Fractionation, Purification and Some Properties of Proteolytic Enzymes from Stem Bromelain

Abstract

The heterogeneity of the proteolytic enzymes in the stem bromelain was investigated by the isoelectric focusing with carrier ampholytes. The isoelectric focusing of the stem bromelain demonstrated the presence of two types of proteolytic enzymes which were distinguishable from each other by their isoelectric points. One of these was a basic protein having an isoelectric point of 9.45. This basic enzyme comprised almost all of basic protein which are found in stem bromelain. The other was an acidic protein having an isoelectric point near pH 4.7. This was a minor compooent. The purification of the two enzymes was carried out by use of chromatographics on Chi-Sephadex, DEAE-Sephadex and Sephadex at pH 7.0. © 1971, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.