Skip to main content
Fig. 3 | Biotechnology for Biofuels and Bioproducts

Fig. 3

From: MpADC, an l-aspartate-α-decarboxylase, from Myzus persicae, that enables production of β-alanine with high yield by whole-cell enzymatic catalysis

Fig. 3

Biochemical characterization of MpADC. a Activity of MpADC at different reaction temperatures. The reaction was performed in buffer [0.2 M phosphate buffer (pH 7.5)] at different temperatures for 5 min. b Activity of MpADC at different reaction pHs. The reaction was performed in different buffers at 37 °C for 5 min. c Stability of MpADC at different temperatures. ADC activity was measured after treatment at the corresponding temperature for 12 h. d Stability of MpADC at different reaction pHs. The stability was analyzed by monitoring the residual activity after the enzyme was incubated in various pH conditions for 12 h at 30 °C. The maximum activity is defined as 100%. e Activity of MpADC at different concentration of PLP. The initial activity without PLP was set to 100%; f Effects of metal ions and chelating agents on its activity. The initial MpADC activity without metal ions and chelating agents was set to 100%. (All assays were performed in triplicate, and the standard deviations of the biological replicates were represented by error bars.)

Back to article page

Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

Contact us