Arch Biochem Biophys. 1988 Jun;263(2):256-63.

Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum.

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Department of Biochemistry and Biophysics, University of California 95616.

Abstract

The hydroxynitrile lyase (EC 4.1.2.--) which catalyzes the dissociation of the cyanohydrins of acetone and 2-butanone has been isolated and purified from young seedlings of flax (Linum usitatissimum L.). The purification procedure involved precipitation with (NH4)2SO4, chromatofocusing, and chromatography on DEAE-cellulose, hydroxylapatite, Sephacryl 200, and Matrex Red A gel columns with a final recovery of 21%. Purification of 136-fold yielded an apparently homogeneous preparation that, in contrast to the lyases isolated from Prunus species, is not a flavoprotein. The subunit molecular weight of 42,000 was estimated by gel electrophoresis in the presence of sodium dodecyl sulfate. The native molecular weight of the enzyme was estimated by gel filtration (HPLC) to be 82,000. The enzyme has a narrow pH optimum around 5.5 and is highly stable at 4 degrees C.

PMID:: 3377504; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

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Research Support, U.S. Gov't, P.H.S.

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Grant Support

GM-05301-29/GM/NIGMS NIH HHS/United States

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Cited by 3 PubMed Central articles

Purification and Characterization of a Novel (R)-Mandelonitrile Lyase from the Fern Phlebodium aureum. [Plant Physiol. 1995]
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