A comparative study of physicochemical and functional properties of silver carp myofibrillar protein glycated with glucose and maltodextrin

Liu, Shulai; Zhao, Peng; Zhang, Jingjing; Xu, Qiang; Ding, Yuting; Liu, Jianhua

doi:10.1039/c6ra25088b

Cited by 11 publications

(6 citation statements)

References 39 publications

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“…The coating helps to stabilize the droplets from aggregation and coalescence and may also help reduce oxidation. Moreover, the emulsion stabilizing ability of food proteins could be improved following glycation (Maillard reaction), which has been widely reported. − Regarding structural changes during glycation, food proteins can undergo gradual changes in total SH content, surface hydrophobicity, and conformation, which renders proteins more flexible and enhances steric hindrance . These changes improve the emulsifying ability of food proteins.…”

Section: Introductionmentioning

confidence: 99%

Fish Oil Emulsions Stabilized with Caseinate Glycated by Dextran: Physicochemical Stability and Gastrointestinal Fate

Liu

Salt

et al. 2018

J. Agric. Food Chem.

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Incorporation of fish oil containing ω-3 polyunsaturated fatty acids (PUFAs) into functional foods remains challenging. In this study, caseinate and glycoconjugates (CD6, CD40, CD70, CD100) of caseinate to dextrans of different molecular weights (D6, D40, D70, D100 kDa) were used to stabilize fish oil emulsions, and the impact on physicochemical stability and gastrointestinal fate was investigated. The glycoconjugate of CD6 exhibited significantly higher conjugation efficiency, lower surface hydrophobicity (H0), and lower surface activity than other glycoconjugates. The glycoconjugate of CD70 displayed the best emulsifying activity and emulsion stability. Except CD6 stabilized emulsions, all other emulsions showed fine storage stability over 14 d at 22 ± 1 °C. The glycoconjugate stabilized emulsions exhibited significantly lower peroxide value (PV) (P < 0.05) than that of the caseinate stabilized one. During in vitro gastrointestinal tract digestion, the glycation of caseinate with dextrans changed the ζ-potential, average particle size (D 32), and particle size distribution of the emulsions, which influenced flocculation and coalescence of droplets, as demonstrated by confocal microscopy. Caseinate after glycation with dextrans significantly retarded the release of free fatty acids from emulsions (P < 0.05) during in vitro lipolysis. These results suggested that the dextrans attached to caseinate by glycation played a vital role in physicochemical stability and gastrointestinal fate of emulsions, mainly by its steric hindrance to effectively prevent flocculation and coalescence of droplets.

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Section: Introductionmentioning

confidence: 99%

Fish Oil Emulsions Stabilized with Caseinate Glycated by Dextran: Physicochemical Stability and Gastrointestinal Fate

Liu

Salt

et al. 2018

J. Agric. Food Chem.

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“…As the unreacted glucose was removed after glycation, the MRPs were re-dissolved in 0.5 M NaCl containing 40 mM Tris-HCl (pH 7.5). The amount of glucose bound to MF was determined by the phenol-sulphuric acid method (Liu et al, 2017a(Liu et al, , 2017b.…”

Section: Bound Glucose To Mfmentioning

confidence: 99%

“…Silver carp ( Hypophthalmichthys molitrix ) is a major freshwater fish, where myofibrillar protein (MF) constitutes about 60% of the total protein and serves as important functional component (Liu et al ., 2016). Many studies have found that glycation of silver carp MF via MR could effectively tune protein emulsifying properties (Liu et al ., 2017a), gel‐forming ability (You et al ., 2012), solubility (Liu et al ., 2019), and thermal stability (Liu et al ., 2016). In the present study, the ‘dry’ glycation of silver carp MF with glucose was systematically investigated to explore the physicochemical properties, the loss of Lys and Arg, and the formation of corresponding AGEs in resultant glycoconjugates.…”

Section: Introductionmentioning

confidence: 99%

Formation of advanced glycation end‐products in glycation of silver carp myofibrillar protein with glucose: Relationship with its chemical indicators

Ren

Mao

Zhang

et al. 2022

Int J of Food Sci Tech

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The formation of advanced glycation end products (AGEs), regarded as a potentially harmful substance, in the protein glycation course is still under investigation. This study investigated the glycation modification of silver carp myofibrillar protein (MF) with glucose via Maillard-driven chemistry. The resultant conjugates and glycation extent were characterised by chemical indicators, such as Fourier transform infrared spectroscopy, sodium dodecyl sulphate-polyacrylamide gel electrophoresis, colour development, and AGEs level. As the primary responsibility for glycation, the loss of Lysine (Lys) and Arginine (Arg) in MF with longer glycation time (>24 h) was more than 25%. While, the associated AGEs, including Nε-carboxymethyl-lysine (CML), Nε-carboxyethyl-lysine (CEL), and methylglyoxal-derived hydroimidazolone 1 (MG-H1), presented a gradually increasing tendency with glycation time. The kinetic studies indicated that the formation of CML and MG-H1 presented a highly linear correlation with heating time, while the CEL development could be described as an exponential function of glycation time (r ≥ 0.95). Moreover, the correlation analysis among these chemical indicators indicated that colour development was positively correlated with AGEs (r ≥ 0.85), while negatively related to the loss of Lys and Arg (r ≤ −0.89). The findings may help to better control the glycation course of food protein based on the formation of AGEs.

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“…Thus, glycation has been exploited to improve the solubility and emulsifying properties of MPs since the very beginning of this industry (Saeki, 1997; Saeki & Inoue, 1997). Generally, saccharides with smaller molecules showed faster reaction rates (Liu et al., 2017a).…”

Section: Glycation and Glycosylationmentioning

confidence: 99%

“…Glycation of konjac oligo‐glucomannan (KOG) with silver carp myofibrils and myosin was examined in several studies. The functionalities of MP‐KOG conjugates, including solubility and emulsion activity, reached a maximum after 8 to 12 hr dry‐heating glycation, while longer incubation periods might result in thermal denaturation (Liu et al., 2017a). 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).…”

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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A comparative study of physicochemical and functional properties of silver carp myofibrillar protein glycated with glucose and maltodextrin

Abstract: Myofibrillar protein (Mf) from silver carp (Hypophthalmichthys molitrix) was incubated with glucose and maltodextrin for 0–96 h at 50 °C and 75% relative humidity to obtain glycoconjugates in different periods of the Maillard reaction.

Cited by 11 publications

References 39 publications

Fish Oil Emulsions Stabilized with Caseinate Glycated by Dextran: Physicochemical Stability and Gastrointestinal Fate

Fish Oil Emulsions Stabilized with Caseinate Glycated by Dextran: Physicochemical Stability and Gastrointestinal Fate

Formation of advanced glycation end‐products in glycation of silver carp myofibrillar protein with glucose: Relationship with its chemical indicators

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

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