Purification and Immobilization ofAspergillus Niger Pectinase on Magnetic Latex Beads
- 1 January 1995
- journal article
- research article
- Published by Taylor & Francis in Biocatalysis and Biotransformation
- Vol. 12 (4) , 293-298
- https://doi.org/10.3109/10242429509003191
Abstract
A commercial preparation of pectinase pectinex was purified with the help of alginate-magnetite beads. The purified pectinase was immobilized an magnetic latex beads via carbodiimide coupling. The maximum efficiency of the immobilized preparation was calculated as 81% of the total activity bound to the beads. This was at the lowest level of coupling tried. The pH optimum (pH 4.5 for both free as well as immobilized enzyme) and km (0.7 mg/ml for free enzyme; 1 mg/ml for immobilized enzyme) did not vary significantly upon immobilization. While the half life of free enzyme was calculated as 9 min., the immobilized preparation remained stable up to 3 h at 60d`C.Keywords
This publication has 6 references indexed in Scilit:
- Pectic Enzymes in Fruit and Vegetable Juice ManufacturePublished by Elsevier ,1993
- Screening for plant lectins by latex agglutination testsPhytochemistry, 1991
- Strain and process for production of polygalacturonaseEnzyme and Microbial Technology, 1990
- Isolation and purification of endo-polygalacturonase by affinity chromatography in a fluidized bed reactorThe Chemical Engineering Journal, 1989
- Dried calcium alginate/magnetite spheres: A new support for chromatographic separations and enzyme immobilizationBiotechnology & Bioengineering, 1985
- Selective purification of Aspergillus niger endopolygalacturonase by affinity chromatography on cross-linked pectic acidBiochimica et Biophysica Acta (BBA) - Enzymology, 1972