Myofibrillar protein conformation enhance gel properties of mixed surimi gels with Nemipterus virgatus and Hypophthalmichthys molitrix

Shi, Yi Wei; Li, Qiang; Qiao, Cuiping; Zhang, Chang; Wang, Wei; Xu, Yongxia; Mi, Hongbo; Li, Xuepeng; Lǐ, Jiànróng

doi:10.1016/j.foodhyd.2020.105924

Cited by 75 publications

(46 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It was possible that the myosin of a 5:1 (H:N) mixture of silver carp and golden threadfin bream unfolded upon heating to expose many R‐SH groups, which is most beneficial for the cross‐linking and aggregation of myosin. Likewise, some studies also proved that there was a high correlation between increased gel properties and the reduction of sulfhydryl group content for wheat gluten proteins (Wang et al., 2017) and fish myofibrillar proteins (Yi et al., 2020; Zhang, Li, Shi, Zhu, & Luo, 2018) because of gelation.…”

Section: Resultsmentioning

confidence: 93%

Physicochemical properties, protein conformation, and aggregate morphology of heated myosin from Hypophthalmichthys molitrix and Nemipterus virgatus mixtures

Shi

Lǐ

et al. 2020

Food Frontiers

Self Cite

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 93%

Physicochemical properties, protein conformation, and aggregate morphology of heated myosin from Hypophthalmichthys molitrix and Nemipterus virgatus mixtures

Shi

Lǐ

et al. 2020

Food Frontiers

Self Cite

View full text Add to dashboard Cite

show abstract

“…The increase of nonfrozen water content indicates that the tightly bound water in the TGase‐induced gel was also increasing, which was specifically reflected in the increase of water holding capacity of MP/WG gel. In addition, with the addition of TGase, the binding capacity of proteins to water increased, resulting in the increase of water quality of the gel network, and the interaction of hydrophilic groups also promoted the formation of more nonfreezing water (Yi et al., 2020).…”

Section: Resultsmentioning

confidence: 99%

“…Yi et al. (2020) believed that hydrophobic interactions and hydrogen bonds occurred between the protein structures in the late gelation period to form aggregates, which formed a more stable network structure. This was consistent with the conclusion of intermolecular force analysis in this study.…”

Section: Resultsmentioning

confidence: 99%

“…The increased self‐binding of both proteins formed separate phases, reducing the stabilizing effect of the gluten proteins between the salt‐soluble proteins chains. Myofibrillar protein (MP) was one of the most important salt‐soluble proteins in meat and was an essential component of pork products (Yi et al., 2020). It has unique functionalities such as gel‐forming ability and water‐holding ability, which contribute to the stable structure of processed meat products (Wei et al., 2020).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Properties of transglutaminase‐induced myofibrillar/wheat gluten gels

Ouyang

et al. 2021

Journal of Food Science

View full text Add to dashboard Cite

Gelation properties of myofibrillar protein (MP)/wheat gluten (WG) induced by glutamine transaminase (TGase) were studied. Results showed that the inclusion of transglutaminase increased the gel strength, water‐holding capacity (WHC), and nonfreezable water (Wnf) of MP/WG mixture. Circular dichroism (CD) analysis showed that the β‐sheet and random coil content of the MP/WG treated with TGase addition increased by 12.1% and 3.7%, while the α‐helix and β‐turn content decreased by 14.2% and 1.8%. Rheological measurements showed that TGase induced higher energy storage modulus value during the MP/WG gel heating‐cooling cycle. the hydrogen bond and hydrophobic interaction content of the MP/WG gels increased by 80 and 120 ug/L, and the disulfide bond decreased by 200 ug/L, with TGase addition was increased from 0 to 120 U/g protein. Scanning electron microscope (SEM) showed that MP/WG gel with TGase had uniform and dense network structure. Practical Application The properties of myofibrillar/wheat gluten gel induced by TGase crosslinking was studied. The gel structure and water holding capacity of MP/WG were improved by the cross‐linking of TGase. The study of the gel properties of MP/WG induced by TGase crosslinking also can provide a theoretical basis for analyzing the effect of TGase on the application of gluten protein in complex meat emulsion system.

show abstract

“…During the last 10 years, consumers were interested in surimi and heat-induced surimi gelation products. With a reduction in the global production of marine fish resources and an increase in marine fishing costs, freshwater fish has been regarded as potential alternative surimi resources to meet demands in the surimi market, especially in China (Chen et al, 2020;Yi et al, 2020). However, problems have been faced in the production of surimi from freshwater fish species, such as grass carp.…”

Section: Introductionmentioning

confidence: 99%

Effects of ozone water rinsing on protein oxidation, color, and aroma characteristics of grass carp ( Ctenopharyngodon idellus ) surimi

Liu

Lin

et al. 2021

J. Food Process. Preserv.

Self Cite

View full text Add to dashboard Cite

This study investigates the effects of ozone water rinsing on the myofibrillar protein (MP) oxidation, color, and aroma characteristics of grass carp surimi. The results showed that the incubation of surimi with increased concentrations of ozone water led to a gradual generation of MP carbonyl derivatives and a loss of sulfhydryl.Additionally, the surface hydrophobicity of the MP increased, accompanied by a loss in tryptophan residues. The cross-linking via disulfide linkages and aggregates of the MP was formed after ozone water rinsing. The surimi treated with 3, 5, 7 and 10 mg/L ozone water had higher L* and whiteness values than that of the control group. After rinsing with ozone water, the relative contents of main volatile compounds including hexanal, heptanal, and 1-octen-3-ol declined significantly. The results demonstrated that rinsing with ozone water can improve the sensory quality of grass carp surimi, and also lead to MP oxidation.Novelty impact statement: Rising surimi with ozone water is an effective method to improve the color property of freshwater fish surimi. The work provides detailed information about the effects of ozone water on protein oxidation, whiteness, and volatile compounds of grass carp surimi. This not only contributes to perform a reasonable assessment for scientists to the use of ozone water in surimi production, but also give a reference for the production of high-quality surimi.

show abstract

Myofibrillar protein conformation enhance gel properties of mixed surimi gels with Nemipterus virgatus and Hypophthalmichthys molitrix

Cited by 75 publications

References 44 publications

Physicochemical properties, protein conformation, and aggregate morphology of heated myosin from Hypophthalmichthys molitrix and Nemipterus virgatus mixtures

Physicochemical properties, protein conformation, and aggregate morphology of heated myosin from Hypophthalmichthys molitrix and Nemipterus virgatus mixtures

Properties of transglutaminase‐induced myofibrillar/wheat gluten gels

Effects of ozone water rinsing on protein oxidation, color, and aroma characteristics of grass carp ( Ctenopharyngodon idellus ) surimi

Contact Info

Product

Resources

About