Investigation of the binding mechanism of glucoamylase to alkylamine derivatives of titanium(IV)-activated porous inorganic supports
- 30 September 1982
- journal article
- Published by Elsevier in Enzyme and Microbial Technology
- Vol. 4 (5), 337-342
- https://doi.org/10.1016/0141-0229(82)90057-6
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Immobilization of amyloglucosidase on alkylamine derivatives of metal‐link‐activated inorganic supportsBiotechnology & Bioengineering, 1981
- Fluidized‐bed immobilized‐enzyme reactor for the hydrolysis of cornstarch to glucoseBiotechnology & Bioengineering, 1979
- The Tate and Lyle carbohydrate chemistry award lecture. Transition-metal oxide chelates of carbohydrate-directed macromoleculesChemical Society Reviews, 1979
- Stability and Kinetic Properties of a Magnetic Immobilized alpha-Amylase KStarch ‐ Stärke, 1979
- Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supportsBiotechnology & Bioengineering, 1978
- Water-insoluble papain conjugates of hydrous titanium(IV) oxide and of surface-coating materials modified to contain hydrous titanium(IV) oxideJournal of the Chemical Society, Perkin Transactions 1, 1978
- Immobilisation of α‐Amylase on Polyaromatic and Titanium Compounds Incorporating a Magnetic MaterialStarch ‐ Stärke, 1977
- Microbial cells living immobilised on metal hydroxidesNature, 1976
- Hydrous titanium oxides–new supports for the simple immobilisation of enzymesJournal of the Chemical Society, Perkin Transactions 1, 1976
- Insoluble complexes of amino-acids, peptides, and enzymes with metal hydroxidesJournal of the Chemical Society, Perkin Transactions 1, 1976