The role of molecular interactions on Michaelis constants of α-chymotrypsin catalyzed peptide hydrolyses
Authors:
- Michael KnierbeinMKMichael Knierbein
- Christoph HeldCHChristoph Held
- Gabriele SadowskiGSGabriele Sadowski
- 1 September 2020
- journal article
- research article
- Published by Elsevier in The Journal of Chemical Thermodynamics
- Vol. 148
Abstract
No abstract availableKeywords
Funding Information
- Deutsche Forschungsgemeinschaft
This publication has 50 references indexed in Scilit:
- Solubility of Pharmaceuticals and Their Salts As a Function of pHIndustrial & Engineering Chemistry Research, 2013
- A Broader View: Microbial Enzymes and Their Relevance in Industries, Medicine, and BeyondBioMed Research International, 2013
- Experimental investigation and prediction of oiling out during crystallization processJournal of Crystal Growth, 2008
- Modeling of aqueous amino acid and polypeptide solutions with PC-SAFTChemical Engineering and Processing - Process Intensification, 2008
- Stability and catalytic activity of α‐amylase from barley malt at different pressure–temperature conditionsBiotechnology and Bioengineering, 2006
- Biotechnology—a sustainable alternative for chemical industryBiotechnology Advances, 2005
- Pressure–temperature phase diagrams of biomoleculesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2002
- Perturbed-Chain SAFT: An Equation of State Based on a Perturbation Theory for Chain MoleculesIndustrial & Engineering Chemistry Research, 2001
- Using Molecular Orbital Calculations To Describe the Phase Behavior of Cross-associating MixturesIndustrial & Engineering Chemistry Research, 1998
- Über die Bestimmung von Trypsin und Chymotrypsin mit Aminosäure-p-nitroanilidenHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1965