| Autor: |
Jasti, Lakshmi Swarnalatha, Dola, Sandhya Rani, Kumaraguru, Thenkrishnan, Bajja, Sreedhar, Fadnavis, Nitin W., Addepally, Uma, Rajdeo, Kishor, Ponrathnam, Surendra, Deokar, Sarika |
| Předmět: |
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| Zdroj: |
Biotechnology Progress; Mar2014, Vol. 30 Issue 2, p317-323, 7p |
| Abstrakt: |
Allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) shows excellent bovine serum albumin (BSA) adsorption (up to 16% (w/w)) at pH 8.0 and the adsorbed BSA is strongly bound. This protein-coated polymer provides a novel matrix with naturally existing functional groups such as thiol, amino, and carboxylic acid that are available for covalent immobilization of functional enzymes. Employing appropriate strategies, trypsin as a model protein was covalently bound to BSA-coated matrix both independently, and in a stepwise manner on the same matrix, with less than 5% loss of enzyme activity during immobilization. Glutaraldehyde crosslinking after immobilization provide stable enzyme preparation with activity of 510 units/g recycled up to six times without loss of enzyme activity. AFM studies reveal that the polymer surface has protein peaks and valleys rather than a uniform monolayer distribution of the protein and the immobilized enzyme preparation can best be described as polymer supported cross-linked enzyme aggregates (CLEAs). © 2014 American Institute of Chemical Engineers Biotechnol. Prog., 30:317-323, 2014 [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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