(R)-mandelonitrile lyase

This is an abbreviated version!
For detailed information about (R)-mandelonitrile lyase, go to the full flat file.

Word Map on EC




Oxynitrilase, Hydroxynitrile lyase, HNL, (R)-Oxynitrilase, D-Hydroxynitrile lyase, (R)-Mandelonitrile lyase, PhaMDL, (R)-(+)-Mandelonitrile lyase, MDL, D-Oxynitrilase, Lyase, mandelonitrile, D-alpha-hydroxynitrile lyase, PaHNL, PaHNL1, FAD-HNL, hydroynitrile lyase, (R)-hydroxynitrile lyase, mandelonitrile lyase, almond oxynitrilase, R-hydroxynitrile lyase, HNL1, Mdl1, (R)-HNL, PmHNL, PaHNL5, EjHNL, R-selective hydroxynitrile lyase, (R)-PeHNL, R-selective HNL, AtHNL, PaMDL, (R)-HNL5, (R)-selective HNL, HNL2, R-HNL, cupin 2 domain-containing protein, cupin 2 conserved barrel domain protein, AciX9_0562, HNL4, HNL5, NdHNL, DtHNL1, APHNL, ParsHNL


     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
       (R)-mandelonitrile lyase

General Stability

General Stability on EC - (R)-mandelonitrile lyase

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(R)-oxynitrilase immobilized as a cross-linked enzyme aggregate via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde is stable and recyclable
both of immobilized enzymes (Eupergit C and Eupergit C250L) are used repeatedly 20times and the residual activities are about 97% of their initial activities
Prunus pseudoarmeniaca
crosslinked enzyme aggregates result in significant enhancement of the biocatalyst stability under acidic conditions (activity is retained after 168 h at pH 2.4)
the cross-linked enzyme aggregate of Prunus dulcis hydroxynitrile lyase can be reused several times without loss of enantioselectivity
the enzyme is stabilized by addition of sorbitol and saccharose
the enzyme is stable without the substrate but is remarkably unstable upon incubation with benzaldehyde and KCN
the fusion protein of Arabidopsis thaliana hydroxynitrile lyase and a family 2 carbohydrate-binding module derived from the exoglucanase/xylanase Cex of Cellulomonas fimi and a fluorescent reporter module protein shows increases stability at weakly acidic pH values, which is further increased by immobilization
the immobilized enzyme preparations (immobilized onto Eupergit CM and Eupergit C 250 L supports) are successfully reused 10times without loss of activity and enantioselectivity
the presence of glycan can prevent the self-degradation of this enzyme at 10°C