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Enzymatic Hydrolysis of Hydrophilic Diethyleneglycol and Polyethyleneglycol Esters of Peptides and Glycopeptides by Lipases
Author(s) -
Kunz Horst,
Kowalczyk Danuta,
Braun Peter,
Braum Günther
Publication year - 1994
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199403361
Subject(s) - chemistry , hydrolysis , cleave , lipase , organic chemistry , peptide , glycopeptide , ether , enzyme , enzymatic hydrolysis , biochemistry , antibiotics
New potentials not only in peptide synthesis are opened up by esters of diethyleneglycol monomethyl ether (MEE esters). Surprisingly, these esters can be hydrolyzed by lipases in neutral media. It was previously assumed that lipases cleave only esters that have both hydrophobic and polar regions, like the natural lipase substrates. During the ester hydrolysis, peptide linkages and common protective groups in peptide and carbohydrate chemistry remain intact. Remarkably, lipases in neutral medium can be used not only for MEE esters but also for polyethyleneglycol esters.