups and hydrophobic bonding sites. Nevertheless, lengthy heating (>10 min) caused protein refolding and accelerated aggregation of protein, thus reducing hydrophobic interactions and weakening the resultant capacity of MP to bind to flavor compounds. CONCLUSION The results suggested that hydrophobic interactions were enhanced upon short‐term heating, whereas long‐term heating weakend them. The results provide information concerning improvement of the flavor profile of freshwater fish surimi products. © 2019 Society of Chemical Industry

show abstract

“…This means that the aggregation started just at the beginning of the frozen storage period (Huidobro and Mohamed 1998). The enthalpy maxima recorded in these fish minces was similar to that found in good-quality Alaska Pollock surimi (Grade KA) (Núñez-Flores et al 2018), meaning that the protein was not extensively denatured in any sample. Table 3 shows data from the cooking loss analysis.…”

Section: Differential Scanning Calorimetry (Dsc)supporting

confidence: 70%

“…Comparison of the electrophoretic profiles of fish minces just after freezing (day 0) (a) and after 6 months of frozen storage (b) showed more bands with molecular weight over 250 kDa in the latter, indicating some polymerization or aggregation (Konno and Imamura 2000;Núñez-Flores et al 2018). Also, after 6 months of frozen storage the MHC band appeared slightly denser than at day 0, indicating that native myosin had probably been slightly aggregated as a consequence of frozen storage.…”

Section: Sds-page In Polyacrylamide/agarose Gels: Analysis Of Myosin mentioning

confidence: 99%

“…This could be due to the loss of other protein fractions of lower molecular weight (more soluble) in the washing step (Park et al 2013). Washed mince showed more bands in the higher molecular weight area of electrophoretic gels ([ 250 kDa),which could be molecules of polymerized or aggregated myosin (Núñez-Flores et al 2018). This may also be related to the washing process, which could affect the protein muscle structure.…”

Section: Sds-page In Polyacrylamide/agarose Gels: Analysis Of Myosin mentioning

confidence: 99%

See 1 more Smart Citation

Valorization of recurrently discarded fish species in trawler fisheries in North-West Spain

et al. 2018

View full text Add to dashboard Cite

The progressive elimination of fish discards established by the European Union Council in 2013 has stimulated the valorization of flesh from discarded highquality species with good protein functional properties but which frequently have excessive fish-bones, fat, strange flavours, soft texture, etc. The present study therefore focuses on valorization of the extracted muscle (minced muscle), from several fish species frequently discarded in northwestern Spanish fisheries (Atlantic Ocean): Blue whiting (Micromesistius poutassou), Mackerel (Scomber scombrus), Red scorpionfish (Scorpaena scrofa), Pouting (Trisoreptus luscus) and Gurnard (Trigla spp.). Valorization of these discarded fish resources is a key objective for the survival of the fishery sector in this area. In this regard present study was planned to examine the behaviour of the mince during 6 months of frozen storage by means of physicochemical and sensory analyses, and to test consumer acceptance of three technologically different products (burgers, nuggets and structured fingers) prepared with fish mince from different species. Results indicated that protein aggregation started at the outset of frozen storage but progressed very slowly, with the exception of nonwashed blue whiting and red scorpionfish minces. Moreover, during frozen storage lipid oxidation increased in all samples; the increase was with two objectives highest in minced mackerel, a fatty fish, but no rancid flavour was detected. All mince samples presented acceptable physicochemical properties and good sensory acceptability after 6 months of frozen storage. Acceptability of final products made with these minces was high in all cases. Burgers were more acceptable for consumers aged over 40 and fingers and nuggets more for younger people.

show abstract

Importance of salt and temperature in myosin polymerization during surimi gelation

Cited by 87 publications

References 30 publications

Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Binding of aldehydes to myofibrillar proteins as affected by two‐step heat treatments

Effect of heat treatment on the binding of selected flavor compounds to myofibrillar proteins

Valorization of recurrently discarded fish species in trawler fisheries in North-West Spain

Contact Info

Product

Resources

About