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Stem Bromelain: An Enzyme That Naturally Facilitates Oriented Immobilization

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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

Document Type: Research Article


Affiliations: Interdisciplinary Biotechnology Unit and Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.

Publication date: 2007-03-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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