4.1.2.10: (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 4.1.2.10

Reaction

(R)-mandelonitrile
=
cyanide
+
benzaldehyde

Synonyms

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

ECTree

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

Temperature Stability

Temperature Stability on EC 4.1.2.10 - (R)-mandelonitrile lyase

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0
pH 5.0, wild-type, half-life 18 min, surface-modified mutant, half-life 137 min
0 - 20
-
stable
100
-
1 h, complete loss of activity
15 - 40
1 h, no loss of activity
22
-
the relative activity of free enzyme decreases rapidly and depletes at the end of 15 days storage time while the immobilized hydroxynitrile lyases are very active at the same conditions with retained initial activities of 67% and 83% for hydroxynitrile lyase immobilized onto Eupergit CM and hydroxynitrile lyase immobilized onto Eupergit C 250 L, respectively. At the end of 30 days storage time, the corresponding retained activities are 48% and 71% for hydroxynitrile lyase immobilized onto Eupergit CM and hydroxynitrile lyase immobilized onto Eupergit C 250 L
25
-
t1/2: 216 h
25 - 50
Prunus pseudoarmeniaca
-
the half lives of free enzyme at 25 and 50°C are 49.9 and 30.5 h, respectively and these correspondingly are 96.3 and 43.6 h for immobilized enzyme onto Eupergit C, and 138.6 and 50.2 h for immobilized enzyme onto Eupergit C 250 L
30 - 50
1 h, stable, hydroxynitrile lyase from leaves, hydroxynitrile lyase expressed in Pichia pastoris, hydroxynitrile lyase expressed in Escherichia coli, hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris
4
-
the enzyme does not show any significant loss of activity at 4°C, hence it has good potential for industrial application
5 - 20
Prunus pseudoarmeniaca
-
free and immobilized enzyme preparations show optimal carboligation activity at 5°C. As the temperature is increased from 5 to 20°C, the yields decrease, however enantiomeric excess values (99%) unchange
75
1 h, complete loss of activity
90
-
1 h, 85% loss of activity
additional information
the hydroxynitrile lyase from leaves and that expressed in Pichia pastoris show much better thermostability, pH stability, and organic solvent tolerance than the deglycosylated enzyme expressed in Escherichia coli and the deglycosylated mutant N105Q expressed in Pichia pastoris