Contribution of cathepsins B, L and D to muscle protein profiles correlated with texture in rainbow trout (Oncorhynchus mykiss)

Degradation of myofibrils in cultured yellowtail Seriola quinqueradiata burnt meat: effects of a myofibril-bound EDTA-sensitive protease

“…Several studies have shown that the different types of endogenous protease, such as cathepsins [12][13][14][15][16], aspartic acid proteases [17] or serine proteinases [18,19], especially the myofibril-bound serine proteinases [20,21], led to the degradation of myofibrillar proteins in fish meat.…”

The effect of vacuum packaging on physicochemical changes in rainbow trout (Oncorhynchus mykiss) during cold storage

“…Endogenous proteases also play an important role in the post mortem degradation of fish muscle protein (Godiksen et al 2009). These processes lead to a change to the textural and sensory characteristics of fish muscle.…”

Changes in the Physicochemical and Volatile Flavor Characteristics of Scomberomorus niphonius during Chilled and Frozen Storage

“…From the results, storing mackerels at temperatures of −20 and −55℃ delayed postmortem deterioration of quality, and the decrease in textural properties perhaps was attributed to the water retaining capacity and drip loss of fish muscle at lower temperature values, leading to the ordered formation of muscle protein structure (Riebroy et al, 2007). More specifically, the values of hardness, springiness, cohesiveness, and chewiness of the samples in the second stage had a tendency to decrease at all temperature, the reasons might be the breakdown of the myofibrillar structure, be ascribed mainly to the activity of lysosomal cathepsins, in particular cathepsin B, cathepsin L and cathepsin D (Godiksen et al, 2009), which were highly active in the 5 and 0℃ storage fish. eigenvalue (Zhou et al, 2011).…”