Tannic acid-induced changes in water distribution and protein structural properties of bacon during the curing process

Li, Haijing; Deng, Siyang; Ren, Yanming; Kong, Baohua; Xia, Xiufang

doi:10.1016/j.lwt.2020.110381

Cited by 11 publications

(3 citation statements)

References 44 publications

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“…As can be seen from Figure 4a–c, the spectral peaks of amide I bands of the 13 groups of samples are all within the range of 1650 ~ 1660 cm −1 , indicating that a large number of α‐helical structures maintained by CO and NH with hydrogen bonds are concentrated in this band (Zhong et al, 2021). When compared to the control group, the peak absorption became more robust and the peak area expanded as the mass fraction of GSE, ACE, and BBE increased.…”

Section: Resultsmentioning

confidence: 94%

Enhancing gel behavior of yellow croaker surimi by fruit extracts: Physicochemical properties and molecular mechanism

Wang,

Lin,

Wang

et al. 2023

Journal of Texture Studies

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The aim of this study was to investigate the effects of grape seed extract (GSE), acerola cherry extract (ACE), and blueberry extract (BBE) on the physicochemical properties and structure of the yellow croaker surimi gel. In addition, molecular docking and molecular dynamics (MD) simulation were utilized to study the binding mechanism of yellow croaker's fibrillin and fruit extracts. Surimi gel with 1.5% GSE, ACE, and BBE had the highest water holding capacity, hardness, chewability, cohesion, breaking force, breaking distance, gel strength, and densest 3D network structure, according to the experiment's findings. Nevertheless, the cross‐linking of proteins in surimi was blocked with the further increase of fruit extract (1.5%–2.0%), and the existing network of surimi was weakened or even destroyed. Three fruit extracts had little effect on the secondary structure of the surimi gel. Besides, hydrophobic and disulfide bonds are the main chemical bonds of croaker surimi. Molecular docking showed that B‐type procyanidine (BP) interacted with ASN‐183, SER‐571, ASP‐525, ARG‐350, LYS‐188, GLU‐349, CYS‐353, and other active amino acids in croaker protein. Moreover, it can form strong hydrogen bond interaction with ASN‐183, SER‐571, ASP‐525, and ARG‐350 at the active sites of protein. The BP‐Larimichthys crocea protein system's MD simulation was carried out, and calculations for the simulation's root mean square deviation, root mean square fluctuation, radius of gyration, solvent accessible surface area, and hydrogen bonds were made. It was found that these indices can demonstrate that the BP binding contributes to the stability of the yellow croaker structure.

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Section: Resultsmentioning

confidence: 94%

Enhancing gel behavior of yellow croaker surimi by fruit extracts: Physicochemical properties and molecular mechanism

Wang,

Lin,

Wang

et al. 2023

Journal of Texture Studies

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“…Consistent with the results presented in this paper, the study by Zhong et al . (2021) found that curing bacon with 1–2 g/kg tannic acid increased the S 0 of MP.…”

Section: Resultsmentioning

confidence: 99%

“…However, Chen et al (2020) attributed this to the binding of organic acids to the reactive site of tryptophan in MP. Zhong et al (2021) used different concentrations of tannic acid to marinate bacon and found that low concentrations (0.5 g/kg) of tannic acid interacted with the protein to protect the protein structure with high fluorescence intensity, whereas high concentrations (1.0 and 2.0 k/kg) of tannic acid produced a shielding effect and reduced MP fluorescence intensity. These results are different from the present study.…”

Section: Circular Dichroismmentioning

confidence: 99%

Complex organic acids treatment on crayfish (Procambarus clarkii): the relationship between myofibrillar protein structure and meat quality

Zhu,

Xiong,

2023

Int J of Food Sci Tech

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SummaryThe effect of complex organic acids (COA) treatment at different concentrations (0, 1%, 5%, 10% and 15%) on the myofibrillar protein (MP) structure and meat quality of crayfish (Procambarus clarkii) was investigated. The results showed that with increasing concentrations of COA treatment, the sulfhydryl content of MP decreased and dityrosine content increased. The MP secondary structure has a reduced α‐helix content and an increased β‐fold content. The MP tertiary structure unfolded, exposing hydrophobic and other amino acids to a polar environment. MP aggregation was induced in the 1% and 5% COA treatment groups and MP degradation was induced in the 10% and 15% COA treatment groups. Crayfish meat in the 5% COA treatment group showed improved textural properties due to protein aggregation. It also enhanced the colour, aroma and micromorphology of the crayfish meat.

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Investigating Morphology of Food Systems and Water-biopolymer Interactions in Food Using 1H NMR Relaxometry

et al. 2022

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Tannic acid-induced changes in water distribution and protein structural properties of bacon during the curing process

Cited by 11 publications

References 44 publications

Enhancing gel behavior of yellow croaker surimi by fruit extracts: Physicochemical properties and molecular mechanism

Enhancing gel behavior of yellow croaker surimi by fruit extracts: Physicochemical properties and molecular mechanism

Complex organic acids treatment on crayfish (Procambarus clarkii): the relationship between myofibrillar protein structure and meat quality

Investigating Morphology of Food Systems and Water-biopolymer Interactions in Food Using 1H NMR Relaxometry

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