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Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/2447

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dc.contributor.authorTyagi, Renu-
dc.contributor.authorGupta, M N-
dc.identifier.citationProcess Biochemistry, 29(6), 443-448p.en
dc.description.abstractThe acylation of amino groups of proteins by pyromellitic dianhydride (PMDA) leads to an increase in negative charges on the protein surface by 4 units for every amino group modified. This reaction has been used to modify enzymes for the purpose of adsorption on DEAE-cellulose. The 49% amino groups of amyloglucosidase were modified with 90% residual enzyme activity. Whereas the native enzyme bound to DEAE-cellulose and could be eluted out with 0·1 sodium chloride, the modified enzyme exhibited stronger binding and could only be eluted with 0·25 sodium chloride. In the case of adsorbed native enzyme, heating at 60°C for 1 h led to desorption of 97% protein. In the case of the modified enzyme, the immobilized preparation retained full enzyme activity under similar conditions. beta-Glucosidase (which did not bind to DEAE-cellulose) upon modification with PMDA was found to bind to DEAE-cellulose and could be eluted out with 97% protein recovery by washing with 0·2 sodium chloride. Thus, chemical modification with PMDA may be a useful and general strategy for obtaining enzyme derivatives for reversible adsorption on anion exchangers.en
dc.format.extent197196 bytes-
dc.subjectpyromellitic dianhydrideen
dc.subjectamino groupen
dc.titleNoncovalent and reversible immobilization of chemically modified amyloglucosidase and beta-glucosidase on DEAE-celluloseen
Appears in Collections:Chemistry

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