Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility

Sun, Weizheng; Zhou, Feibai; Zhao, Mouming; Yang, Bao; Cui, Chun

doi:10.1016/j.foodchem.2011.04.101

Cited by 100 publications

(65 citation statements)

References 30 publications

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“…The peaks 2, 3, and 7 are caused by the intermolecular β-sheets, which increased with time and was higher in oxidized WPI samples compared with that of nonoxidized WPI (P < 0.05; Table 2). The β-sheets are the indicator of protein aggregation (Sun et al, 2011); these results also supported the changes of particles size from dynamic light scattering. Moreover, peak 3 was caused by parallel β-sheets, whereas peaks 2 and 7 were generally considered antiparallel β-sheets (Pelton and McLean, 2000).…”

Section: Structural Changes Of Oxidized Wpisupporting

confidence: 68%

“…The changes of particle size and Z-average diameter also supported the loss of thiol groups, the formation of disulfide bonds, dityrosine, and improvement of surface hydrophobicity protein, whereas all these changes can promote aggregation of WPI in radical-mediated oxidation. The aggregation measured by particle size and Z-average diameter also supported the increase of turbidity in oxidized WPI samples (Sun et al, 2011;Cui et al, 2012).…”

Section: Structural Changes Of Oxidized Wpimentioning

confidence: 53%

“…This proved that noncovalent protein-protein associations were also enhanced by oxidation. Changes in surface hydrophobicity reflect changes in chemical and physical characteristics of the protein structure (Sun et al, 2011). Consequently, protein hydrophobicity has been widely applied to assess the protein oxidation and denaturation (Sante-Lhoutellier et al, 2007).…”

Section: Structural Changes Of Oxidized Wpimentioning

confidence: 99%

“…Oxidation and denaturation of protein not only alter physiochemical, but also alter structural properties of protein during food treatments. Carbonyls, disulfide, and dityrosine bridges generated by oxidation of AA residues cause the polymerization and aggregation of proteins and change its secondary and tertiary structure (Sun et al, 2011;Cui et al, 2012). Structure is the base characteristic of protein, and characteristics such as hydrophobicity will be changed following the changes in structure and numerous biological processes will be affected.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Susceptibility of whey protein isolate to oxidation and changes in physicochemical, structural, and digestibility characteristics

Feng

Ullah

et al. 2015

Journal of Dairy Science

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Oxidation is an important factor for denaturing of whey protein isolate (WPI) during food processing. We studied the effects of chemical oxidation on physicochemical and structural changes along with in vitro digestibility of WPI in this work. Evaluation of physicochemical changes showed that carbonyl level and dityrosine content increased, whereas total and free thiol group levels decreased for oxidized WPI samples. For the structural changes, protein aggregation was measured by surface hydrophobicity, turbidity, and particle diameter, which was increased for oxidized WPI samples. The increase of the secondary structure β-sheets and antiparallel β-sheet also supported the aggregation of oxidized WPI. A direct quantitative relationship between physicochemical and structural changes and protein digestibility indicated that oxidation-related damage restricts the susceptibility of WPI to proteases. In conclusion, WPI had high susceptibility to oxidative stress, and both physicochemical and structural changes caused by severe oxidative stress could decrease the rate of in vitro digestibility of WPI.

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Section: Structural Changes Of Oxidized Wpisupporting

confidence: 68%

Section: Structural Changes Of Oxidized Wpimentioning

confidence: 53%

Section: Structural Changes Of Oxidized Wpimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Susceptibility of whey protein isolate to oxidation and changes in physicochemical, structural, and digestibility characteristics

Feng

Ullah

et al. 2015

Journal of Dairy Science

View full text Add to dashboard Cite

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“…Each spectrum from wave number 400-4000 cm À1 was obtained with an average of 128 scans at a resolution of 4 cm À1 . The pretreatment method for samples was according to that reported by Sun et al [24] with slight modification. One gram of freeze dried sample was mixed with 100 mg KBr and then the powder (13-mm diameter disk) was subjected to 15 tons of pressure for 5 min.…”

Section: Fourier Transformed Infrared Spectroscopy (Ftir)mentioning

confidence: 99%

Effects of power ultrasound on oxidation and structure of beef proteins during curing processing

Kang

Zou

Cheng

et al. 2016

Ultrasonics Sonochemistry

241

102

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The aim of this study was to evaluate the effects of power ultrasound intensity (PUS, 2.39, 6.23, 11.32 and 20.96Wcm(-2)) and treatment time (30, 60, 90 and 120min) on the oxidation and structure of beef proteins during the brining procedure with 6% NaCl concentration. The investigation was conducted with an ultrasonic generator with the frequency of 20kHz and fresh beef at 48h after slaughter. Analysis of TBARS (Thiobarbituric acid reactive substances) contents showed that PUS treatment significantly increased the extent of lipid oxidation compared to static brining (P<0.05). As indicators of protein oxidation, the carbonyl contents were significantly affected by PUS (P<0.05). SDS-PAGE analysis showed that PUS treatment increased protein aggregation through disulfide cross-linking, indicated by the decreasing content of total sulfhydryl groups which would contribute to protein oxidation. In addition, changes in protein structure after PUS treatment are suggested by the increases in free sulfhydryl residues and protein surface hydrophobicity. Fourier transformed infrared spectroscopy (FTIR) provided further information about the changes in protein secondary structures with increases in β-sheet and decreases in α-helix contents after PUS processing. These results indicate that PUS leads to changes in structures and oxidation of beef proteins caused by mechanical effects of cavitation and the resultant generation of free radicals.

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Effect of Peroxyl‐Radicals‐Induced Oxidative Modification in the Physicochemical and Emulsifying Properties of Walnut Protein

Mao

Wang

Sun

et al. 2020

J Americ Oil Chem Soc

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In this paper, the effects of peroxyl radical oxidation on the physicochemical and functional properties of walnut protein were investigated. Walnut protein isolate (WPI) containing 2,2 0 -azobis(2-amidinopropane) dihydrochloride (AAPH) was oxidatively stressed under aerobic conditions in peroxyl radical-generating media. Incubation of walnut protein with increasing concentration of AAPH resulted in gradual carbonyl generation and free sulfhydryl group degradation. The results of surface hydrophobicity implied that oxidation leads to protein aggregation thus decreasing protein solubility in an AAPH concentration-dependent manner (P < 0.05). Emulsifying properties exhibited a significant increase (P < 0.05) at AAPH concentrations up to 0.2 mM and higher AAPH concentrations reduced the emulsifying capacity of WPI. These results indicate that appropriate oxidation is helpful to improve the emulsifying properties of protein, and with an increase of oxidation degree, emulsifying functional will damage.

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Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility

Cited by 100 publications

References 30 publications

Susceptibility of whey protein isolate to oxidation and changes in physicochemical, structural, and digestibility characteristics

Susceptibility of whey protein isolate to oxidation and changes in physicochemical, structural, and digestibility characteristics

Effects of power ultrasound on oxidation and structure of beef proteins during curing processing

Effect of Peroxyl‐Radicals‐Induced Oxidative Modification in the Physicochemical and Emulsifying Properties of Walnut Protein

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