Physicochemical characteristics and gel-forming properties of myofibrillar protein in an oxidative system affected by partial substitution of NaCl with KCl, MgCl2 or CaCl2

Ge, Ge; Han, Yurui; Zheng, Jiabao; Zhao, Ming; Sun, Weizheng

doi:10.1016/j.foodchem.2019.125614

Cited by 49 publications

(29 citation statements)

References 38 publications

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“…As expected, the carbonyl content in oxidised MP at 0.6 M NaCl was higher ( P < 0.05) than that in non‐oxidised MP, which is similar to the results of Ge et al . (2020). There was no significant difference in carbonyl content upon oxidation treatment between low and high salt concentrations regardless of Lys and His addition ( P > 0.05).…”

Section: Resultsmentioning

confidence: 99%

Oxidative characteristics and gel properties of porcine myofibrillar proteins affected by l‐lysine and l‐histidine in a dose‐dependent manner at a low and high salt concentration

Guo

Meng

et al. 2022

Int J of Food Sci Tech

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Summary This study investigated the effects of l‐lysine (Lys) and l‐histidine (His) on the oxidative characteristics and gel properties of porcine myofibrillar proteins (MP). Results showed that Lys and His had a strong ferrous ion‐chelating ability and hydroxyl radical‐scavenging activity. Moreover, Lys and His inhibited the protein carbonyl formation and MP aggregation at 0.2 M and 0.6 M NaCl, respectively, in a dose‐dependent manner. Furthermore, 2 and 4 mg mL−1 Lys and His decreased the oxidation‐induced loss of the tertiary structure of MP accompanied by the lower surface hydrophobicity. The water‐holding capacity and gel strength of MP gels increased with increasing Lys and His concentrations due to more regular and lamellar structures with smaller and homogeneous pores at 0.6 M NaCl and more orderly crosslinking via fibrous filament at 0.2 M NaCl. In summary, Lys and His chelated the ferrous ions and scavenged hydroxyl radicals, decreased the oxidation‐induced physicochemical changes, thus preventing oxidative damage during the formation of a three‐dimensional gel network, which resulted in better gel quality.

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Section: Resultsmentioning

confidence: 99%

Oxidative characteristics and gel properties of porcine myofibrillar proteins affected by l‐lysine and l‐histidine in a dose‐dependent manner at a low and high salt concentration

Guo

Meng

et al. 2022

Int J of Food Sci Tech

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“…Liu [ 21 ] hypothesized that an increase in temperature might increase the fluidity of myosin and affect the aggregation between MPs, resulting in a slight decrease in G′ . The significant decrease of G′ and G″ in the NC group from 22 °C to 31 °C might be due to the excessive oxidation of MPs caused by the addition of SC and NaCl [ 1 , 22 ]. The G′ of NaCl (46–48 °C), SG (20–36 °C), SC (26–32 °C), ST (43–50 °C), NG (35–41 °C), NC (33–39 °C), and NT (36–43 °C) increased slightly in the temperature range of 20 °C–50 °C ( Figure 2 A), which was the result of the denaturation and aggregation of the myosin head and cross-linking components, and indicated the initial formation of a gel network [ 23 ].…”

Section: Resultsmentioning

confidence: 99%

“…Myofibrillar proteins (MPs) are a group of gelatinous, salt-soluble proteins accounting for 55–65% of the total meat muscle proteins [ 1 ]. High-purity MPs, also known as surimi, are usually obtained by the boning, harvesting, rinsing, and dehydration of fish and are processed into surimi-based products [ 2 ].…”

Section: Introductionmentioning

confidence: 99%

Improvement of Gel Quality of Squid (Dosidicus gigas) Meat by Using Sodium Gluconate, Sodium Citrate, and Sodium Tartrate

Chu

Deng

et al. 2022

Foods

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In order to improve the quality of squid surimi products, squid surimi gels were prepared using several types of organic salts under two heating conditions to study the effects of organic salts on squid gel properties. Compared with the NaCl group, organic salts reduced the solubilization capacity of myofibrillar protein, and significant (p < 0.05) decreases in the breaking force, breaking distance, texture, and water-holding capacity of the gel were observed in the sodium gluconate group, while significant (p < 0.05) increases in the breaking force, breaking distance, texture, and water-holding capacity of the gel were observed in the sodium citrate and sodium tartrate groups. Although the mixed addition of NaCl and organic salt improved surimi gel quality, the effective improvement was still lower than that of only organic salt. Rheological properties indicated that sodium citrate and sodium tartrate had high viscoelasticity. The squid surimi gel prepared by direct heating exhibited better properties than gels prepared by two-step heating. The chemical force of squid gel prepared with sodium citrate and sodium tartrate formed a stronger matrix than the gels prepared with other salts. For color, the addition of sodium citrate resulted in an undesirable color of squid surimi gels, while the addition of sodium tartrate improved the whiteness of the surimi gel. The results showed that the quality of surimi gel was dependent upon the choice of heating method and the types of salt used. Sodium citrate and sodium tartrate could significantly improve the gel properties of squid surimi. This study provides reliable guidance for improving the overall quality of squid surimi gels.

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“…This indicated that the substitution of Na + by K + , Ca 2+ , and Mg 2+ could improve the gel viscosity. The higher G' and G" values enhanced the interaction between proteins and improved viscoelastic gel matrix, thereby increasing WHC in the compound gel system (Ge et al, 2020). The highest G' and G" values were shown in the group C, indicating that the optimal gel property was obtained when the substitution amount of NaCl by KCl, CaCl 2, and MgCl 2 was 35, 10, and 5%, respectively.…”

Section: Resultsmentioning

confidence: 99%

Effect of partial substitution of NaCl by KCl , CaCl ₂ , and MgCl ₂ on properties of mixed gelation from myofibrillar protein and Flammulina velutipes protein

Chen

et al. 2022

Food Processing Preservation

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The effects of substitution of sodium chloride (NaCl) by chloride salt mixtures (KCl, CaCl 2 , and MgCl 2 ) with different formulas on quality characteristics of mixed protein system containing 80% myofibrillar protein (MP) and 20% Flammulina velutipes protein (FVP) were investigated in this study. The addition of chloride salts (KCl, CaCl 2 , and MgCl 2 ) into a reduced-sodium (0.3 M NaCl) mixed gel system, increased the gel properties, and network structure of the MP-FVP gel, which might be attributed to the increase in protein solubility and rheological properties. The examination of the turbidity, particle size, zeta potential, UV spectroscopy, and Fourier transform infrared spectroscopy indicated that the protein molecules were obviously aggregated, that the electrostatic interaction was weakened, that the hydrophobic interaction and β-sheet content was increased. The results showed that when KCl, CaCl 2 , and MgCl 2 were used to replace NaCl at 35, 10, and 5%, respectively, the gel properties reached the maximum. Practical applicationsThis study evaluated the effects of different types of sodium salt substitution on the structural properties of proteins and the structural properties of mixed myofibrillar protein and Flammulina velutipes protein gels. The results revealed that the mixed protein molecules apparently aggregated under different replacement of KCl, CaCl 2, and MgCl 2 (i.e., 35, 10, and 5%). The hydrophobicity and β-sheet content significantly increased, while the electrostatic interaction decreased, leading to enhanced mixed gel properties. The results indicated the different replacements of sodium salts could improve the gels characteristics, which may be a guide for the future production of low-salt meat products.

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Physicochemical characteristics and gel-forming properties of myofibrillar protein in an oxidative system affected by partial substitution of NaCl with KCl, MgCl2 or CaCl2

Cited by 49 publications

References 38 publications

Oxidative characteristics and gel properties of porcine myofibrillar proteins affected by l‐lysine and l‐histidine in a dose‐dependent manner at a low and high salt concentration

Oxidative characteristics and gel properties of porcine myofibrillar proteins affected by l‐lysine and l‐histidine in a dose‐dependent manner at a low and high salt concentration

Improvement of Gel Quality of Squid (Dosidicus gigas) Meat by Using Sodium Gluconate, Sodium Citrate, and Sodium Tartrate

Effect of partial substitution of NaCl by KCl , CaCl ₂ , and MgCl ₂ on properties of mixed gelation from myofibrillar protein and Flammulina velutipes protein

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Physicochemical characteristics and gel-forming properties of myofibrillar protein in an oxidative system affected by partial substitution of NaCl with KCl, MgCl2 or CaCl2

Cited by 49 publications

References 38 publications

Oxidative characteristics and gel properties of porcine myofibrillar proteins affected by l‐lysine and l‐histidine in a dose‐dependent manner at a low and high salt concentration

Oxidative characteristics and gel properties of porcine myofibrillar proteins affected by l‐lysine and l‐histidine in a dose‐dependent manner at a low and high salt concentration

Improvement of Gel Quality of Squid (Dosidicus gigas) Meat by Using Sodium Gluconate, Sodium Citrate, and Sodium Tartrate

Effect of partial substitution of NaCl by KCl , CaCl 2 , and MgCl 2 on properties of mixed gelation from myofibrillar protein and Flammulina velutipes protein

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Effect of partial substitution of NaCl by KCl , CaCl ₂ , and MgCl ₂ on properties of mixed gelation from myofibrillar protein and Flammulina velutipes protein