The enzyme
activity was completely inhibited by the action of
ethylenediaminetetraacetic acid (EDTA) suggesting
that the collagenase enzyme isolated from the fish
waste is a metalloproteinase enzyme requiring metal
ions for enzyme activity. Dialysis against KSCN decreased
the enzyme total activity and increased its
specific activity. Sodium dodecyl sulphate polyacrylamide
gel electrophoresis (SDS-PAGE) indicated that
the purified procollagenase enzyme have only one
band at molecular weight of 50 kilodaltons (kDa).
When the enzyme was cleaved with trypsin, it was
found to consist of two subunits: a large unit with a
molecular weight of 50 kDa and a small unit with a
molecular weight of 10 kDa.
Keywords: Fish Waste; Collagenase Enzyme;
Extraction; Purification; Inhibitors; Activators