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Effect of Heating Temperature and Muscle Type on Porcine Muscle Extracts as Determined by Reverse Phase High Performance Liquid Chromatography
Author(s) -
McCORMICK R.J.,
KROPF D.H.,
REECK G.R.,
HUNT M.C.,
KASTNER C.L.
Publication year - 1987
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1987.tb05859.x
Subject(s) - myoglobin , high performance liquid chromatography , chemistry , longissimus dorsi , chromatography , lactate dehydrogenase , longissimus , biochemistry , anatomy , enzyme , food science , biology
ABSTRACT Samples from porcine longissimus muscles were heated to temperatures ranging from 40–80°C to reach endpoint temperatures (0 min) or held at endpoint temperature for 30 min. Proteins in water‐soluble extracts of these samples were separated and quantified by reverse phase high performance liquid chromatography (RP‐HPLC). After heating to 60°C for 0 min or to 55°C and holding for 30 min, lactate dehydrogenase (LDH), pyruvate kinase (PK) and myoglobin appeared to comprise the bulk of the remaining soluble protein. RP‐HPLC analysis of water soluble extracts from longissimus dorsi, serratus ventralis and psoas major muscles from barrows and sows indicated differences in proportions of LDH and myoglobin.