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Meat Sci. 2016 Sep;119:80-8. doi: 10.1016/j.meatsci.2016.04.024. Epub 2016 Apr 21.

Proteomic investigation of protein profile changes and amino acid residue-level modification in cooked lamb longissimus thoracis et lumborum: The effect of roasting.

Author information

1
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.
2
Wine, Food & Molecular Biosciences, Lincoln University, Faculty of Agriculture and Life Sciences, PO Box 85084, Canterbury 7647, New Zealand.
3
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.
4
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.

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.

KEYWORDS:

Cooking; Lamb; Meat; Protein modifications; Proteomics; Sheep

PMID:
27150797
DOI:
10.1016/j.meatsci.2016.04.024
[Indexed for MEDLINE]

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