Physicochemical and structural properties of composite gels prepared with myofibrillar protein and lard diacylglycerols

Diao, Xiaoqin; Guan, Haining; Zhao, Xinxin; Diao, Xinping; Kong, Baohua

doi:10.1016/j.meatsci.2016.07.002

Cited by 58 publications

(33 citation statements)

References 45 publications

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“…(C), but the disulfide bonds were not significant forces in this study as it showed lower solubility ( P < 0.05) than hydrogen bonds and hydrophobic interactions. A similar result was observed by Diao et al . who reported that the disulfide bonds had a minimal influence.…”

Section: Resultsmentioning

confidence: 77%

Assessing gel properties of Amur sturgeon (Acipenser schrenckii) surimi prepared by high‐temperature setting (40 °C) for different durations

et al. 2020

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BACKGROUND Setting effects are different for each fish species tested. There is no published literature on the response of Amur sturgeon (Acipenser schrenckii) to increased setting times. This study investigated the effects of high‐temperature setting (40 °C) for different durations on the gel properties of A. schrenckii surimi. As A. schrenckii is a new surimi material, it is also necessary to conduct a sensory evaluation and to report the surimi yields. RESULTS Increasing setting durations (0.5–1.5 h) significantly improved the gel properties. The best results in terms of molecular forces, gel strength, texture profile analysis (TPA), water holding capacity (WHC), and whiteness were obtained by the gels with setting durations of 1 and 1.5 h. The protein degradation detected as a result of extended setting durations (>2 h) significantly decreased the gel properties. The most inferior gel properties were shown by the gel with setting for 3 h. Protein degradation also resulted in higher cooking loss and poor microstructures. The sensory evaluation indicated that A. schrenckii surimi was generally accepted by the panelists in terms of color, texture, and aroma. The surimi yield obtained in this study was 32.4%, which was similar to commercial surimi and higher than several surimi yields in recent studies. CONCLUSION Setting durations from 0.5 to 1.5 h can be implemented to improve the properties of A. schrenckii surimi. Extended durations (>2 h) must be avoided. Overall, this work provided some necessary information about setting response, gel properties, sensory evaluation, and surimi yield in A. schrenckii, which will be useful for further studies. © 2020 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 77%

Assessing gel properties of Amur sturgeon (Acipenser schrenckii) surimi prepared by high‐temperature setting (40 °C) for different durations

et al. 2020

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“…Jiang and Xiong (2013) reported that SPI and its emulsions in pork myofibrillar protein gels would be destroyed with the addition of a certain chemical reagent. Protein–protein interaction can also be interrupted by fats (Diao, Guan, Zhao, Diao, & Kong, 2016). Thus, the solubility of the protein after adding different force‐disruption chemical solutions denoted the formation of a structure whose components are more strongly bonded than with other proteins.…”

Section: Resultsmentioning

confidence: 99%

Effects of soybean protein isolate on protein structure, batter rheology, and water migration in emulsified sausage

Sha

Susu

Liu

2020

J Food Process Preserv

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This study investigated the effect of mixing soybean protein isolate (SPI) in meat batter on the protein structure and water distribution of emulsified sausages. With SPI (5%) addition, ionic bonds and hydrogen bonds in the batter with SPI (batter–SPI) significantly decreased and increased, respectively. The disulfide bonds in sausage with SPI (sausage–SPI) significantly increased compared with sausage without SPI. Batter–SPI displayed no significant decrease in protein solubility after thermal treatment compared with the control (batter). The water migration did not change significantly as SPI was added. SPI increased the viscosity and shear stress of the emulsified sausage during processing. The rheological analysis showed that the time of degradation temperature of protein ahead in batter–SPI compared with control. Raman spectroscopy revealed a decreased level of α‐helix and an increased level of β‐sheet during heat treatment. In conclusion, SPI has mainly affected the changes in the protein structure of emulsified sausages. Practical applications Loss of water and oil often occurs in emulsified sausages, which usually led to production and economic losses. Thus, our research investigated how the addition of soybean protein isolate affected the physicochemical properties of minced meat. This study has an important theoretical and practical significance for the active regulation of gel formation process and development of high quality emulsified sausage products.

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“…Diao et al . () suggested that fluorescence intensity is closely related to tryptophan concentration. Therefore, the reduced fluorescence intensity might be associated with the consumption of tryptophan by ROO·.…”

Section: Resultsmentioning

confidence: 99%

“…Thus, the exposure of tryptophan on protein surfaces may cause them to become more vulnerable to the ROOÁ attack. Diao et al (2016) suggested that fluorescence intensity is closely related to tryptophan concentration. Therefore, the reduced fluorescence intensity might be associated with the consumption of tryptophan by ROOÁ.…”

Section: Resultsmentioning

confidence: 99%

Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

Wang

Gan

et al. 2018

Int J of Food Sci Tech

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Summary We investigated the effect of peroxyl radicals (ROO·), which are products of lipid peroxidation, on the structure and gel properties of myofibrillar proteins (MPs) isolated from rabbit meat. 2,2′‐Azobis(2‐amidinopropane) dihydrochloride (AAPH) was heated to stably derive ROO·. As the AAPH concentration increased, the protein carbonyl compounds significantly accumulated (P < 0.05), and the total sulfhydryl content was significantly lost (P < 0.05). Circular dichroism spectra, UV absorption spectra, intrinsic fluorescence spectra and surface hydrophobicity revealed that ROO· caused protein unfolding and conformational changes in MPs. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) analysis indicated that moderate (0–3 mm) and relatively high (5 and 10 mm) AAPH concentrations could lead to protein crosslinking and protein aggregation, respectively. These changes in protein structure could influence the gelling properties of MPs. Low‐level protein oxidation could increase gel strength and water holding capacity, whereas high‐level protein oxidation could reduce gel properties.

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Physicochemical and structural properties of composite gels prepared with myofibrillar protein and lard diacylglycerols

Cited by 58 publications

References 45 publications

Assessing gel properties of Amur sturgeon (Acipenser schrenckii) surimi prepared by high‐temperature setting (40 °C) for different durations

Assessing gel properties of Amur sturgeon (Acipenser schrenckii) surimi prepared by high‐temperature setting (40 °C) for different durations

Effects of soybean protein isolate on protein structure, batter rheology, and water migration in emulsified sausage

Effect of peroxyl radicals on the structure and gel properties of isolated rabbit meat myofibrillar proteins

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