Poultry Muscle as Food

Degradation of inosine-5′-monophosphate (IMP) in aqueous and in layering chicken muscle fibre systems: Effect of pH and temperature

“…On the other hand, in the case of leg meat fibres, the IMP degradation at pH 11 was higher (Pp0:05) at 80 and 100 1C and lower at 120 1C compared to corresponding values at pH 2. Such differences between breast and leg meat fibres on IMP degradation could be due to different amino acid contents in fibres and due to differences in physiological functions of these muscles (Addis, 1986). Meynier and Mottram (1995) observed that Maillard reaction between the amino acids glycine, lysine, cysteine or methionine and sugars in buffer was pH dependent with the intensity of browning increasing with pH and suggested protonation of functional group of the amino acid is important in Maillard reaction.…”

Effect of water activity and temperature on degradation of 5′-inosine monophosphate in a meat model system

“…The meat fiber allowed easy control of a w in the system and the biological variation could also be minimized. Since there are differences in chemical composition, flavor and texture of two types of muscles (Addis, 1986), it is necessary to understand the degree of degradation of IMP as a flavor precursor and its degraded products under identified conditions in both the types of muscles. Against this background, the effect of different water activity and temperature conditions on the degradation of IMP in a meat fiber system was evaluated.…”

Glycogen debranching enzyme and some other factors relating to post‐mortem pH decrease in poultry muscles

“…1 Chicken pectoralis superficialis muscle is composed almost entirely of glycolytic white αW fibres 2,3 while thigh muscles are more oxidative. Nevertheless, the proportion of αW fibres in thigh muscles exceeds 50%, with only a few percent oxidative βR fibres.…”