title: Proteomic investigation of protein profile changes and amino acid residue-level modification in cooked lamb longissimus thoracis et lumborum: The effect of roasting.
abstract: Protein modifications of meat cooked by typical dry-heat methods (e.g., roasting) are currently not well understood. The present study utilised a shotgun proteomic approach to examine the molecular-level effect of roasting on thin lamb longissimus thoracis et lumborum patties, in terms of changes to both the protein profile and amino acid residue side-chain modifications. Cooking caused aggregation of actin, myosin heavy chains and sarcoplasmic proteins. Longer roasting time resulted in significantly reduced protein extractability as well as protein truncation involving particularly a number of myofibrillar and sarcoplasmic proteins, e.g., 6-phosphofructokinase, beta-enolase, l-lactate dehydrogenase A chain, alpha-actinin-3, actin and possibly myosin heavy chains. Modifications that have potential influence on nutritional properties, including carboxyethyllysine and a potentially glucose-derived N-terminal Amadori compound, were observed in actin and myoglobin after roasting. This study provided new insights into molecular changes resulting from the dry-heat treatment of meat, such as commonly used in food preparation.
authors.affiliation: Food & Bio-Based Products, AgResearch Lincoln Research Centre, Private Bag 4749, Christchurch 8140, New Zealand; Wine, Food & Molecular Biosciences, Lincoln University, Faculty of Agriculture and Life Sciences, PO Box 85084, Canterbury 7647, New Zealand. Electronic address: Robert.Yu@agresearch.co.nz.
authors.forename: Tzer-Yang
authors.initials: TY
authors.lastname: Yu
authors.affiliation: Wine, Food & Molecular Biosciences, Lincoln University, Faculty of Agriculture and Life Sciences, PO 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, Lincoln University, Faculty of Agriculture and Life Sciences, PO 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: D000185:Actinin / Q000737:chemistry; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002853:Chromatography, Liquid; D003296:Cooking; D006358:Hot Temperature; D007770:L-Lactate Dehydrogenase / Q000737:chemistry; D009124:Muscle Proteins / Q000737:chemistry; D009210:Myofibrils / Q000737:chemistry; D064170:Paraspinal Muscles / Q000737:chemistry*; D010732:Phosphofructokinase-1 / Q000737:chemistry; D010751:Phosphopyruvate Hydratase / Q000737:chemistry; D040901:Proteomics; D000069466:Red Meat / Q000032:analysis*; D012519:Sarcoplasmic Reticulum / Q000737:chemistry*; D012756:Sheep; D053719:Tandem Mass Spectrometry
chemical_list: D000596:Amino Acids; D009124:Muscle Proteins; D000185:Actinin; D007770:L-Lactate Dehydrogenase; D010732:Phosphofructokinase-1; D010751:Phosphopyruvate Hydratase
keywords: Cooking; Lamb; Meat; Protein modifications; Proteomics; Sheep