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. 2018 Jun 29;19(7):1911. doi: 10.3390/ijms19071911

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© 2018 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Assays of LaOMT1 enzyme activity in vitro for different substrates. (A) HPLC analysis of cafferic acid (1) incubated with the recombinant LaOMT1 protein. Two new peaks representing ferulic acid (2) and isoferulic acid (3) were verified, according to each identical retention time. (B) A dose-dependent activity of LaOMT1 when 1 mM caffeic acid incubated with the recombinant LaOMT1 enzyme in different concentrations. Each dataset represents the mean ± standard deviation (SD) from triplicate measurements. (C) HPLC analysis of 3,4-dihydroxybenzaldehyde incubated with the recombinant LaOMT1 protein, where two new peaks with the same retention time as isovanillin (red arrow) and vanillin (blue arrow) were found. (D) HPLC analysis of norbelladine incubated with the recombinant LaOMT1 protein. The two new products were indicated with blue arrow and red arrow, respectively.