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The use of selected engineered galactose oxidase (GOase) variants for the oxidation of amino alcohols to aldehydes under mild conditions in aqueous systems is reported. GOase variant F-2 catalyses the regioselective oxidation of N-carbobenzyloxy (Cbz)-protected 3-amino-1,2-propanediol to the corresponding -hydroxyaldehyde which was then used in an aldolase reaction. Another variant, M3-5, was found to exhibit activity towards free and N-Cbz-protected aliphatic and aromatic amino alcohols allowing the synthesis of lactams such as 3,4-dihydronaphthalen-1(2H)-one, 2-pyrrolidone and valerolactam in one-pot tandem reactions with xanthine dehydrogenase (XDH) or aldehyde oxidase (PaoABC).
Despite the rapid development of Pickering interfacial catalysis (PIC) at liquid-liquid interfaces with chemocatalysts, the use of unstable biocatalysts at emulsion interfaces remains a technical challenge. Herein, we present a Pickering interfacial biocatalysis (PIB) platform based on robust and recyclable enzyme-polymer conjugates that act as both catalytic sites and stabilizers at the interface of Pickering emulsions. The conjugates were prepared by growing poly(N-isopropylacrylamide) on a fragile enzyme, benzaldehyde lyase, under physiological conditions. The mild in situ conjugation process preserved the enzyme structure, and the conjugates were used to emulsify a water-organic two-phase system into a stable Pickering emulsion, leading to a significantly larger interfacial area and a 270-fold improvement in catalytic performance as compared to the unemulsified two-phase system. The PIB system could be reused multiple times. Conjugates of other enzymes were also fabricated and applied for cascade reactions.