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286 13 Key-Study on NHase/AMase System
References [20] [20] [20] [18] [18] [28] [28] — — References [34] [24] [34] [23] [23]
Inactivation constant, k d , or energy E ∗ a at 4 ◦ C k d = 0.034 h −1 at 4 ◦ C k d = 0.081 h −1 at 10 ◦ Ctill k d = 0.04 h −1 S = 300 mM E ∗ = 91.63 kJ mol −1 E ∗ = 51.57 kJ mol −1 at 30 ◦ C k d = 0.122 h −1 Inactivation constant, k d , or energy E ∗ a E ∗ = 51.60 kJ mol −1 (range k d = 0.0002 h −1 5–50 ◦ C) Negligible till 50 ◦ C at 50 ◦ C k d
(kJ mol −1 ) — 38.37 — — — 25.54 b 37.7 c — 77.06 — a — 53.40 — a (kJ mol −1 ) 49.17 a — 55.61 66.72 — 52.65 53.46
E a E a
of temperature on AMase- and NHase-catalyzed reaction and on inactivation process.
Bioreactor configuration Batch CSMR CSMR Batch CSMR Batch CSMR Batch CSMR Bioreactor configuration CSMR Batch CSMR Batch CSMR
( ◦ C) ( ◦ C) One unit of nitrile hydratase, U NHase , and of amidase, U AMase , have been defined as the amount of enzyme that produces 1 μmol of product (acrylamide or acrylic acid)
T range 10–30 4 4 5–25 5–25 10–55 5–30 5–40 10–30 T range 5–50 10–80 5–50 10–60 10–60 per min, when the proper substrate is incubated per 20 min at 20 ◦ C, 250 rpm, 50 mM Na-phosphate buffer, and appropriate amount of cells.
[Enzyme] (U NHase ml −1 ) 0.29 0.29 0.29 0.059 0.32 1.58 0.275 0.236 0.69–1.52 [Enzyme] (U AMase ml −1 ) 0.33–1.00 0.19 0.33–1.00 0.33 0.33 a Substrate inhibited kinetics already at 200 mM even at lower concentration with Haldane equation prediction.
Nitrile hydratase-catalyzed reaction [Substrate] (mM) 100 100 200 500 a 200 10 10 50 50 [Substrate] (mM) 50 10 50 100 100 d k d -Valuesfor NHaseis57timeshigherthanthatfor AMaseat15 ◦ C.
Effect Amidase-catalyzed reaction b Partial control by mass transport. c Lower diffusional control.
Table 13.2 Substrate Acrylonitrile Acrylonitrile Acrylonitrile Propionitrile Propionitrile Benzonitrile Benzonitrile d 3-Cyanopyridine 3-Cyanopyridine Substrate Acrylamide Benzamide Benzamide Nicotinamide Nicotinamide