A mild and efficient method for the conversion of C-terminal esters of side-chain protected
peptides into an amide function via enzyme-catalysed ammonolysis in organic media with …

Two commercial proteases from Bacillus licheniformis (Alcalase 2.4 L FG and Alcalase 2.5
L, Type DX) were screened for the production of Z-Ala-Phe-NH2 in batch reaction. Alcalase …

The couplings of N-protected amino acid esters with amino acid amides proved to be carried
out in anhydrous acetonitrile in the presence of Bacillus licheniformis protease (subtilisin …

The properties of synthetic peptides, including potency, stability, and bioavailability, are
strongly influenced by modification of the peptide chain termini. Unfortunately, generally …

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The focus of this review is to simplify the role of acyl donor (P1) and the nucleophile (P 1) in
an enzymatic reaction. The specificity of P1 and P 1 is described and arranged in order. In …

The progress of enzymatic peptide synthesis catalyzed by α-chymotrypsin and subtilisin from
Bacillus subtilis strain 72 (subtilisin 72) in low-water systems was studied. The initial reaction …

Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective
peptide production on a large scale. As an alternative to the traditional C→ N strategy, which …

A series of novel glycine esters was evaluated for efficiency in subtilisin A-CLEA-catalysed
peptide synthesis. The reactivity of the easily accessible carboxyamidomethyl (Cam) ester …

Bacillus subtilis protease (Amano protease N) was examined as a catalyst for peptide bond
formation via both the kinetically and thermodynamically controlled approaches. In general …