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A Protocol for Computer-Based Protein Structure and Function Prediction
Published on: November 3, 2011
Effects of Oxidation in Vitro on Structures and Functions of Myofibrillar Protein from Beef Muscles
Qingquan Fu1, Rui Liu2, Haiou Wang1
1Jiangsu Provincial Key Construction Laboratory of Special Biomass Waste Resource Utilization, School of Food Science , Nanjing Xiaozhuang University , Nanjing , Jiangsu 211171 , People's Republic of China.
Abstract:
The main purpose of this study was to investigate the effects of oxidation in vitro on the biochemical properties of myofibrillar protein isolates (MPIs) from beef muscles. MPIs were incubated at 4 °C for 24 h with hydroxyl-radical-generating systems consisting of 0.01 mM FeCl3 and 0.1 mM ascorbic acid plus 0, 0.2, 1, 5, 10, and 20 mM hydrogen peroxide. The results showed that oxidation caused drastically structural changes in bovine MPIs. The carbonyl content, the surface hydrophobicity, and the particle diameter of MPIs were significantly increased, while the free sulfhydryl group content was dramatically decreased with increasing hydrogen peroxide concentrations. Oxidation caused the protein aggregations through cross-linking between proteins and amino acids. Proteomics study identified protein sites in which they were easy to be oxidized. Oxidized catalytic activities and binding sites of enzymes that were susceptible to oxidation were also identified.
Insights
Oxidation significantly alters beef myofibrillar protein isolates (MPIs), increasing structural changes and protein aggregation. This study details how hydrogen peroxide affects MPI biochemical properties and identifies susceptible protein sites.
Area of Science:
- Food Science
- Biochemistry
- Protein Chemistry
Background:
- Myofibrillar protein isolates (MPIs) are crucial in meat products.
- Understanding protein oxidation is vital for meat quality and safety.
- In vitro oxidation models help elucidate biochemical changes.
Purpose of the Study:
- To investigate the in vitro effects of oxidation on beef MPI biochemical properties.
- To determine the impact of varying hydrogen peroxide concentrations on MPI structure and function.
- To identify specific protein sites and enzyme activities affected by oxidation.
Main Methods:
- Beef MPIs were incubated with a hydroxyl-radical-generating system.
- Hydrogen peroxide concentrations ranged from 0 to 20 mM.
- Biochemical analyses included carbonyl content, surface hydrophobicity, particle diameter, and free sulfhydryl groups.
- Proteomics was employed to identify oxidized protein sites and enzyme activities.
Main Results:
- Oxidation significantly increased carbonyl content, surface hydrophobicity, and particle diameter of MPIs.
- Free sulfhydryl group content decreased with increasing hydrogen peroxide levels.
- Protein aggregation occurred due to cross-linking between proteins and amino acids.
- Proteomics identified specific oxidation-prone sites on proteins and susceptible enzyme activities.
Conclusions:
- In vitro oxidation drastically alters the biochemical and structural properties of beef MPIs.
- Hydrogen peroxide concentration is a key factor in the extent of MPI oxidation and aggregation.
- Oxidation affects specific amino acid residues and enzyme functions within MPIs, impacting protein integrity.
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