High-pressure processing influences the conformation, water distribution, and gel properties of pork myofibrillar proteins containing Artemisia sphaerocephala Krasch gum

Zhao, Shengming; Zhao, Li; Liu, Yu; Zhao, Yong; Yuan, Xiaorui; Kang, Zhuang‐Li; Zhu, Meifang; Ma, Haile

doi:10.1016/j.fochx.2022.100320

Cited by 19 publications

(9 citation statements)

References 41 publications

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“…NO could bind to cysteine residues in the hydrophobic region and mask the hydrophobic groups, thus limiting their interaction with the ANS. 32 In addition, Zhao et al 36 demonstrated that the oxidative stress induced by GSNO led to the protein re-crosslinkage and polymerization to form protein aggregation, which eventually reduced the surface hydrophobicity of the protein.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Effect of Nitric Oxide and Its Induced Protein S-Nitrosylation on the Structures and In Vitro Digestion Properties of Beef Myofibrillar Protein

Feng

Yin

Zhou

et al. 2023

J. Agric. Food Chem.

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This study aimed to investigate the effects of nitric oxide (NO) and its induced protein S-nitrosylation on the structures and digestion properties of beef myofibrillar protein (MP). The MP was treated with 0, 50, 250, 500, and 1000 μM concentrations of NO-donor S-nitrosoglutathione (GSNO) for 30 min at 37 °C. The results indicated that GSNO treatment significantly decreased the sulfhydryl contents whereas the carbonyl contents increased. Meanwhile, compared with the control group, the surface hydrophobicity, the intrinsic fluorescence intensity, and the α-helix content of proteins were decreased significantly with the enhancement of GSNO concentrations. In addition, 250 μM GSNO treatment increased the gastric digestibility of MP, while the gastrointestinal digestibility and the release of peptides were both inhibited by 500 and 1000 μM GSNO treatments. These data demonstrate that protein S-nitrosylation can affect the in vitro digestion properties of proteins by altering the physicochemical properties and structure of MP.

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Section: ■ Materials and Methodsmentioning

confidence: 99%

Effect of Nitric Oxide and Its Induced Protein S-Nitrosylation on the Structures and In Vitro Digestion Properties of Beef Myofibrillar Protein

Feng

Yin

Zhou

et al. 2023

J. Agric. Food Chem.

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“…Excessively prolonged HC treatments can lead to a decrease in H 0 as a result of the transient high temperatures generated and free radical effects that lead to the re-polymerization of TMP. Zhao et al [ 30 ] also found that high-pressure processing was able to unfold the pork MP, exposing the internal hydrophobic groups, but too much stress can lead to increased aggregation between proteins.…”

Section: Resultsmentioning

confidence: 99%

“…However, the fluorescence intensities of the TMP samples all increased when the HC treatment time reached 4 min, which could be attributed to the cavitation effect produced by HC inducing the refolding of the TMP molecules, which buried the exposed Trp residues [ 28 ]. These results indicate that proper HC treatment causes the unfolding of protein molecules, and the tertiary structure becomes loose, exposing internally buried hydrophobic groups with reactive sulfhydryl groups, which contributes to the formation of thermally induced gels by MP intermolecular cross-linking [ 30 ].…”

Section: Resultsmentioning

confidence: 99%

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Insight into the Effects of Hydrodynamic Cavitation at Different Ionic Strengths on Physicochemical and Gel Properties of Myofibrillar Protein from Tilapia (Oreochromis niloticus)

Xie,

Yang,

Ren

et al. 2024

Foods

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Effects of different ionic strengths (0.2, 0.4, and 0.6 mol/L) and different hydrodynamic cavitation (HC) treatment times (0, 1, 2, 3, and 4 min) on the conformation and gel properties of tilapia myofibrillar proteins (TMP) were investigated. The results showed that the solubility of TMP was significantly enhanced (p < 0.05) with the increase in NaCl concentration, and the gel characteristics were significantly improved. After HC treatment of TMP, the average particle size was significantly reduced (p < 0.05) and solubility was significantly enhanced (p < 0.05) with the increase in treatment time, the internal hydrophobic groups and reactive sulfhydryl groups were exposed. The intrinsic fluorescence spectra showed the unfolding of the spatial tertiary structure of proteins, and the circular dichroism spectroscopy showed the significant reduction in the content of α-helix in the secondary structure of the proteins (p < 0.05). In addition, the WHC and gel strength of the TMP heat-induced gels were enhanced, which improved the microstructure of the gels, and scanning electron microscopy showed that the gel network of the TMP gels became denser and more homogeneous. Dynamic rheology results showed that HC treatment resulted in a significant increase in the final G’ and G” values of TMP. In conclusion, HC treatment was able to improve the physicochemical structure and gel properties of TMP at different ionic strengths. This study presents a novel processing technique for the quality maintenance aspect of salt-reduced surimi gel products.

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“…The findings revealed that a pressure of 200 MPa yielded the most favourable results. This study showed similar results for pork gels (Zhao et al ., 2022). Furthermore, the application of pressure during the curing process enhances the meat's water retention capacity.…”

Section: Meat Water Retention Technologymentioning

confidence: 99%

Advances and applications in water retention technology for meat and meat products: Status and future research directions

Ji,

Nie,

Zhou

et al. 2024

Int J of Food Sci Tech

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SummaryWater retention technology plays a critical role in enhancing the flavour and yield of meat products, as well as maximising the economic advantages of meat processing in contemporary practices. This technique enhances the economic viability of the firm by augmenting the texture profile of meat products and optimising the yield. Water retention approaches essentially encompass the manipulation of pH levels, the inhibition of protein oxidation denaturation, and the alteration of the micro‐spatial structure of muscles. This study reviewed the different factors that contribute to water loss in meat and meat products, encompassing aspects such as animal species and cuts, pH levels, processing methodologies, storage and packing conditions, and salt concentration. This study reviewed the application of water retention techniques in the context of meat processing and its resultant products. The primary objective of this study is to offer theoretical justification for the reduction of juice loss, preservation of essential water content, enhancement of texture, and improvement of meat quality throughout the stages of processing and storage.

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High-pressure processing influences the conformation, water distribution, and gel properties of pork myofibrillar proteins containing Artemisia sphaerocephala Krasch gum

Cited by 19 publications

References 41 publications

Effect of Nitric Oxide and Its Induced Protein S-Nitrosylation on the Structures and In Vitro Digestion Properties of Beef Myofibrillar Protein

Effect of Nitric Oxide and Its Induced Protein S-Nitrosylation on the Structures and In Vitro Digestion Properties of Beef Myofibrillar Protein

Insight into the Effects of Hydrodynamic Cavitation at Different Ionic Strengths on Physicochemical and Gel Properties of Myofibrillar Protein from Tilapia (Oreochromis niloticus)

Advances and applications in water retention technology for meat and meat products: Status and future research directions

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