title: Proteomic Investigation of Protein Profile Changes and Amino Acid Residue Level Modification in Cooked Lamb Meat: The Effect of Boiling.
abstract: Hydrothermal treatment (heating in water) is a common method of general food processing and preparation. For red-meat-based foods, boiling is common; however, how the molecular level effects of this treatment correlate to the overall food properties is not yet well-understood. The effects of differing boiling times on lamb meat and the resultant cooking water were here examined through proteomic evaluation. The longer boiling time was found to result in increased protein aggregation involving particularly proteins such as glyceraldehyde-3-phosphate dehydrogenase, as well as truncation in proteins such as in α-actinin-2. Heat-induced protein backbone cleavage was observed adjacent to aspartic acid and asparagine residues. Side-chain modifications of amino acid residues resulting from the heating, including oxidation of phenylalanine and formation of carboxyethyllysine, were characterized in the cooked samples. Actin and myoglobin bands from the cooked meat per se remained visible on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, even after significant cooking time. These proteins were also found to be the major source of observed heat-induced modifications. This study provides new insights into molecular-level modifications occurring in lamb meat proteins during boiling and a protein chemistry basis for better understanding the effect of this common treatment on the nutritional and functional properties of red-meat-based foods.
authors.affiliation: Food & Bio-Based Products, AgResearch Lincoln Research Centre , Private Bag 4749, Christchurch 8140, New Zealand.|Wine, Food & Molecular Biosciences, Faculty of Agriculture and Life Sciences, Lincoln University , P.O. Box 85084, Canterbury 7647, New Zealand.
authors.forename: Tzer-Yang
authors.initials: TY
authors.lastname: Yu
authors.affiliation: Wine, Food & Molecular Biosciences, Faculty of Agriculture and Life Sciences, Lincoln University , P.O. Box 85084, Canterbury 7647, New Zealand.
authors.forename: James D
authors.initials: JD
authors.lastname: Morton
authors.affiliation: Food & Bio-Based Products, AgResearch Lincoln Research Centre , Private Bag 4749, Christchurch 8140, New Zealand.|Biomolecular Interaction Centre, University of Canterbury , Private Bag 4800, Christchurch 8140, New Zealand.
authors.forename: Stefan
authors.initials: S
authors.lastname: Clerens
authors.affiliation: Food & Bio-Based Products, AgResearch Lincoln Research Centre , Private Bag 4749, Christchurch 8140, New Zealand.|Wine, Food & Molecular Biosciences, Faculty of Agriculture and Life Sciences, Lincoln University , P.O. Box 85084, Canterbury 7647, New Zealand.|Riddet Institute, Massey University , Palmerston North 4442, New Zealand.|Biomolecular Interaction Centre, University of Canterbury , Private Bag 4800, Christchurch 8140, New Zealand.
authors.forename: Jolon M
authors.initials: JM
authors.lastname: Dyer
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D003296:Cooking; D008460:Meat / Q000032:analysis*; D009124:Muscle Proteins / Q000737:chemistry*; D018482:Muscle, Skeletal / Q000737:chemistry; D040901:Proteomics; D012756:Sheep
chemical_list: D000596:Amino Acids; D009124:Muscle Proteins
keywords: cooking; lamb; meat; protein modifications; proteomics; sheep