Overall, this work demonstrates that rational mutagenesis can alter polyesterase activity against structurally distinct biodegradable polyesters, providing potential mechanistic insights to guide the development of specialized biocatalysts for targeted polyester degradation.
Konstantinos Makryniotis, Panagiota Karampa, M. Dimarogona et al.· Enzyme and Microbial Technol...· 0 citations
Lignocellulosic biomass is a renewable and abundant resource for producing high-value chemicals as sustainable alternatives to petroleum-derived products. Among these, 5-hydroxymethylfurfural (HMF) and furfural (FA), generated through catalytic dehydration of biomass-derived sugars, serve as pivotal intermediates for enzymatic synthesis of valuable platform chemicals like 2,5-furandicarboxylic acid (FDCA). In recent studies, glyoxal oxidases (GlyOx, EC 1.2.3.15) have emerged as promising candidates for the biotransformation of furan derivatives. This study focused on the recombinant production and characterization of a GlyOx from the medicinal basidiomycete Ganoderma lucidum capable of oxidizing HMF and FA with 51.5% and 23.0% conversion, respectively, after 48 h. Furthermore, the enzyme oxidized HMF derived from hexose-rich wheat straw hydrolysates, leading to 32.4% conversion after 72 h, as well as FA derived from beechwood hemicellulosic hydrolysates, leading to furoic acid with 17.0% conversion after 48 h, marking the first time such enzymatic activity has been demonstrated on furans originating from genuine lignocellulosic biomass sugar streams.
Maria-Konstantina Karonidi, Κoar Chorozian, A. Marianou et al.· Journal of Agricultural and...· 1 citation
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