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. 2019 Jan 14;6:211. doi: 10.3389/fbioe.2018.00211

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Copyright © 2019 Schmieg, Döbber, Kirschhöfer, Pohl and Franzreb.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Michaelis–Menten kinetics of the investigated biocatalytic reactions with freely dissolved enzymes. Kinetic parameters v_max and K_m were calculated by fitting the data to the Michaelis–Menten function, which is shown including 95% confidence bounds. In the whole figure, each data point represents one sample. (A) β-Gal kinetics for the cleavage of ONPG at pH 4.6 (n = 3 separate runs). (B) BFD kinetics for the carboligation of benzaldehyde and a respective 2.5-fold excess of acetaldehyde (n = 2 separate runs). Estimation of the confidence bounds was omitted because of limited data for substrate excess. (C) ADH kinetics for the reduction of acetophenone. (D) ADH kinetics for the reduction of (S)-HPP, which was previously synthesized by BFD. For ADH kinetics, data points were generated in one batch due to shortage of the enzyme.