✦ LIBER ✦

Large acceleration of α-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents

✍ Scribed by Dirk-Jan van Unen; Johan F. J. Engbersen; David N. Reinhoudt

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 69 KB
Volume: 59
Category: Article
ISSN: 0006-3592
DOI: 10.1002/(sici)1097-0290(19980905)59:5<553::aid-bit4>3.0.co;2-9

No coin nor oath required. For personal study only.

✦ Synopsis

The effects of 18-crown-6 on the synthesis of peptides catalyzed by ␣-chymotrypsin are reported. Lyophilization of the enzyme in the presence of 50 equivalents of 18-crown-6 results in a 425-fold enhanced activity when the reaction between the 2-chloroethylester of N-acetyl-L-phenylalanine and L-phenylalaninamide is carried out in acetonitrile. Addition of crown ether renders the dipeptide synthesis in nonaqueous solvents catalyzed by ␣-chymotrypsin possible on a preparative scale. The acceleration is observed in different solvents and for various peptide precursors.

📜 SIMILAR VOLUMES

Synthesis of L-tyrosine glyceryl ester c

Synthesis of L-tyrosine glyceryl ester catalyzed by α-chymotrypsin in water-miscible organic solvents: A possible sun-tan accelerator product

✍ Pedro Lozano; Didier Combes; José L. Iborra; Arturo Manjón 📂 Article 📅 1993 🏛 Springer Netherlands 🌐 English ⚖ 383 KB

The synthesis of L-tyrosine glyceryl ester, from glycerol and L-tyrosine methyl ester, was carried out by a transesterification reaction catalyzed by a-chymotrypsin. Values of 60 % (v/v) for glycerol and 200 mM for L-tyrosine methyl ester were optimal for the transesterification reaction. Additional