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Improved purification of an (R)‐oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range
Author(s) -
Albrecht J.,
Jansen I.,
Kula MR
Publication year - 1993
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1993.tb00239.x
Subject(s) - linum , chemistry , substrate (aquarium) , yield (engineering) , chromatography , gel permeation chromatography , solvent , ether , ion exchange , cyanohydrin , organic chemistry , catalysis , botany , ion , oceanography , materials science , metallurgy , biology , geology , polymer
The purification of (R)‐oxynitrilase (EC 4.1.2.10) from Linum usitatissimum (flax) has been improved considerably. The enzyme is obtained from seedlings in 60% yield by fractional salt precipitation followed by ion‐exchange and hydrophobic‐interaction chromatography. Final gel‐permeation chromatography yields a protein with a specific activity of 53 units/mg at pH 4.1. The N‐terminal sequence is reported and microheterogeneity demonstrated. The substrate range was investigated using (R)‐oxynitrilase immobilized on Eupergit and t‐butyl methyl ether as solvent. The addition of HCN to various aliphatic ketones and aldehydes is catalysed by the enzyme, while aromatic ketones are not converted. (R)‐Butan‐2‐one cyanohydrin was synthesized on a preparative scale and the product characterized.