Reducing enzyme conformational flexibility by multi-point covalent immobilisation
✍ Scribed by R. Fernandez-Lafuente; A. N. P. Wood; D. A. Cowan
- Book ID
- 104644994
- Publisher
- Springer-Verlag
- Year
- 1995
- Tongue
- English
- Weight
- 337 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0951-208X
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✦ Synopsis
A thermostable esterase was generate "limited-linkage" immobilised to glyoxyl-agarose under conditions designed to and "multi-uoint" covalent derivatives. The multi-noint derivative was 830-fold more thermostab& than the limited-linkage derivative and &.&ed more activity in the presence of sodium chloride and organic solvents. Medium chain (C8) aliphatic p-nitrophenyl ester substrates, which inactivate the soluble enzyme, were shown to be more readily hydrolysed. Together these data support the contention that multi-point covalent immobilisation results in a more rigid, less conformationally flexible protein structure.