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Bioaffinity Based Immobilization of Enzymes

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Book cover Thermal Biosensors, Bioactivity, Bioaffinitty

Part of the book series: Advances in Biochemical Engineering/Biotechnology ((ABE,volume 64))

Abstract

Procedures that utilize the affinities of biomolecules and ligands for the immobilization of enzymes are gaining increasing acceptance in the construction of sensitive enzyme-based analytical devices as well as for other applications. The strong affinity of polyclonal/monoclonal antibodies for specific enzymes and those of lectins for glycoenzymes bearing appropriate oligosaccharides have been generally employed for the purpose. Potential of affinity pairs like cellulose-cellulose binding domain bearing enzymes and immobilized metal ion-surface histidine bearing enzymes has also been recognised. The bioaffinity based immobilization procedures usually yield preparations exhibiting high catalytic activity and improved stability against denaturation. Bioaffinity based immobilizations are usually reversible facilitating the reuse of support matrix, orient the enzymes favourably and offer the possibility of enzyme immobilization directly from partially pure enzyme preparations or even cell lysates. Enzyme lacking innate ability to bind to various affinity supports can be made to bind to them by chemically or genetically linking the enzymes with appropriate polypeptides/domains like the cellulose binding domain, protein A, histidine-rich peptides, single chain antibodies, etc.

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  1. Department of Biochemistry, Faculty of Life Sciences and Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202 002, India

    M. Saleemuddin

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P. K. Bhatia B. Danielsson P. Gemeiner S. Grabley F. Lammers A. Mukhopadhyay K. Ramanathan M. Saleemuddin T. Scheper V. Stefuca R. Thiericke B. Xie

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Saleemuddin, M. (1999). Bioaffinity Based Immobilization of Enzymes. In: Bhatia, P.K., et al. Thermal Biosensors, Bioactivity, Bioaffinitty. Advances in Biochemical Engineering/Biotechnology, vol 64. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-49811-7_6

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  • DOI: https://doi.org/10.1007/3-540-49811-7_6

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