title: Enzymatic optical resolution via acylation-hydrolysis on a solid support.
abstract: By taking advantage of the reversibility of the thermolysin-catalysed amide synthesis-hydrolysis reaction on a solid support, both L,L and L,D diastereoisomers of dipeptides and L-amino acids are accessible in good yields starting from enantiomeric mixtures of amino acids.
authors.affiliation: School of Chemistry, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh, UK EH9 3JJ.
authors.forename: Rein V
authors.initials: RV
authors.lastname: Ulijn
authors.forename: Nicola
authors.initials: N
authors.lastname: Bisek
authors.forename: Sabine L
authors.initials: SL
authors.lastname: Flitsch
mesh_terms: D000215:Acylation; D000596:Amino Acids / Q000302:isolation & purification*; D004151:Dipeptides / Q000138:chemical synthesis* / Q000302:isolation & purification*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006868:Hydrolysis; D013237:Stereoisomerism; D013820:Thermolysin / Q000378:metabolism
chemical_list: D000596:Amino Acids; D004151:Dipeptides; D004800:Enzymes, Immobilized; D013820:Thermolysin