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EC Number	Storage Stability
4.1.2.10	10°C, 12 h, the stabilities of hydroxynitrile lyase from leaves and hydroxynitrile lyase expressed in Pichia pastoris are comparable, with remaining enzyme activities of 60-94%. The activities of hydroxynitrile lyase mutant N105Q expressed in Pichia pastor and hydroxynitrile lyase expressed in Escherichia coli vary between 70% and 0% in all biphasic systems apart from those with DEE and DIPE. The nonglycosylated hydroxynitrile lyase expressed in Escherichia coli and hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris both lose 50% of their activity in aqueous buffer with shaking at 1500 rpm at 10°C
4.1.2.10	4°C, 20 mM potassium phosphate buffer, pH 6.0, stable for 30 d

EC Number

Storage Stability

4.1.2.10

10°C, 12 h, the stabilities of hydroxynitrile lyase from leaves and hydroxynitrile lyase expressed in Pichia pastoris are comparable, with remaining enzyme activities of 60-94%. The activities of hydroxynitrile lyase mutant N105Q expressed in Pichia pastor and hydroxynitrile lyase expressed in Escherichia coli vary between 70% and 0% in all biphasic systems apart from those with DEE and DIPE. The nonglycosylated hydroxynitrile lyase expressed in Escherichia coli and hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris both lose 50% of their activity in aqueous buffer with shaking at 1500 rpm at 10°C

4.1.2.10

4°C, 20 mM potassium phosphate buffer, pH 6.0, stable for 30 d

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Release 2023.1 (January 2023)