Thermodynamic and kinetic study of stability of the native and chemically modified β-glucosidases from Aspergillus niger
- 28 February 1998
- journal article
- Published by Elsevier in Process Biochemistry
- Vol. 33 (2) , 109-115
- https://doi.org/10.1016/s0032-9592(97)00036-8
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- The stability of extracellular β-glucosidase fromAspergillus niger is significantly enhanced by non-covalently attached polysaccharidesFolia Microbiologica, 1996
- Increased thermal and solvent tolerance of acetylated horseradish peroxidaseEnzyme and Microbial Technology, 1996
- Arthrobacter d-xylose isomerase: chemical modification of carboxy groups and protein engineering of pH optimumBiochemical Journal, 1993
- Chemical Modification of β-Glucosidase from Trichoderma reesei QM 9414The Journal of Biochemistry, 1993
- Irreversible thermoinactivation of glucoamylase from Aspergillus niger and thermostabilization by chemical modification of carboxyl groupsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Chemical modification of a β-glucosidase from Schizophyllum commune: evidence for essential carboxyl groupsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis α-amylaseBiochemical Journal, 1989
- Structure-stability relationships in proteins: new approaches to stabilizing enzymesEnzyme and Microbial Technology, 1984
- Effect of acetylation of Bacillus subtilis α-amylase on the kinetics of heat inactivationBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- DENATURATION AND INACTIVATION OF ENZYME PROTEINSThe Journal of Biochemistry, 1957