Cathepsin B was the most active cysteine proteinase in the Pacific whiting
(Merluccius productus) fish fillet, and cathepsin L in surimi when the activities of the
most active cysteine proteinases (cathepsin L, B, and H) were compared. Cathepsin L
showed maximum activity at 55°C in both fish fillet and surimi,...
Kinetic properties of the two proteases, causing textural degradation of Pacific
whiting (Merluccius productus) during heating, were compared and characterized with the
synthetic substrate, Z-Phe-Arg-NMec. Pacific whiting P-I and P-II showed the highest
specificity on Z-Phe-Arg-NMec, specific substrate for cathepsin L. The K [subscript m] of
preactivated P-I and P-II...
Proteolysis of myofibrillar proteins in Pacific whiting surimi occurs when the 50-
70°C temperature range is reached during standard cooking procedures (e.g. 90°C for 15
min). This proteolytic activity results in the softening of surimi gels. Bovine plasma
protein (BPP) is the most effective of the food-grade inhibitors used to...
Proteolytic degradation of fish flesh occurring at elevated temperatures is the
primary limitation for the commercial utilization of arrowtooth flounder (ATF).
Characterization of the autolytic activity of ATF muscle incubated at various pHs
and temperatures indicated the involvement of heat-activated proteinases active at
acidic and alkaline pHs. Further characterization of...