Protein Variants | Comment | Organism |
---|---|---|
additional information | the enzyme subtilisin A is immobilized by simple hydrophobic adsorption onto various surface-grafted macroporous silica gels resulting in easy-to-prepare and stable biocatalysts enabling the efficient kinetic resolution (KR) and dynamic kinetic resolution (DKR) of racemic N-tert-butyloxycarbonylphenylalanine ethyl thioester with benzylamine | Bacillus licheniformis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus licheniformis | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Bacillus licheniformis | - |
Storage Stability | Organism |
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effect of one year storage on activity and selectivity of 23 different Alcalase preparations in the kinetic resolution of racemic N-tert-butyloxycarbonylphenylalanine ethyl thioester with benzylamine, overview | Bacillus licheniformis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 rac-N-tert-butoxycarbonylphenylalanine ethyl thioester + 1-phenylmethanamine + tert-butanol | continuous-flow cascade reactor system for subtilisin A-catalyzed dynamic kinetic resolution (DKR). The continuous-mode DKR of the racemic thioester in a serial cascade system of six biocatalyst-filled columns at 50°C for KR and five grafted silica gel-filled columns at 150°C for racemization results in the formation of the (S)-benzylamide in 79% conversion, 8.17 g/l/h volumetric productivity and 98% enantiomeric excess. Method evaluation, overview | Bacillus licheniformis | N-benzyl-Nalpha-(tert-butoxycarbonyl)-L-phenylalaninamide + (R)-N-tert-butoxycarbonylphenylalanine ethyl thioester + ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Alcalase | - |
Bacillus licheniformis |
subtilisin A | - |
Bacillus licheniformis |