Anne Ferjancic

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Subtilisin from Bacillus subtilis was modified with polyethylene glycol (PEG), or adsorbed either on celite or porous glass, or directly used as a suspended powder to catalyse peptide synthesis and transesterification reactions in organic solvents. The rather low yield of peptide synthesis probably resulted from the enzyme tendency to catalyse hydrolysis(More)
Polyethylene glycol-modified papain catalyzed the oligomerization of amino acid amides in toluene. The water content of the organic solvent was a critical factor determining the extent of polymerization. Under optimized conditions, lysine and phenylalanine oligomers containing up to 10 residues were obtained. In sharp contrast to what is observed in aqueous(More)
Polyethylene glycol-modified thermolysin was found to efficiently catalyze peptide synthesis in organic solvents. As in aqueous media, the reaction occurred through a rapid equilibrium random bireactant mechanism. However, the substrate specificity of modified thermolysin was actually changed since hydrophilic as well as acidic amino acids were better(More)
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