title: Proteome basis for intramuscular variation in color stability of beef semimembranosus.
abstract: The objective of the present study was to characterize the proteome basis for intramuscular color stability variations in beef semimembranosus. Semimembranosus muscles from eight carcasses (n=8) were fabricated into 2.54-cm thick color-labile inside (ISM) and color-stable outside (OSM) steaks. One steak for sarcoplasmic proteome analysis was immediately frozen, whereas other steaks were allotted to retail display under aerobic packaging. Color attributes were evaluated instrumentally and biochemically on 0, 2, and 4days. Sarcoplasmic proteome was analyzed using two-dimensional electrophoresis and tandem mass spectrometry. ISM steaks demonstrated greater (P<0.01) abundance of glycolytic enzymes (fructose-bisphosphate aldolase A, phosphoglycerate mutase 2, and beta-enolase) and phosphatidylethanolamine-binding protein 1 than their OSM counterparts. Possible rapid post-mortem glycolysis in ISM, insinuated by over-abundance of glycolytic enzymes, could lead to rapid pH decline during early post-mortem, which in turn could potentially compromise its color stability. These results indicated that differential abundance of sarcoplasmic proteome contributes to intramuscular variations in beef color stability.
authors.affiliation: Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA.
authors.forename: Mahesh N
authors.initials: MN
authors.lastname: Nair
authors.affiliation: Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA. Electronic address: spsuma2@uky.edu.
authors.forename: Surendranath P
authors.initials: SP
authors.lastname: Suman
authors.affiliation: Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA; Department of Livestock Products Technology, Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana 241004, Punjab, India.
authors.forename: Manish K
authors.initials: MK
authors.lastname: Chatli
authors.affiliation: Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA.
authors.forename: Shuting
authors.initials: S
authors.lastname: Li
authors.affiliation: Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA; Kalsec, Inc., Kalamazoo, MI 49005, USA.
authors.forename: Poulson
authors.initials: P
authors.lastname: Joseph
authors.affiliation: Proteomics Core Facility, University of Kentucky, Lexington, KY 40506, USA.
authors.forename: Carol M
authors.initials: CM
authors.lastname: Beach
authors.affiliation: Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, USA.
authors.forename: Gregg
authors.initials: G
authors.lastname: Rentfrow
mesh_terms: D000818:Animals; D002417:Cattle / Q000235:genetics / Q000502:physiology; D005786:Gene Expression Regulation / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D015227:Lipid Peroxidation; D008460:Meat / Q000032:analysis*; D009124:Muscle Proteins / Q000235:genetics / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D010858:Pigmentation; D010860:Pigments, Biological; D020543:Proteome / Q000235:genetics*; D012519:Sarcoplasmic Reticulum / Q000378:metabolism
chemical_list: D009124:Muscle Proteins; D010860:Pigments, Biological; D020543:Proteome
keywords: Beef color; Color stability; Glycolytic enzymes; Sarcoplasmic proteome; Semimembranosus