Light-Driven Enzymatic Decarboxylation of Dicarboxylic Acids

Area of Science:

• Biocatalysis
• Enzymology
• Organic Chemistry

Background:

• Photodecarboxylase from Chlorella variabillis (CvFAP) is a light-activated enzyme.
• CvFAP typically catalyzes the decarboxylation of mono-fatty acids into C1-shortened alkanes.
• Existing engineered CvFAP variants and decoy molecules have substrate limitations, primarily to mono-fatty acids.

Purpose of the Study:

• To investigate and demonstrate the enzymatic conversion of long chain dicarboxylic acids using CvFAP.
• To explore the potential of CvFAP in a chemically challenging reaction: the decarboxylation of dicarboxylic acids to alkanes.
• To evaluate the efficiency, pathway, and stability of CvFAP for this novel application.

Main Methods:

• Utilized engineered Chlorella variabillis photodecarboxylase (CvFAP) for light-driven enzymatic decarboxylation.
• Applied CvFAP to a series of long chain dicarboxylic acids.
• Conducted reaction pathway studies to identify intermediates.
• Assessed the thermostability, storage stability, and recyclability of CvFAP.

Main Results:

• Demonstrated for the first time that CvFAP can convert long chain dicarboxylic acids into C2-shortened alkanes.
• Achieved good yields of alkanes from dicarboxylic acids, even at preparative scales.
• Identified mono-fatty acids as key intermediates in the reaction pathway.
• CvFAP exhibited favorable thermostability, storage stability, and recyclability for dicarboxylic acid decarboxylation.

Conclusions:

• CvFAP successfully catalyzes the decarboxylation of dicarboxylic acids, expanding its substrate scope beyond mono-fatty acids.
• This light-driven enzymatic approach provides an efficient method for synthesizing C2-shortened alkanes from dicarboxylic acids.
• The evaluated stability and recyclability of CvFAP highlight its potential for practical applications in biocatalysis.