Bromelain purification

T, Mvradii, M. Yasui, and Y. Yasuda. Purification and physical characterization of stem bromelain. Biochemistry J 48 (1964). 

F, Yamada, N. Takabashi, and T. Munchi. Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2.X Bioctum (Tokyo) 79 1223 (1976). 

Since heterogeneity of stem bromelain was reported by Heinicke and Gortner [8], a number of studies have indicated that crude stem bromelain contains several proteolytically active components together with some nonproteolytic enzymes, inhibitors, and activators [9-31]. An extensive review of the purification procedures of different proteolytic components of crude stem bromelain up to 1976 is given by Cooreman et al. [7]. 

W. Cooreman, A. Lauwers, and S. Scharp . Proceedings purification of stem bromelain by affinity chromatography. Hoppe-Seylers Z Physiol. Chem. 555 1185 (1974). 

Bromelains.— The reactive sulphydryl groups of stem and juice bromelains have been blocked with phenylmercuriacetate during purification of the enzymes, which were further modified by reaction with 2-hydroxy-5-nitrobenzyl bromide or tetranitromethane or hydrogen peroxide. The activities of the modified enzymes towards substrates of high or low molecular weight were examined. 

Hung, T. H., Fu, J. Y., Chiang, C. L., et al. (2002). Purification and characterization of hydrolase with chitinase and chitosanase activity from commercial stem bromelain. 

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