Effects of high pressure versus conventional thawing on the quality changes and myofibrillar protein denaturation of slow/fast freezing beef rump muscle

LI, Li

doi:10.1590/fst.91421

Cited by 3 publications

(1 citation statement)

References 37 publications

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“…Therefore, different strategies are needed to improve the meat color stability of different varieties and muscles. Some studies have shown that HI and NHI, as oxidation products of Mb and hemoglobin (Hb), participate in free radical chain reactions to form lipid and protein oxidation products, which can weaken the oxidative stability of the muscles (Li, 2022).…”

Section: Introductionmentioning

confidence: 99%

Study on meat color stability of Qinchuan cattle during post-slaughter storage

CHEN

Yang

et al. 2023

Food Sci. Technol

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To study the stability of meat color in the post-slaughter storage process of Qinchuan cattle, three different bovine muscles, including longissimus dorsi (LD), knee round (KR) and psoas major (PM) muscles of Qinchuan cattle, were selected as research objects to determine the changes in meat color, myoglobin (Mb) relative content, pH, oxygen consumption rate (OCR), total iron, heme iron (HI) and other contents during storage. With the prolongation of the storage time, the relative content of oxymyoglobin (OxyMb) decreased, the relative content of metmyoglobin (MetMb) gradually increased, and muscle browning was due to the increase of a* value and hue value; Among them, HI and non-heme iron (NHI) reduced the stability of meat color by accelerating lipid oxidation, which was consistent with the results of Mb content and meat color index determining meat color stability. Therefore, the total iron content in muscles can also be used as an indicator of meat color stability.

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Section: Introductionmentioning

confidence: 99%

Study on meat color stability of Qinchuan cattle during post-slaughter storage

CHEN

Yang

et al. 2023

Food Sci. Technol

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Direct or indirect immersion freezing systems

Sánchez-Vega,

Aguiló-Aguayo,

Rodríguez-Roque

2024

Low-Temperature Processing of Food Products

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Physicochemical and structural changes of myofibrillar proteins in muscle foods during thawing: Occurrence, consequences, evidence, and implications

Zhang

Liu

Xie

et al. 2023

Comp Rev Food Sci Food Safe

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Myofibrillar protein (MP) endows muscle foods with texture and important functional properties, such as water‐holding capacity (WHC) and emulsifying and gel‐forming abilities. However, thawing deteriorates the physicochemical and structural properties of MPs, significantly affecting the WHC, texture, flavor, and nutritional value of muscle foods. Thawing‐induced physicochemical and structural changes in MPs need further investigation and consideration in the scientific development of muscle foods. In this study, we reviewed the literature for the thawing effects on the physicochemical and structural characters of MPs to identify potential associations between MPs and the quality of muscle‐based foods. Physicochemical and structural changes of MPs in muscle foods occur because of physical changes during thawing and microenvironmental changes, including heat transfer and phase transformation, moisture activation and migration, microbial activation, and alterations in pH and ionic strength. These changes are not only essential inducements for changes in spatial conformation, surface hydrophobicity, solubility, Ca2+‐ATPase activity, intermolecular interaction, gel properties, and emulsifying properties of MPs but also factors causing MP oxidation, characterized by thiols, carbonyl compounds, free amino groups, dityrosine content, cross‐linking, and MP aggregates. Additionally, the WHC, texture, flavor, and nutritional value of muscle foods are closely related to MPs. This review encourages additional work to explore the potential of tempering techniques, as well as the synergistic effects of traditional and innovative thawing technologies, in reducing the oxidation and denaturation of MPs and maintaining the quality of muscle foods.

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Effects of high pressure versus conventional thawing on the quality changes and myofibrillar protein denaturation of slow/fast freezing beef rump muscle

Cited by 3 publications

References 37 publications

Study on meat color stability of Qinchuan cattle during post-slaughter storage

Study on meat color stability of Qinchuan cattle during post-slaughter storage

Direct or indirect immersion freezing systems

Physicochemical and structural changes of myofibrillar proteins in muscle foods during thawing: Occurrence, consequences, evidence, and implications

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