Abstract
Quantitative and predictive relationships have been developed for horseradish peroxidase catalysis in both aqueous and organic media. These relationships take into account the physicochemical characteristics of both substrate (e.g., hydrophobicity and electronic characteristics) and solvent (e.g., hydrophobicity and polarity). The results suggest that solvent effects on hydrophobic interactions within proteins are secondary to effects on electrostatic forces.
| Original language | English |
|---|---|
| Pages (from-to) | 277-282 |
| Number of pages | 6 |
| Journal | Biotechnology Techniques |
| Volume | 6 |
| Issue number | 3 |
| DOIs | |
| State | Published - May 1992 |
| Externally published | Yes |