title: In situ evaluation of lipase performances through dynamic asymmetric cyanohydrin resolution.
abstract: A dynamic resolution process based on multiple reversible cyanohydrin formation coupled to lipase-mediated transesterification is demonstrated. The resulting process resulted in the efficient evaluation of complex lipase performances in asymmetric cyanohydrin acylate synthesis. Dynamic systems were generated and resolved in situ, and the effects of the reaction conditions could be directly monitored for the overall system. By this concept, the enzyme activity, chemo- and stereoselectivity for all involved substrates could be simultaneously evaluated.
authors.affiliation: Department of Chemistry, KTH-Royal Institute of Technology, Teknikringen 30, S-10044, Stockholm, Sweden.
authors.forename: Morakot
authors.initials: M
authors.lastname: Sakulsombat
authors.forename: Pornrapee
authors.initials: P
authors.lastname: Vongvilai
authors.forename: Olof
authors.initials: O
authors.lastname: Ramström
mesh_terms: D055162:Biocatalysis; D016956:Burkholderia cepacia / Q000201:enzymology*; D008049:Lipase / Q000378:metabolism*; D015394:Molecular Structure; D009570:Nitriles / Q000737:chemistry* / Q000378:metabolism; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D009570:Nitriles; C430593:cyanohydrin; D008049:Lipase