Enhanced heat stability and antioxidant activity of myofibrillar protein-dextran conjugate by the covalent adduction of polyphenols.

Modification of myofibrillar protein via glycation: Physicochemical characterization, rheological behavior and solubility property

In the present study, myofibrillar protein (MP) and dextran (DX) conjugates were prepared via glycation in a liquid solution. The effects of DX molecular weight on structural and emulsifying properties of conjugates compared with those of MP were investigated. The glycation was confirmed by evaluating modification degree of glycation (DG), electrophoresis and Fourier transform infrared spectroscopy. As DX molecular weight increased, the Ca2+-ATPase activity decreased markedly due to modification of MP, and the formation of MP-DX conjugates reduced surface hydrophobicity owing to the unfolding behaviour of MP and covalent attachment of DX. In addition, combined analysis of turbidity and reactive sulfhydryl contents indicated that MP may undergo a conformation unfolding and become looser and more flexible upon glycation. Glycation was able to increase the emulsifying activity and emulsion stability of MP, and MP-DX 70 showed the best emulsifying properties. A good correlation between reactive sulfhydryl contents and emulsifying properties was obtained, and the correlation coefficients were 0.930 for emulsifying activity and 0.961 for emulsion stability. Meanwhile, there was a negative correlation between surface hydrophobicity and emulsifying properties with correlation coefficients of −0.965 and −0.895, respectively. Overall, glycation could alter the structural characteristics and enhance the emulsifying properties of MP.

Glycation-induced structural modification of myofibrillar protein and its relation to emulsifying properties

The present study was performed to clarify the effects of pulsed electric field (PEF) on the physicochemical properties and conformations of myofibrillar proteins (MPs) extracted from pale, soft, exudative (PSE)-like chicken breast meat. Various PEF parameters, including the electric field intensity (0–28 kV/cm) and pulse frequency (0–1000 Hz), were varied. The results showed that as the PEF intensity increased, the solubility, surface hydrophobicity and sulfhydryl group content of the MPs were significantly improved. However, when the intensity exceeded 18 kV/cm, these properties declined, which was possibly due to protein aggregation caused by functional group interactions. Additionally, the PEF treatment altered the rheological properties of PSE-like MPs and induced the formation of low-elasticity MPs. However, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that the primary structure of the MPs was not altered after the PEF treatment. According to the circular dichroism (CD) spectroscopy results, the α-helix contents of the PEF-treated samples were increased but the β-turn and random coil contents were reduced. Industrial relevance The occurrence of PSE-like chicken meat is one of the most serious quality issues worldwide and can decrease the consumer's purchasing desire and result in extensive economic losses for the poultry processing industry. MPs play a vital role in the qualitative characteristics of chicken products. As a potential novel processing technology, PEF has potential applications for improving the functionality of PSE-like chicken protein to expand its application in the food industry.

Physicochemical and structural properties of myofibrillar proteins isolated from pale, soft, exudative (PSE)-like chicken breast meat: Effects of pulsed electric field (PEF)

Background Salt-soluble myofibrillar proteins (MPs) form the major protein component of meat and have several advantages over plant-derived proteins, including high digestibility and the presence of all the essential amino acids However, MPs are not widely used because the presence of myosin filaments limits their functionality in low ionic strength media Hence, an approach for effectively inhibiting or disrupting the formation of myosin filaments is a challenging issue in the development of novel meat protein based products Scope and approach To develop a strategy for inhibiting or destroying the formation of myosin filaments, an understanding of the process of myosin self-association is needed at the molecular level Hence, the present review systematically elaborates the assembly mechanism of myosin filaments and its relation to the functionality of MPs Additionally, the review focuses on the description of several chemical and physical strategies, with an emphasis on advantages, disadvantages, and recent progress Key findings and conclusions The assembly of myosin into filaments has been shown to be mediated by sequentially distributed charges in the myosin tail Moreover, the dissociation of myosin filaments, leading to improved functional properties of the MPs, has been demonstrated by amino acid treatment, glycation, high-intensity ultrasonication (HIU), and high-pressure homogenization (HPH) in low ionic strength media Nevertheless, these strategies still face a number of limitations and, hence, further research is needed in order to achieve large-scale industrial production In addition, the enhanced development of novel meat protein based products requires a consideration of the thermal stability of MPs throughout the entire process from product sterilization through to preservation and consumption

Filamentous myosin in low-ionic strength meat protein processing media: Assembly mechanism, impact on protein functionality, and inhibition strategies

Protein glycosylation results in structural changes which affects its functionalities. In this study, myofibrillar protein (MP) from pale, soft and exudative (PSE)-like chicken breast meat was grafted onto the glucosamine (GlcN) backbone using microbial transglutaminase (MTGase) as a biocatalyst and the impacts of glycosylation on structural and solubility properties of the conjugation product were investigated. The covalent attachment was verified by HPLC and Fourier transform infrared spectroscopy (FT-IR). The optimal conjugation conditions were 37 °C at pH 7.5 for 6 h with a MP to GlcN weight ratio of 1:3. The results of secondary structure analysis suggested that the glycosylated MP had decreased α-helix level and increased β-sheet, β-turns and random coil levels. After glycosylated with GlcN, the surface hydrophobicity was significantly reduced and the solubility of MP at the isoelectric point was markedly improved (P

Structural and solubility properties of pale, soft and exudative (PSE)-like chicken breast myofibrillar protein: Effect of glycosylation

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Structural and solubility properties of pale, soft and exudative (PSE)-like chicken breast myofibrillar protein: Effect of glycosylation