Effects of isochoric freezing on myofibrillar protein conformational structures of chicken breasts

Rinwi, Tsekwi Gracious; Ma, Ji; Sun, Da‐Wen

doi:10.1016/j.lwt.2023.114768

Cited by 12 publications

(4 citation statements)

References 56 publications

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“…The purified TMP was used within 24 h after storing at 4 °C. The biuret method using BSA as the standard [ 29 ] was used for the determination of protein concentration of TMP suspension with the help of an UV-Vis spectrophotometer.…”

Section: Methodsmentioning

confidence: 99%

“…Finally, the samples were thoroughly washed with pH 7.0 PBS buffer, passed through three layers of gauze, and centrifuged one last time to yield a final precipitate that was TMP. The purified TMP was used within 24 h after storing at 4 • C. The biuret method using BSA as the standard [29] was used for the determination of protein concentration of TMP suspension with the help of an UV-Vis spectrophotometer.…”

Section: Extraction Of Tmpmentioning

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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Section: Methodsmentioning

confidence: 99%

Section: Extraction Of Tmpmentioning

confidence: 99%

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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show abstract

“…The rising inclination towards expedient and nourishing ready-to-eat (RTE) meat products can be attributed to the contemporary fastpaced lifestyles (Jiang & Xiong, 2015). RTE chicken meat (e.g., cooked marinated chicken breasts and drumsticks) is favored by consumers due to its high protein content, low-calorie content, low-fat content, and characteristics of no religious restrictions, propelling the projected market size for RTE chicken food products of an impressive $9.67 billion by 2025 in China (Rinwi et al, 2023).…”

Section: Introductionmentioning

confidence: 99%

Insight into the evolution of textural properties and juiciness of ready‐to‐eat chicken breasts upon different thermal sterilization: From the perspective of protein degradation

Liu,

Zhou,

Chen

et al. 2024

Journal of Texture Studies

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Texture deterioration of meat products upon high‐temperature sterilization is a pressing issue in the meat industry. This study evaluated the effect of different thermal sterilization temperatures on the textural and juiciness of ready‐to‐eat (RTE) chicken breast. In this study, by dynamically monitoring the texture and juiciness of chicken meat products during the process of thermal sterilization, it has been observed that excessively high sterilization temperatures (above 100°C) significantly diminish the shear force, springiness and water‐holding capacity of the products. Furthermore, from the perspective of myofibrillar protein degradation, molecular mechanisms have been elucidated, unveiling that the thermal sterilization treatment at 121°C/10 min triggers the degradation of myosin heavy chains and F‐actin, disrupting the lattice arrangement of myofilaments, compromising the integrity of sarcomeres, and resulting in an increase of approximately 40.66% in the myofibrillar fragmentation index, thus diminishing the quality characteristics of the products. This study unravels the underlying mechanisms governing the dynamic changes in quality of chicken meat products during the process of thermal sterilization, thereby providing theoretical guidance for the development of high‐quality chicken products.

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“…Chicken, as one of the most commonly consumed poultry meats, possesses a rich nutritional profile, including essential amino acids, unsaturated fatty acids, and other micronutrients [1]. It is renowned for its tender texture, delicious taste, and widespread popularity worldwide [2].…”

Section: Introductionmentioning

confidence: 99%

Cooking-Induced Oxidation and Structural Changes in Chicken Protein: Their Impact on In Vitro Gastrointestinal Digestion and Intestinal Flora Fermentation Characteristics

Lv,

Wang,

Wei

et al. 2023

Foods

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Meat digestion and intestinal flora fermentation characteristics are closely related to human dietary health. The present study investigated the effect of different cooking treatments, including boiling, roasting, microwaving, stir-frying, and deep-frying, on the oxidation of chicken protein as well as its structural and digestion characteristics. The results revealed that deep-fried and roasted chicken exhibited a relatively higher degree of protein oxidation, while that of boiled chicken was the lowest (p < 0.05). Both stir-frying and deep-frying led to a greater conversion of the α-helix structure of chicken protein into a β-sheet structure and resulted in lower protein gastrointestinal digestibility (p < 0.05), whereas roasted chicken exhibited moderate digestibility. Further, the impact of residual undigested chicken protein on the intestinal flora fermentation was assessed. During the fermentation process, roasted chicken generated the highest number of new intestinal flora species (49 species), exhibiting the highest Chao 1 index (356.20) and a relatively low Simpson index (0.88). Its relative abundance of Fusobacterium was the highest (33.33%), while the total production of six short-chain fatty acids was the lowest (50.76 mM). Although stir-fried and deep-fried chicken exhibited lower digestibility, their adverse impact on intestinal flora was not greater than that of roasted chicken. Therefore, roasting is the least recommended method for the daily cooking of chicken. The present work provides practical advice for choosing cooking methods for chicken in daily life, which is useful for human dietary health.

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Effects of isochoric freezing on myofibrillar protein conformational structures of chicken breasts

Cited by 12 publications

References 56 publications

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

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

Insight into the evolution of textural properties and juiciness of ready‐to‐eat chicken breasts upon different thermal sterilization: From the perspective of protein degradation

Cooking-Induced Oxidation and Structural Changes in Chicken Protein: Their Impact on In Vitro Gastrointestinal Digestion and Intestinal Flora Fermentation Characteristics

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