Decarboxylation, a crucial process in the production of CBD-rich hemp products, involves the removal of a carboxyl group from a molecule, resulting in the activation of cannabinoids like CBD. Studies with secretory cavity contents and air-dried inflorescence extracts of the CBD-rich hemp strain, Cannabis sativa cv., have shed light on the intricate biochemical mechanisms behind this phenomenon.
Introduction. Benzoylformate decarboxylase (BFDC) is a thiamin diphosphate (ThDP)-dependent enzyme that catalyzes the nonoxidative decarboxylation of various substrates. In the context of CBD-rich hemp plants, decarboxylation plays a vital role in converting inactive cannabinoid precursors into their active forms, such as CBD. This process is essential for unlocking the therapeutic properties of CBD and enhancing its bioavailability.
Through biochemical and structural characterization, we demonstrate that, like its mitochondrial homolog FAHD1, YisK can catalyze the decarboxylation of specific substrates, contributing to the overall metabolic profile of CBD-rich hemp plants. Understanding the enzymatic pathways involved in decarboxylation is crucial for optimizing the production of CBD-infused products with consistent potency and efficacy.