New method for the determination of kinetic constants for two‐stage deactivation of biocatalysts
Open Access
- 1 June 1984
- journal article
- review article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 26 (6) , 620-622
- https://doi.org/10.1002/bit.260260610
Abstract
No abstract availableThis publication has 5 references indexed in Scilit:
- Thermal inactivation of immobilized enzymes: A kinetic studyJournal of Solid-Phase Biochemistry, 1980
- Proteolytic denaturation and methods of improving the stability of glucose isomerase preparationsBiotechnology & Bioengineering, 1979
- A new model to describe enzyme inactivationBiotechnology & Bioengineering, 1978
- Purification and properties of a novel enzyme, L-α-amino-ϵ-caprolactamase fromCryptococcus laurentiiFEBS Letters, 1978
- The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashionBiochimica et Biophysica Acta (BBA) - Enzymology, 1977