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Fig. 1 | Bioresources and Bioprocessing

Fig. 1

From: Enzymatic synthesis of high-titer nicotinamide mononucleotide with a new nicotinamide riboside kinase and an efficient ATP regeneration system

Fig. 1

Characterization of the nicotinamide riboside kinase from Kluyveromyces marxianus. A pH optima of the purified Klm-NRK. The activity was measured in the potassium phosphate buffers (pH 6.0–8.5). Relative activity was expressed as a percentage of maximum activity under the experimental conditions. The maximum activity of Klm-NRK at pH 7.5 was 8.9 U·mg–1 (100%). B Activity–temperature profile. It was determined at various temperatures (30–65 °C) in potassium phosphate buffer (100 mM, pH 7.0). The maximum activity of Klm-NRK at 55 °C was 30.3 U·mg–1 (100%). C Thermal inactivation of Klm-NRK. Purified Klm-NRK (2 mg·mL–1) was preincubated in potassium phosphate buffer (100 mM, pH 7.0) at 30 °C (), 40 °C (▲), 50 °C () or 60 °C (■), then the residual activity was measured. The initial activity of Klm-NRK was 7.9 U·mg–1 at 30 °C (100%)

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