Reducing enzyme conformational flexibility by multi-point covalent immobilisation |
| |
Authors: | R Fernandez-Lafuente A N P Wood D A Cowan |
| |
Institution: | (1) Department of Biochemistry and Molecular Biology, University College, London, UK |
| |
Abstract: | Summary A thermostable esterase was immobilised to glyoxyl-agarose under conditions designed to generate limited-linkage and multi-point covalent derivatives. The multi-point derivative was 830-fold more thermostable than the limited-linkage derivative and retained 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. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|