Proteome basis for intramuscular variation in color stability of beef semimembranosus

Mahesh N. Nair; Surendranath P. Suman; Manish K. Chatli; Shuting Li; Poulson Joseph; Carol M. Beach; Gregg Rentfrow

doi:10.1016/j.meatsci.2015.11.003

Proteome basis for intramuscular variation in color stability of beef semimembranosus

Mahesh N. Nair, Surendranath P. Suman, Manish K. Chatli, Shuting Li, Poulson Joseph, Carol M. Beach, Gregg Rentfrow

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

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 4. days. 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.

Original language	English
Pages (from-to)	9-16
Number of pages	8
Journal	Meat Science
Volume	113
DOIs	https://doi.org/10.1016/j.meatsci.2015.11.003
State	Published - Mar 1 2016

Bibliographical note

Funding Information:
This project was supported by the Agriculture and Food Research Initiative Grant 2012-67018-30166 from the USDA National Institute of Food and Agriculture . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research . This is publication number 15-07-001 of the Kentucky Agricultural Experiment Station and is published with the approval of the director.

Publisher Copyright:
© 2015 Elsevier Ltd.

Keywords

Beef color
Color stability
Glycolytic enzymes
Sarcoplasmic proteome
Semimembranosus

ASJC Scopus subject areas

Food Science

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10.1016/j.meatsci.2015.11.003

Cite this

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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 4. days. 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.",

keywords = "Beef color, Color stability, Glycolytic enzymes, Sarcoplasmic proteome, Semimembranosus",

author = "Nair, {Mahesh N.} and Suman, {Surendranath P.} and Chatli, {Manish K.} and Shuting Li and Poulson Joseph and Beach, {Carol M.} and Gregg Rentfrow",

note = "Funding Information: This project was supported by the Agriculture and Food Research Initiative Grant 2012-67018-30166 from the USDA National Institute of Food and Agriculture . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research . This is publication number 15-07-001 of the Kentucky Agricultural Experiment Station and is published with the approval of the director. Publisher Copyright: {\textcopyright} 2015 Elsevier Ltd.",

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AU - Joseph, Poulson

AU - Beach, Carol M.

AU - Rentfrow, Gregg

N1 - Funding Information: This project was supported by the Agriculture and Food Research Initiative Grant 2012-67018-30166 from the USDA National Institute of Food and Agriculture . Mass spectrometric analysis was performed at the University of Kentucky's Proteomics Core Facility, supported in part by funds from the Office of the Vice President for Research . This is publication number 15-07-001 of the Kentucky Agricultural Experiment Station and is published with the approval of the director. Publisher Copyright: © 2015 Elsevier Ltd.

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Proteome basis for intramuscular variation in color stability of beef semimembranosus

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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