The enzyme from ginger rhizomes was purified to electrophoretic
homogeneity as evidenced by the presence of a single protein
band on 15% SDS–PAGE gel, which also suggested a monomeric
nature of the enzyme (Fig. 1a). The molecular mass of the purified
enzyme was computed as 36 kDa. Previously, different molecular
mass of ginger protease has been reported in literature. In the
study of n reported in literature. In the
study of Ichikawa et al. (1973), the molecular weights of both
GP-I and GP-II (ginger proteases) were estimated to be 22.5 kDa. separated ginger proteases into three fractions each with 29 kDa, while