Changed dynamics in myofibrillar protein aggregation as a consequence of heating time and temperature.
The kinetics of protein aggregation induced by cooking were investigated in pig M. Longissimus dorsi. The 4 day aged muscles were cooked either in water or under dry heat conditions for 30 min. Four temperatures from 50 to 100 degrees C were tested for the "in water" cooking mode and an additional temperature of 140 degrees C was tested in the dry condition. Raw and cooked meat specimens were ground in a KCl solution. After delipidation of the meat extract, protein aggregation was evaluated with a laser granulometer (Sysmex FPIA-3000) which enabled reliable and reproducible characterization of particle number, size, and shape distribution using automated imaging techniques. The cooking mode (dry/"in water") did not affect the granulometry measurements. But, increasing cooking time and temperature affected the number, the size, and the shape of particles. An important decrease in particle number was observed during cooking in parallel with a reduction in particle size and a change in circularity. From these data a model with intermediary fibrillar aggregates and final amorphous aggregates was proposed.
Promeyrat
A
A
INRA, UR370 Qualité des Produits Animaux, F-63122 Saint Genès-Champanelle, France.
Bax
M L
ML
Traoré
S
S
Aubry
L
L
Santé-Lhoutellier
V
V
Gatellier
Ph
P
D000818:Animals; D003296:Cooking / Q000379:methods*; D006358:Hot Temperature; D007091:Image Processing, Computer-Assisted; D008460:Meat; D008954:Models, Biological; D009124:Muscle Proteins / Q000737:chemistry*; D018482:Muscle, Skeletal / Q000737:chemistry; D009210:Myofibrils / Q000737:chemistry* / Q000648:ultrastructure; D010316:Particle Size; D013552:Swine; D013997:Time Factors; D014867:Water
D009124:Muscle Proteins; D014867:Water