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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.
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Kunz et al. (1994) studied this question.
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