Characterization of sand as a support for immobilized enzymes
- 31 March 1976
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 18 (4) , 527-543
- https://doi.org/10.1002/bit.260180407
Abstract
The potential of sand as a support for immobilized enzymes was investigated by preparing alkylamine sand and devising methods to measure the total number of amine groups present and the fraction available for immobilization of enzymes. Alcohol dehydrogenase (alcohol:NAD oxidoreductase, EC 1.1.1.1) and lactate dehydrogenase (L‐lactate: NAD oxidoreductase, EC 1.1.1.27) were immobilized on alkylamine sand, and the stability of the immobilized protein and dehydrogenase activity was measured. Urease (urea amidohyrdrolase, EC 3.5.1.5) was also immobilized on sand to test the applicability of these methods to larger scale immobilizations. Results suggest that sand shows promise as a support for immobilized enzymes.This publication has 9 references indexed in Scilit:
- Kinetics of a hollow fiber dehydrogenase reactorBiotechnology & Bioengineering, 1975
- Lactoperoxidase Immobilization on Inorganic SupportsBiochemical Society Transactions, 1974
- Studies on the Immobilization of β-GalactosidasesBiochemical Society Transactions, 1974
- The Immobilization of Lactoperoxidase and β-Fructofuranosidase on Glass and on Sand, by the Metal-Link MethodBiochemical Society Transactions, 1974
- Multiple immobilized enzyme reactors: Determination of pyruvate and phosphoenolpyruvate concentrations using immobilized lactate dehydrogenase and pyruvate kinaseBiotechnology & Bioengineering, 1973
- Structure of Liver Alcohol Dehydrogenase at 2.9-Å ResolutionProceedings of the National Academy of Sciences, 1973
- Fluorescamine: A Reagent for Assay of Amino Acids, Peptides, Proteins, and Primary Amines in the Picomole RangeScience, 1972
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951