Bacillus licheniformis protease-catalyzed peptide synthesisvia the kinetically controlled approach using the carbamoylmethyl ester as an acyl donor in anhydrous acetonitrile

Kinetics of Alcalase-catalyzed dipeptide synthesis in near-anhydrous organic media

“…Alcalase can for instance catalyze the coupling of an ␣-amino amide and a chemically synthesized activated N-protected amino acid, e.g. an N-protected amino acid carbamoylmethyl (Cam) ester [6][7][8][9][10][11][12].…”

Effect of enzyme dehydration on alcalase‐catalyzed dipeptide synthesis in near‐anhydrous organic media

“…Alcalase can be used in the chemo‐enzymatic synthesis of peptides, which are important for health care, nutrition, and cosmetics . Alcalase can catalyze the coupling of a α‐amino amide and a chemically synthesized activated N‐protected amino acid, such as an N‐protected amino acid carbamoylmethyl (Cam) ester …”

“…[1][2][3][4][5] Alcalase can catalyze the coupling of a aamino amide and a chemically synthesized activated N-protected amino acid, such as an N-protected amino acid carbamoylmethyl (Cam) ester. [6][7][8][9][10][11][12] In this study the effect of enzyme dehydration by molecular sieves on the coupling of phenylalanine amide (H-Phe-NH 2 ) and the carbamoylmethyl ester of phenylalanine (of which the amino group was protected using benzyloxycarbonyl, Z-Phe-OCam) in near-anhydrous tetrahydrofuran (THF) was investigated. This coupling was catalyzed by Alcalase covalently immobilized onto macroporous acrylic beads (in this paper abbreviated as Cov); these immobilized enzymes were hydrated prior to use.…”