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Disulfides, as fundamental scaffolds, are widely present in peptides, natural products, and pharmaceutical molecules. However, traditional synthesis of disulfides often involves the utilization of toxic reagents or environmentally unfriendly reaction conditions. In this work, a green and efficient method was developed for synthesizing pyrrole disulfides using β-ketothioamides and ethyl cyanoacetate as substrates, with lipase serving as a catalyst. Under the optimal conditions (β-Ketothioamides (1 mmol), ethyl cyanoacetate (1 mmol), PPL (200 U), and EtOH (5 mL)), lipase leads to the formation of pyrrole disulfides in yields of up to 88% at 40 °C. The related mechanism is also speculated in this paper. This approach not only presents a new application of lipase in enzyme catalytic promiscuity, but also offers a significant advancement in the synthetic pathway for pyrrole disulfides and aligns with the current mainstream research direction of green chemistry, contributing to the further development of environmentally friendly biocatalytic processes. [ABSTRACT FROM AUTHOR]

The development of non-natural enzymatic catalysis is important for multicomponent tandem organic transformations. However, the delicate acting environments of biological enzymes still present some challenges in the synthesis of spirooxindole skeleton via enzymatic catalysis. To address these issues, a lipase-catalyzed method was developed for the synthesis of spirooxindole frameworks. Using easily available isatins, cycloketones, and malononitriles as substrates, mild reaction conditions, and a reasonable reaction time, moderate to good yields (67–92%) and excellent functional group tolerance were accomplished via this protocol. The related mechanism explanation is also speculated in this paper. [ABSTRACT FROM AUTHOR]