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Understanding tenderness variability and ageing changes in buffalo meat: biochemical, ultrastructural and proteome characterization

Published online by Cambridge University Press:  06 January 2016

M. Kiran ,
B. M. Naveena ,
K. S. Reddy ,
M. Shahikumar ,
V. R. Reddy ,
V. V. Kulkarni ,
S. Rapole  and
T. H. More
M. Kiran*
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
B. M. Naveena
Affiliation:
National Research Centre on Meat, Chengicherla, Hyderabad 500092, India
K. S. Reddy
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
M. Shahikumar
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
V. R. Reddy
Affiliation:
Department of Livestock Products Technology, College of Veterinary Sciences, Hyderabad 500030, India
V. V. Kulkarni
Affiliation:
National Research Centre on Meat, Chengicherla, Hyderabad 500092, India
S. Rapole
Affiliation:
Proteomics Lab, National Centre for Cell Science, Pune 411007, India
T. H. More
Affiliation:
Proteomics Lab, National Centre for Cell Science, Pune 411007, India
*
†E-mail: kiranm.321@rediffmail.com
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Abstract

Understanding of biological impact of proteome profile on meat quality is vital for developing different approaches to improve meat quality. Present study was conducted to unravel the differences in biochemical, ultrastructural and proteome profile of longissimus dorsi muscle between buffaloes (Bubalus bubalis) of different age groups (young v. old). Higher (P<0.05) myofibrillar and total protein extractability, muscle fibre diameter, and Warner-Bratzler shear force (WBSF) values was observed in old buffalo meat relative to meat from young buffaloes. Scanning electron microscopy photographs revealed reduced fibre size with increased inter-myofibrillar space in young compared with old buffalo meat. Transmission electron microscopy results revealed longer sarcomeres in young buffalo meat relative to meat from old buffaloes. Proteomic characterization using two-dimensional gel electrophoresis (2DE) found 93 differentially expressed proteins between old and young buffalo meat. Proteome analysis using 2DE revealed 191 and 95 differentially expressed protein spots after 6 days of ageing in young and old buffalo meat, respectively. The matrix assisted laser desorption ionization time-of flight/time-of flight mass spectrometry (MALDI-TOF/TOF MS) analysis of selected gel spots helped in identifying molecular markers of tenderness mainly consisting of structural proteins. Protein biomarkers identified in the present study have the potential to differentiate meat from young and old buffaloes and pave the way for optimizing strategies for improved buffalo meat quality.

Keywords

buffalo meatproteomicsmass spectrometrytendernessultrastructure
Type
Research Article
Information
animal , Volume 10 , Issue 6 , June 2016 , pp. 1007 - 1015
Copyright
© The Animal Consortium 2016 

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