title: Racemase activity of B. cepacia lipase leads to dual-function asymmetric dynamic kinetic resolution of α-aminonitriles.
authors.affiliation: Department of Chemistry, KTH-Royal Institute of Technology, Teknikringen 30, 10044 Stockholm, Sweden.
authors.forename: Pornrapee
authors.initials: P
authors.lastname: Vongvilai
authors.forename: Mats
authors.initials: M
authors.lastname: Linder
authors.forename: Morakot
authors.initials: M
authors.lastname: Sakulsombat
authors.forename: Maria
authors.initials: M
authors.lastname: Svedendahl Humble
authors.forename: Per
authors.initials: P
authors.lastname: Berglund
authors.forename: Tore
authors.initials: T
authors.lastname: Brinck
authors.forename: Olof
authors.initials: O
authors.lastname: Ramström
mesh_terms: D016956:Burkholderia cepacia / Q000201:enzymology*; D007700:Kinetics; D008049:Lipase / Q000737:chemistry*; D009570:Nitriles / Q000737:chemistry*; D019998:Racemases and Epimerases / Q000737:chemistry*
chemical_list: D009570:Nitriles; D008049:Lipase; D019998:Racemases and Epimerases