Abstract
Fractionation and Specificity Studies on Stem Bromelain
Highlights
Bemoval of dinitrophenol was carried out according to Mills [26], and the identification of DNP-amino acids was made by paper chromatography in solvent systems of tert-amyl alcohol-phthalate at pH 6.0 or 1.5 M phosphate at pH 6.0, or two-dimensionally in tert-amyl alcohol-2 N ammonia (4: 1) followed by 1.5 M phosphate at pH 6.0
When cysteine was added to the reaction mixture, the enzyme retained activity through a longer period of incubation
Similar findings were obtained with BAEE as substrate
Summary
E$ect of DFP-DFP, dissolved in n-propanol, was preincubated with crude bromelain at 25” for 1 hour at pH 7.2, and the enzymatic activity toward casein was subsequently measured in the presence and absence of 0.001 M cysteine, under the same conditions as described for Fig. 1. Attempts were made to obtain a crystalline enzyme preparation by fractionation of stem bromelain with ammonium sulfate and sodium chloride.
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