Stem Bromelain: An Enzyme That Naturally Facilitates Oriented Immobilization

Hafeeza      Khatoon; Hina      Younus; Mohammad      Saleemuddin

doi:10.2174/092986607780090900

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.

Keywords: Bromelain, oligosaccharide chain, oriented immobilization, proteolytic activity, stability

« Previous Next »

Rights & Permissions Print Cite

Protein & Peptide Letters

Title: Stem Bromelain: An Enzyme That Naturally Facilitates Oriented Immobilization

Volume: 14 Issue: 3

Author(s): Hafeeza Khatoon, Hina Younus and Mohammad Saleemuddin

Affiliation:

Keywords: Bromelain, oligosaccharide chain, oriented immobilization, proteolytic activity, stability

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.

Export Options

Export File:

RIS (for EndNote, Reference Manager, ProCite)

BibTeX

Text

Content:

Citation Only

Citation and Abstract

About this article

Cite this article as:

Khatoon Hafeeza, Younus Hina and Saleemuddin Mohammad, Stem Bromelain: An Enzyme That Naturally Facilitates Oriented Immobilization, Protein & Peptide Letters 2007; 14 (3) . https://dx.doi.org/10.2174/092986607780090900