Skip to main content
Fig. 6 | Biotechnology for Biofuels

Fig. 6

From: Biochemical characterization of three new α-olefin-producing P450 fatty acid decarboxylases with a halophilic property

Fig. 6

Comparison of the decarboxylation (DC) and hydroxylation (HD) activities between OleTSA (WT) and its mutants. The C8–C12 FFAs were used as substrates for wild-type OleTSA (WT) and the mutants including T47F (M1), I177L (M2), V319A (M3), L405I (M4) and T47F-I177L-V319A-L405I (M5). The hydroxylation (HD) activity was calculated by subtracting the percentage of 1-alkene production from the total substrate conversion ratio. Results are shown as mean ± SD of two parallel experiments

Back to article page

Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

Contact us