H₂O₂-driven enzymatic oxyfunctionalization of tertiary C–H bonds

Abstract

Peroxygenase from Agrocybe aegerita catalyses the selective hydroxylation of tertiary C-H bonds, whereby tertiary alcohols, diols, ketols, etc., were obtained in good to high regioselectivity and turnover numbers. This method...

Glutamine‐derived peptides: Current progress and future directions

“…Generally, the enzymatic hydrolysis process can be divided into three stages: extraction and modification of the source protein, hydrolysis by protease, and purification of the target peptide (Fiedler et al, 2014;Zhang, Wen, et al, 2019). In the protease hydrolysis stage, commonly used proteases include trypsin (EC 3.4.21.4),pepsin (EC 3.4.23.15),neutrase (EC 3.4.24.28),alcalase (EC 3.4.21.1),papain (EC 3.4.22.2),thermolysin (EC 3.4.24.27), and flavorzyme (EC 3.4.15.1) (Chen et al, 2021;Liu et al, 2021;Wang et al, 2018;Zhu et al, 2019).…”

“…Commonly used microorganisms for this purpose include Bacillus subtilis, Lactobacillus, and Aspergillus (Zhu et al, 2019). The isolation of target peptides involves various techniques, such as highperformance liquid chromatography, molecular exclusion chromatography, ion exchange chromatography, and ultrafiltration (Zhang, Wen, et al, 2019). Finally, the structure of the target peptides is ultimately confirmed using mass spectrometry (MS) (Zhang, Wen, et al, 2019).…”

Peroxygenase‐Enabled Reductive Kinetic Resolution for the Enantioenrichment of Organoperoxides

“…[10] Peroxygenases share the same transient iron (IV)-oxo porphyrin radical cation (the so-called Compound I) with P450 monooxygenases as reactive species, as such the reactivity of peroxygenases is still underexplored. [11] Today, peroxygenases have been shown to catalyze the challenging CÀ H bond oxyfunctionalization, [12] C=C bond epoxidation, [13] N-oxidation, [14] and S-oxidation [15] and the recently reported dearomatization reactions [13b] (Scheme 1A). The promiscuity of peroxygenases allowed the synthesis of a broad scope of valuable compounds.…”