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

D.J. van Unen; Johannes F.J. Engbersen; David Reinhoudt

doi:10.1002/(SICI)1097-0290(19980905)59:5<553::AID-BIT4>3.0.CO;2-9

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

Faculty of Science and Technology

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Abstract

The effects of 18-crown-6 on the synthesis of peptides catalyzed by α-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 α-chymotrypsin possible on a preparative scale. The acceleration is observed in different solvents and for various peptide precursors.

Original language	Undefined
Pages (from-to)	553-556
Journal	Biotechnology and bioengineering
Volume	59
Issue number	59
DOIs	https://doi.org/10.1002/(SICI)1097-0290(19980905)59:5<553::AID-BIT4>3.0.CO;2-9
Publication status	Published - 1998

Keywords

METIS-105986
IR-11085
α-chymotrypsin
proteases
organic solvents
enzymatic peptide synthesis
18-crown-6

Access to Document

10.1002/(SICI)1097-0290(19980905)59:5<553::AID-BIT4>3.0.CO;2-9

Cite this

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title = "Large acceleration of a-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents",

abstract = "The effects of 18-crown-6 on the synthesis of peptides catalyzed by α-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 α-chymotrypsin possible on a preparative scale. The acceleration is observed in different solvents and for various peptide precursors.",

keywords = "METIS-105986, IR-11085, α-chymotrypsin, proteases, organic solvents, enzymatic peptide synthesis, 18-crown-6",

author = "\{van Unen\}, D.J. and Engbersen, \{Johannes F.J.\} and David Reinhoudt",

year = "1998",

doi = "10.1002/(SICI)1097-0290(19980905)59:5<553::AID-BIT4>3.0.CO;2-9",

language = "Undefined",

volume = "59",

pages = "553--556",

journal = "Biotechnology and bioengineering",

issn = "0006-3592",

publisher = "Wiley-VCH Verlag",

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TY - JOUR

T1 - Large acceleration of a-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents

AU - van Unen, D.J.

AU - Engbersen, Johannes F.J.

AU - Reinhoudt, David

PY - 1998

Y1 - 1998

N2 - The effects of 18-crown-6 on the synthesis of peptides catalyzed by α-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 α-chymotrypsin possible on a preparative scale. The acceleration is observed in different solvents and for various peptide precursors.

AB - The effects of 18-crown-6 on the synthesis of peptides catalyzed by α-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 α-chymotrypsin possible on a preparative scale. The acceleration is observed in different solvents and for various peptide precursors.

KW - METIS-105986

KW - IR-11085

KW - α-chymotrypsin

KW - proteases

KW - organic solvents

KW - enzymatic peptide synthesis

KW - 18-crown-6

U2 - 10.1002/(SICI)1097-0290(19980905)59:5<553::AID-BIT4>3.0.CO;2-9

DO - 10.1002/(SICI)1097-0290(19980905)59:5<553::AID-BIT4>3.0.CO;2-9

M3 - Article

SN - 0006-3592

VL - 59

SP - 553

EP - 556

JO - Biotechnology and bioengineering

JF - Biotechnology and bioengineering

IS - 59

ER -