Stem Bromelain: An Enzyme That Naturally Facilitates Oriented Immobilization

Abstract

The lone oligosaccharide chain of stem bromelain was oxidized with periodic acid to generate aldehyde groups and the resulting oxidized enzyme coupled to amino-Sepharose in order to obtain an immobilized preparation with uniformly oriented enzyme. The immobilized bromelain exhibited high proteolytic activity and remarkably enhanced thermal stability as compared to soluble bromelain and that coupled to CNBr activated Sepharose.

Preparative purification of bromelain (EC 3.4.22.33) from pineapple fruit by high-speed counter-current chromatography using a reverse-micelle solvent system

“…The purity of the separated protein was excellent, and the band of the separated protein matched well with the standard (Fig. 5), which was found to be around 34 kDa, the same molecular weight as bromelain (Khatoon, Younus, & Saleemuddin, 2007). The UV and MS spectra of the target are shown in Fig.…”