The Electrophoretic Profile Myofibrillar Proteins Extracted From Camel Muscles, Kept in Various Modes

The Electrophoretic Profile Myofibrillar Proteins Extracted From Camel Muscles, Kept in Various Modes



Benaissa Atika, Babelhadj Baaissa, Bayoussef Zahia, Smili Hanane, Becila Samira, Ould el hadj-Khellil Aminata



 Changes in electrophoretic profiles of myofibrillar protein (MFP) in the
Longissimus thoracis (LD) of young camels (2 to 4 years), preserved by
refrigeration has been treated or not by lactic acid solution 4% or
citric acid 1%, were followed during the post-mortem time at the
following times: 1, 2, 4, 6, 8, 10, 12, 24 and 48 hours. The cold
preservation for 48 hours has not shown any particular distinctions in
the protein profiles of this muscle. Changes related to the type of
treatment were recorded during the storage time. Proteolysis of the
myofibrillar fraction was earlier in this muscle in the case of
treatment with one of two solutions of organic acids used, particularly
in the case of using lactic acid. Indeed, these changes have affected at
the first hour after slaughter the proteolysis of the myofibrillar
proteins. Fragments of low molecular weight (42, 36, 33, 26, 23, 18, 16,
14 and 13 kDa) have been identified. The electrophoretic analysis
showed that during refrigeration, LD treated with a solution of lactic
acid is more sensitive to disruption phenomena and muscle protein
proteolysis that lots of this muscle that even in the case of
preservation by refrigeration only or by refrigeration



http://ijeab.com/upload_document/issue_files/1%20IJEAB-JAN-2017-50-The%20Electrophoretic%20Profile%20Myofibrillar%20Proteins%20Extracted.pdf



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