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Laccase-mediated synthesis of bioactive natural products and their analogues

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RSC CHEMICAL BIOLOGY
卷 3, 期 6, 页码 614-647

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ROYAL SOC CHEMISTRY
DOI: 10.1039/d1cb00259g

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Laccases are multicopper oxidases that have versatile catalytic functions, including oxidative coupling reactions and degradation of biopolymers. In recent years, laccases have been proven to be valuable for synthesizing biologically active compounds with therapeutic value and demonstrating environmental friendliness. This review summarizes studies on laccase-mediated synthesis of biologically active natural products and their analogues, as well as the application of laccases in natural polymer modification.
Laccases are a class of multicopper oxidases that catalyse the one-electron oxidation of four equivalents of a reducing substrate, with the concomitant four-electron reduction of dioxygen to water. Typically, they catalyse many anabolic reactions, in which mostly phenolic metabolites were subjected to oxidative coupling. Alternatively, laccases catalyse the degradation or modification of biopolymers like lignin in catabolic processes. In recent years, laccases have proved valuable and green biocatalysts for synthesising compounds with therapeutic value, including antitumor, antibiotic, antimicrobial, and antioxidant agents. Further up to date applications include oxidative depolymerisation of lignin to gain new biomaterials and bioremediation processes of industrial waste. This review summarizes selected examples from the last decade's literature about the laccase-mediated synthesis of biologically active natural products and their analogues; these will include lignans and neolignans, dimeric stilbenoids, biflavonoids, biaryls and other compounds of potential interest for the pharmaceutical industry. In addition, a short section about applications of laccases in natural polymer modification has been included.

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