Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle
Abstract:Oxidation extent of myofibrillar protein (MP) from silver carp (Hypophthalmichthys molitrix) was affected by the content and type of lipid peroxidation (LPO) products. Oxidized linoleic acid (OLA) was selected as a main representative of lipid peroxidation to investigate the effects of oxidative modification of LPO products on MP structure. Structural changes of the oxidized myofibrillar protein were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier trans… Show more
“…When incubated with 0-3 mm linoleic acid, the protein surface hydrophobicity increased as the originally occluded hydrophobic groups were exposed to the protein surface. [63] The surface hydrophobicity of the tropomyosin decreased with an increase in HNE (0-1.0 mm), as previously reported. According to the authors of the study, the decrease in HNE modified shrimp tropomyosin surface hydrophobicity may be attributed to hydrophobic interactions of amino acid, modification of the exposed hydrophobic residues, and the hydrophilic group formation (e.g., protein carbonyl groups).…”
Protein modification by active aldehydes is associated with ageing and some chronic diseases, and it is closely related to food quality and safety. In this study, the modification of bovine serum albumin (BSA) using trans,trans-2,4-decadienal at various concentrations (0-10 mm) is investigated. The results show that the changes in the number of free amino groups and arginine residues, carbonyl formation, aggregation characteristics, and fluorescent lipofuscin-like pigments (LFLP) fluorescence are more severe at (E,E)-2,4-decadienal concentrations of 4-10 mm, whereas the conformational changes are more significant at low concentrations (0.1-2 mm). In the BSA modified by 1-10 mm (E,E)-2,4-decadienal, the microenvironment of tryptophan residues to become more hydrophobic, the structure became compact, hydrophobic binding sites decreases, molecular weight and particle size increases, and covalently cross-linked heterogeneous aggregates increases. At the same time, the relationship between the oxidation parameters and samples is explained using principal component analysis and hierarchical cluster analysis. Practical Applications: (E,E)-2,4-decadienal is highly electrophilically active with biomacromolecules. However, compared to the widely studied malonaldehyde (MDA), acrolein (ACR), 4-hydroxynonenal (HNE), and 4-oxo-trans-2-nonenal (ONE)-protein adducts, research on the modification of a protein by (E,E)-2,4-decadienal is insufficient, and the chemical nature of (E,E)-2,4-decadienal-protein adducts is not clear. This study may be useful for extending our understanding of the specific role of (E,E)-2,4-decadienal in the formation of modified proteins during the occurrence of chronic diseases and provides a theoretical reference for food quality and safety problems caused by protein carbonylation during processing and storage.
“…When incubated with 0-3 mm linoleic acid, the protein surface hydrophobicity increased as the originally occluded hydrophobic groups were exposed to the protein surface. [63] The surface hydrophobicity of the tropomyosin decreased with an increase in HNE (0-1.0 mm), as previously reported. According to the authors of the study, the decrease in HNE modified shrimp tropomyosin surface hydrophobicity may be attributed to hydrophobic interactions of amino acid, modification of the exposed hydrophobic residues, and the hydrophilic group formation (e.g., protein carbonyl groups).…”
Protein modification by active aldehydes is associated with ageing and some chronic diseases, and it is closely related to food quality and safety. In this study, the modification of bovine serum albumin (BSA) using trans,trans-2,4-decadienal at various concentrations (0-10 mm) is investigated. The results show that the changes in the number of free amino groups and arginine residues, carbonyl formation, aggregation characteristics, and fluorescent lipofuscin-like pigments (LFLP) fluorescence are more severe at (E,E)-2,4-decadienal concentrations of 4-10 mm, whereas the conformational changes are more significant at low concentrations (0.1-2 mm). In the BSA modified by 1-10 mm (E,E)-2,4-decadienal, the microenvironment of tryptophan residues to become more hydrophobic, the structure became compact, hydrophobic binding sites decreases, molecular weight and particle size increases, and covalently cross-linked heterogeneous aggregates increases. At the same time, the relationship between the oxidation parameters and samples is explained using principal component analysis and hierarchical cluster analysis. Practical Applications: (E,E)-2,4-decadienal is highly electrophilically active with biomacromolecules. However, compared to the widely studied malonaldehyde (MDA), acrolein (ACR), 4-hydroxynonenal (HNE), and 4-oxo-trans-2-nonenal (ONE)-protein adducts, research on the modification of a protein by (E,E)-2,4-decadienal is insufficient, and the chemical nature of (E,E)-2,4-decadienal-protein adducts is not clear. This study may be useful for extending our understanding of the specific role of (E,E)-2,4-decadienal in the formation of modified proteins during the occurrence of chronic diseases and provides a theoretical reference for food quality and safety problems caused by protein carbonylation during processing and storage.
“…The Raman peak corresponding to disulfide bonds typically appears in the range of 510–540 cm −1 [47] . After protein heating from 20 to 80 ℃, the sulfhydryl group transitions to a stable disulfide bond to form a gel [48] . Therefore, the changes in the disulfide-bond peak indicated the denatured protein aggregation level.…”
“…In addition, oxidation of tryptophan and protein aggregation with protein unfolding may also decrease fluorescence intensity [47] . However, the intrinsic fluorescence increased with further treatment (12 min), possibly because of the aggregation of proteins and specific modification of tryptophan residues in MPs, resulting in lesser exposure of tryptophan residues to the aqueous environment [48] . Fig.…”
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