✦ LIBER ✦
Novel Biocatalysts by Chemical Modification of Known Enzymes: Cross-Linked Microcrystals of the Semisynthetic Peroxidase Seleno-Subtilisin
✍ Scribed by Dietmar Häring; Peter Schreier
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 96 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0044-8249
No coin nor oath required. For personal study only.
✦ Synopsis
The linkage of lysine residues on the surfaces of subtilisin crystals (NH -Enz; see Scheme) with glutardialdehyde affords an immobilized biocatalyst of high stability and purity. The replacement of the serine OH group in the active site (Enz-OH) by SeO H leads to new activity as a peroxidase. Thus for the first time, chemical enzyme engineering has resulted in a biocatalyst with a modified peptide framework as well as a new catalytically active site. This methodology combines reasonable substrate selectivity of a semisynthetic enzyme with the exceptional stability of cross-linked enzyme crystals.