Microwave irradiation promotes aggregation behavior of myosin through conformation changes

Cao, Hongwei; Jiao, Xidong; Fan, Daming; Huang, Jianlian; Zhao, Jianxin; Yan, Biao; Zhou, Wenguo; Zhang, Hao; Wang, Mingfu

doi:10.1016/j.foodhyd.2019.05.002

Cited by 80 publications

(34 citation statements)

References 36 publications

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“…Cao et al. (2019) also found similar turbidity values when silver carp myosin was unheated. However, the turbidity of myosin in all experimental groups was obviously higher than that of the unheated samples, ranging from 0.6 to 1.5 after heating.…”

Section: Resultsmentioning

confidence: 66%

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

Shi

Lǐ

et al. 2020

Food Frontiers

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Section: Resultsmentioning

confidence: 66%

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

Shi

Lǐ

et al. 2020

Food Frontiers

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“…When the PUL concentration was high, there was great resistance in the solution, which prevented the protein fold from opening before the new stable structure formed. New disulfide bonds cannot be altered, leading to the amount of the total SH groups increasing 28 . The amount of total SH groups and surface SH groups decreased slightly as the pH increased (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…New disulfide bonds cannot be altered, leading to the amount of the total SH groups increasing. 28 The amount of total SH groups and surface SH groups decreased slightly as the pH increased ( Fig. 2E).…”

Section: Sh Group Amounts Of Wpc/pul Gelsmentioning

confidence: 92%

Effect of pullulan concentration and pH on the interactions between whey protein concentrate and pullulan during gelation

et al. 2020

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BACKGROUND: Whey protein concentrate (WPC)/pullulan (PUL) hydrogel is applied as a microencapsulation wall material to protect probiotics. However, the interactions between WPC and PUL during gelation have not been clarified. In the present study, the effects of PUL concentration and pH on the interactions between WPC and PUL during gelation were evaluated with respect to appearance, zeta-potential, sulfhydryl group amount, surface hydrophobicity and infrared spectroscopy measurements. The rheological properties of WPC/PUL gels were also determined. RESULTS: The results obtained showed that a proper concentration (0.40 g mL-1) of PUL could improve the gel by enhancing the strength of hydrogen bonding, electrostatic interactions and exposure of hydrophobic groups, whereas too much PUL inhibited the formation of disulfide bonds. Furthermore, hydrophobic interactions, disulfide bonds and hydrogen bonds were destroyed in varying degrees under an alkaline environment. The rheological results also demonstrated a similar effect of PUL concentration and pH on the storage modulus (G') of WPC/PUL gels. CONCLUSION: When the WPC/PUL gel was formed at PUL concentration of 0.40 g mL-1 and pH 7.0, the interaction between WPC and PUL could be enhanced, which is beneficial for the future application of WPC/PUL gels in the food industry.

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“…Turbidity was determined according to Cao et al. (2019). The absorbance of each sample was determined at 340 nm.…”

Section: Methodsmentioning

confidence: 99%

Effects of temperature on the denaturation and aggregation of ( Lateolabrax japonicus ) myosin from sea bass surimi

Liu

Huang

Wanling

et al. 2021

J Food Process Preserv

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This study aimed to investigate the effects of temperatures of 30-90°C on myosin denaturation and aggregation in sea bass (Lateolabrax japonicus) during setting. The result indicated that the myosin of sea bass began to form gels at 60°C, and surface hydrophobicity increased by around 8.9% at 40°C and reached its maximun at 60°C. During setting at 40°C and 60°C, the ratios of α-helix of myosin reduced gradually and finally decreasing by 17.1% and 25.2%, respectively. Incubating at 90°C, α-helix continued to transform into random coil. Association with the results of surface morphology, it further confirmed that the temperatures of 40°C and 60°C were two important denaturation and aggregation temperatures. At 90°C, myosin of sea bass formed a fine and dense gel network under the joint action of nondisulfide covalent bond, disulfide bond and hydrophobic interaction. Practical applicationsThe raw materials for marine surimi are becoming scarcer with marine overfishing and the increasing demand for surimi. Sea bass, an important economic mariculture fish in China, has white meat and less bone spur and is advantageous for the development of surimi products as raw materials. During heating of surimi, the change of myosin structure is a main important key to forming a gel network. This research revealed the changes of sea bass myosin from denaturation, aggregation to gel formation during heating and provided a theoretical basis for the processing of sea bass surimi. 2 of 11 | LIU et aL.ionic bonds on protein structure increase, forming larger molecular agglomerates, and an irreversibly stable three-dimensional network structure is gradually assembled (Lanier et al., 2005;Liu et al., 2008).However, the denaturation and aggregation properties of myosin are known to be different in different fish species (Ogawa et al., 1993;Riebroy et al., 2008), as these properties are determined by the stability of the protein, which depends on the temperature of the fish habitat (Shu-Fang et al., 1989). Yongsawatdigul and Park (2003) reported that the denaturation and aggregation of myosin from threadfin bream (Nemipterus bleekeri) occurred simultaneously at 34.5°C. Formation of protein aggregates and three-dimensional network structures of actomyosin and myosin from yellowcheek carp at 25-30°C was far less than those at 40-45°C (Ding et al., 2014).Hence, it is important to study the aggregation behavior of myosin in different fish species to improve the quality of surimi processing.Marine fishes, with better gel properties and lack of foul odor, are used as raw materials for surimi. However, due to marine overfishing and the increasing demand for surimi, the raw materials for marine surimi are becoming scarcer. (Lin et al., 2020). Sea bass (Lateolabrax japonicus) is an important economic mariculture fish in China. The output of sea bass in China was 180,200 t in 2019, an increase of 8.16% over 2018, with the output increasing annually (Ministry of Agriculture and Rural Affairs of the People's Republic of China, 2020). Additionally, sea...

show abstract

Microwave irradiation promotes aggregation behavior of myosin through conformation changes

Cited by 80 publications

References 36 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

Effect of pullulan concentration and pH on the interactions between whey protein concentrate and pullulan during gelation

Effects of temperature on the denaturation and aggregation of ( Lateolabrax japonicus ) myosin from sea bass surimi

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