Structural changes of silver carp myosin glycated with Konjac oligo-glucomannan: Effects of deacetylation

Liu, Jianhua; Fang, Chunhua; Xu, Xia; Su, Qi; Zhao, Ping; Ding, Yuting

doi:10.1016/j.foodhyd.2019.01.038

Cited by 43 publications

(19 citation statements)

References 42 publications

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“…Notably, the TPI exhibited the highest content of α-helix, while the SPI displayed the highest content of β-sheet. These results are in agreement with previous studies demonstrating that the α-helix content in TPI is higher than that in SPI [29,47]. As shown in Table 1, the TSPCs contained two main structures: α-helix and β-sheet.…”

Section: Resultssupporting

confidence: 92%

“…These findings are similar to those of previous work, which found that both α-helix unfolding and β-sheet formation favor the gelation of myosin [28,43]. According to previous studies [29,32,49], flexible structures are conducive to function-related conformational changes, while tight structures may not be beneficial to functional enhancement. In this study, the tight structure of tilapia proteins may have partially contributed to their highly flexible structures, thus improving the water solubility of the TSPCs.…”

Section: Resultssupporting

confidence: 92%

“…During processing, the a-helix was shown to be negatively related to the elastic modulus of silver carp myosin and the gel strength of shrimp surimi, while the β-sheet was shown to be positively correlated [27,28]. It has been reported that the β-sheet and β-turn content in silver carp myosin increased after glycation, suggesting that a highly flexible conformation is important for determining its functional properties [29]. These correlation studies have demonstrated that the structural flexibility of a protein can provide us with a deep understanding of its functional properties.…”

Section: Introductionmentioning

confidence: 99%

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Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

et al. 2019

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The secondary structure of a protein has been identified to be a crucial indicator that governs its water solubility. Tilapia protein isolate (TPI), soybean protein isolate (SPI), and tilapia-soybean protein co-precipitates (TSPC3:1, TSPC2:1, TSPC1:1, TSPC1:2, and TSPC1:3) were prepared by mixing tilapia meat and soybean meal at different mass ratios. The results demonstrated that the water solubility of TSPCs was significantly greater than that of TPI (p <0.05). The changes in ultraviolet–visible and near-ultraviolet circular dichroism spectra indicated that the local structure of TSPCs was different from that of TPI and SPI. Fourier transform infrared Spectroscopy revealed the co-existence of TPI and SPI structures in TSPCs. The secondary structures of TSPCs were predominantly α-helix and β-sheet. TSPC1:1 was unique compared to the other TSPCs. In addition, there was a good correlation between the water solubility and secondary structure of TSPCs, in which the correlation coefficients of α-helix and β-sheet were −0.964 (p <0.01) and 0.743, respectively. TSPCs displayed lower α-helix contents and higher β-sheet contents compared to TPI, which resulted in a significant increase in their water solubility. Our findings could provide insight into the structure–function relationship of food proteins, thus creating more opportunities to develop innovative applications for mixed proteins.

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Section: Resultssupporting

confidence: 92%

Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

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Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

et al. 2019

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“…17 Liu et al (2019a; 2019b) studied the deacetylation of konjac oligo-glucomannan on the physico-chemical and structural properties of silver carp myosin as well. 18,19 Although a few studies of KGM-protein gels exist, the fundamental mechanism was not clear at the structural level of the molecule itself. As well known, the removal of acetyl groups changes the interaction force and structure of KGM itself.…”

Section: Introductionmentioning

confidence: 99%

Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)

Shi

et al. 2019

RSC Adv.

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“…Similarly, glycation with KOG also increased the emulsion properties of silver carp myosin by increasing the flexibility and steric hindrance of proteins (Liu et al., 2017b). The deacetylation of KOG facilitated its attachment to myosin, resulting in higher levels of glycation, which contributed to increased thermal stability and solubility (Liu et al., 2019a,b). The efficiency of maltose and ribose glycation was optimized with random‐centroid optimization (primarily considering four factors: temperature, relative humidity, reaction time, and quantity of carbohydrate) to obtain improved antioxidant activity (Nishimura & Saeki, 2016, 2018).…”

Section: Glycation and Glycosylationmentioning

confidence: 99%

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

Zhang

Zhou

2020

Comp Rev Food Sci Food Safe

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To improve the quality of meat products is a constant focus for both the meat industry and scientists. As major components in meat protein, the gelation properties of myofibrillar proteins (MPs) predominantly determine the sensory quality and product yield of the final product. Naturally or artificially occurring covalent modifications are known to largely affect MP functionality by changing the protein structure and forming aggregates, leading to both favorable and unfavorable outcomes. The review aims to summarize the mechanisms associated with several covalent modifications and the recent developments in enhancing MP gelation properties. Various extrinsic and intrinsic parameters controlling oxidation, phenolic–protein interactions, enzyme catalysis, glycation, and isoelectric solubilization/precipitation, and their effects on the characteristics of heat‐induced MP gels are discussed. This article provides an improved understanding of the covalent modifications that occur mainly in the MP system and how they can be utilized to promote its gelation properties. Covalent modifications exhibited dose‐dependent and dual‐role manners for MP gelation properties. Mild oxidation, enzyme catalysis, and isoelectric solubilization/precipitation treatment would be beneficial to form more aligned and cross‐linked three‐dimensional networks for MP gels because of moderate protein aggregation. However, an excessive aggregate impedes the MP gelation behavior, leading to reduced gelation quality. Glycation effectively increased hydrophilicity of MPs and phenolic conjugation provides MPs with novel bioactivity. A proper utilization of such a process or even a rational combination of them allowed us to enhance the gelation properties of MP with assorted appreciated functionalities and further improve the quality of meat products.

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Structural changes of silver carp myosin glycated with Konjac oligo-glucomannan: Effects of deacetylation

Cited by 43 publications

References 42 publications

Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

Correlation Between the Water Solubility and Secondary Structure of Tilapia-Soybean Protein Co-Precipitates

Effects of deacetylation of konjac glucomannan on the physico-chemical properties of surimi gels from silver carp (Hypophthalmichthys molitrix)

Covalent chemical modification of myofibrillar proteins to improve their gelation properties: A systematic review

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