Microstructural changes in m. rectus abdominis bovine muscle after heating.
A histological and ultrastructural study was conducted to characterize changes in beef muscle structure after heating. Pieces of rectus abdominis muscle were heated at 100 degrees C over varying time frames from 15 min to 60 min and at 270 degrees C for 1 min; samples were then prepared for optical and transmission electron microscopy. After 15 min of heating, at 100 degrees C, a lateral shrinkage in fibre of 48% and an increase in gaps between the myofibrillar masses of 27% was noted. No more significant evolution was observed as heating duration escalated. The ultrastructure showed strong myofibril to sarcolemma detachments in which granular aggregates, coming in part from myofibrillar proteins, are stored. Neighbouring muscle fibres showed strong heterogeneity in morphological behaviour after thermal treatment, suggesting that differences in composition and structure of the cytoskeleton proteins in the different fibres can cause denaturation/shrinkage of the proteins at different times along the timescale of microstructural changes during heating. Short heating at high temperatures expanded the gaps between myofibrillar mass, but the overall changes in the ultrastructure were similar to those obtained when heating at 100 degrees C.
Astruc
Thierry
T
INRA de Clermont-Ferrand-Theix, UR370 QuaPA, F-63122 St Genès Champanelle, France. thierry.astruc@clermont.inra.fr
Gatellier
Philippe
P
Labas
Roland
R
Lhoutellier
Véronique Santé
VS
Marinova
Penka
P
D000818:Animals; D002417:Cattle; D003296:Cooking; D003599:Cytoskeleton / Q000378:metabolism / Q000648:ultrastructure; D006358:Hot Temperature; D008460:Meat; D018485:Muscle Fibers, Skeletal / Q000378:metabolism / Q000648:ultrastructure*; D009124:Muscle Proteins / Q000378:metabolism / Q000648:ultrastructure*; D011489:Protein Denaturation; D017568:Rectus Abdominis / Q000378:metabolism / Q000648:ultrastructure*; D012508:Sarcolemma / Q000378:metabolism / Q000648:ultrastructure
D009124:Muscle Proteins