μ-Calpain oxidation and proteolytic changes on myofibrillar proteins from Coregonus Peled in vitro

Li, Pingping; Zhang, Zhiwei; Guo, Xin; Zhu, Xuemei; Mao, Xiaoying; Guo, Xia; Deng, Xiaorong; Zhang, Jian

doi:10.1016/j.foodchem.2021.130100

Cited by 23 publications

(15 citation statements)

References 38 publications

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“…Compared with the control, the values of total sulfhydryl content in 0.1, 0.5, 1, 5, and 10 mmol/L H 2 O 2 treatment group decreased by 1.23%, 4.50%, 7.68%, 18.31%, and 23.77%, respectively. A similar result was reported by Zhang et al (2021) and Liu et al (2021), who found that oxidation treatment decreased the total sulfhydryl content in a myofibrillar protein of Coregonus peled . There are two reasons for the decrease in total sulfhydryl content (Zhang, Li, Emara, Hu, Wang, Wang & He, 2020a): the formation of MP aggregates, which was caused by –SH group, forms a disulfide bond (S–S) during oxidation, and another is the production of sulfur‐containing derivatives, such as sulfonic acid, cysteine, or hyposulfonic acid.…”

Section: Resultssupporting

confidence: 89%

Effects of hydroxyl radical oxidation on physicochemical properties and degradation of chicken myofibrillar protein

Wei

Zhang

et al. 2022

Food Processing Preservation

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The most significant issue influencing the preservation and sale of chicken is its oxidative behavior. The effect of hydroxyl radical oxidation on the hydrolysis of myofibrillar protein by μ‐calpain in vitro was explored in this work, which looked at the alteration of chicken myofibrillar protein by hydroxyl radical oxidation. The carbonyl, dimerized tyrosine content and surface hydrophobicity of myofibrillar protein increased significantly as H2O2 concentration increased, tryptophan fluorescence intensity and total sulfhydryl content decreased. Compared with the control group, the carbonyl content of 10 mmol/L H2O2 treatment group increased to 1.7 nmol/mg protein, the surface hydrophobicity and the dimer tyrosine content increased 32.41% and 14.73%, respectively, the total sulfhydryl content decreased to 67.93 nmol/mg protein. The protein cross‐linked and aggregated, and the oxidative modification of chicken myofibrillar protein promoted degradation. Desmin degradation by μ‐calcinase is inhibited by MHC, actin, and troponin‐T. The findings revealed that oxidation influenced the hydrolysis of myofibrillar protein and the tenderness of chicken after slaughter. Novelty impact statement The chicken myofibrillar proteins were cross‐linked and aggregated by hydroxyl radical oxidation. The oxidative modification of hydroxyl radical changes the sensitivity of protein to μ‐calpain. The oxidative modification of chicken myofibrillar protein improved the tenderness of postmortem chicken by promoting the degradation of MHC, actin, and troponin‐T caused by μ‐calcium‐activating enzyme.

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Section: Resultssupporting

confidence: 89%

Effects of hydroxyl radical oxidation on physicochemical properties and degradation of chicken myofibrillar protein

Wei

Zhang

et al. 2022

Food Processing Preservation

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“…The degradation levels of actin with H 2 O 2 treatment significantly increased during storage (p < 0.05), because the methionine oxidation destroyed the non-covalent interactions in actin and reduced the stability of actin. This result is in agreement with a study by Liu et al [40]. The authors found that actin content gradually decreased in the presence of an oxidant, which may be related to enzymatic oxidation.…”

Section: Actinsupporting

confidence: 93%

Oxidative Stress Contributes to Cytoskeletal Protein Degradation of Esox lucius through Activation of Mitochondrial Apoptosis during Postmortem Storage

Zhao

et al. 2022

Foods

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This study investigated the role of oxidative stress in the mitochondrial apoptotic pathways and structural protein degradation of fish during postmortem storage by measuring oxidative stress levels, mitochondrial antioxidant enzyme activity, mitochondrial dysfunction, apoptotic factors, and structural protein degradation (n = 3). The results revealed that reactive oxygen species (ROS) increased gradually within the first 12 h and then decreased (p < 0.05) in mitochondria. Lipid peroxidation was increased, and superoxide dismutase, catalase, and glutathione peroxidase activities were decreased in mitochondria (p < 0.05). Furthermore, oxidative stress induced mitochondrial membrane opening, mitochondrial swelling, as well as the depolarization of mitochondrial potential. This led to an increase in the release of cytochrome c from mitochondria and caspase-3 activation. Ultimately, oxidative stress promoted small protein degradation (troponin-T and desmin) and induced myofibril susceptibility to proteolysis. These observations confirmed that oxidative stress mediated the activation of mitochondrial apoptotic factors-promoted protein degradation, initiating the deterioration of fish muscle through the mitochondrial apoptotic pathway.

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“…During postmortem aging, calpain-1 can translocate from the sarcoplasm to myofibrils, and the myofibril-bound calpain-1 still has proteolytic activity . Moreover, post-translational protein modification, such as s -nitrosylation and oxidation, , has been demonstrated to impact calpain-1 activity.…”

Section: Resultsmentioning

confidence: 99%

Lipid Peroxidation Products Influence Calpain-1 Functionality In Vitro by Covalent Binding

Zhai

Lonergan

Huff-Lonergan

et al. 2023

J. Agric. Food Chem.

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The objective of the current study was to evaluate the effects of lipid peroxidation products, malondialdehyde (MDA), hexenal, and 4-hydroxynonenal (HNE), on calpain-1 function, and liquid chromatography and tandem mass spectrometry (LC-MS/MS) identification of adducts on calpain-1. Calpain-1 activity slightly increased after incubation with 100 μM MDA but not with 500 and 1000 μM MDA. However, calpain-1 activity was lowered by hexenal and HNE at 100, 500, and 1000 μM. No difference in calpain-1 autolysis was observed between the control and 1000 μM MDA. However, 1000 μM hexenal and HNE treatments slowed the calpain-1 autolysis. Adducts of MDA were detected on glutamine, arginine, lysine, histidine, and asparagine residues via Schiff base formation, while HNE adducts were detected on histidine, lysine, glutamine, and asparagine residues via Michael addition. These results are the first to demonstrate that lipid peroxidation products can impact calpain-1 activity in a concentration-dependent manner and may impact the development of meat tenderness postmortem.

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μ-Calpain oxidation and proteolytic changes on myofibrillar proteins from Coregonus Peled in vitro

Cited by 23 publications

References 38 publications

Effects of hydroxyl radical oxidation on physicochemical properties and degradation of chicken myofibrillar protein

Effects of hydroxyl radical oxidation on physicochemical properties and degradation of chicken myofibrillar protein

Oxidative Stress Contributes to Cytoskeletal Protein Degradation of Esox lucius through Activation of Mitochondrial Apoptosis during Postmortem Storage

Lipid Peroxidation Products Influence Calpain-1 Functionality In Vitro by Covalent Binding

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