Investigation of the operational stabilities and kinetics of glucoamylase immobilized on 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) , 343-348
- https://doi.org/10.1016/0141-0229(82)90058-8
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Investigation of the binding mechanism of glucoamylase to alkylamine derivatives of titanium(IV)-activated porous inorganic supportsEnzyme and Microbial Technology, 1982
- Immobilization of amyloglucosidase on alkylamine derivatives of metal‐link‐activated inorganic supportsBiotechnology & Bioengineering, 1981
- Influence of coupling conditions on activity and operational stability of glucoamylase immobilized on titanium (IV)-activated controlled pore glassEnzyme and Microbial Technology, 1981
- An investigation of the properties of glucoamylase immobilized on glass beads involving 5-diazosalicylic acid bonded to a titanium (IV) oxide filmEnzyme and Microbial Technology, 1979
- Fluidized‐bed immobilized‐enzyme reactor for the hydrolysis of cornstarch to glucoseBiotechnology & Bioengineering, 1979
- A new model to describe enzyme inactivationBiotechnology & Bioengineering, 1978
- Some factors affecting the stability of glucoamylase immobilized on hornblende and on other inorganic supportsBiotechnology & Bioengineering, 1978
- Multiphase catalysis. II. Hollow fiber catalystsBiotechnology & Bioengineering, 1971
- Water-Insoluble Derivatives of Enzymes, Antigens, and AntibodiesAnnual Review of Biochemistry, 1966
- [17] Amylases, α and βPublished by Elsevier ,1955