Identification of Cinnamate Reductase / fldZ gene and its role in the degradation of Cinnamic Acid

         Cinnamon is a spice with a long standing history. Cinnamaldehyde and cinnamic acid (CA) are two of the active ingredients in cinnamon. Both display an array of biological activities such as anti-inflammatory, anti-cancer, antidiabetic, and antibacterial properties. Specifically, the antibacterial effects that they impose on many microbes can lead to both cinnamaldehyde and cinnamic acid becoming potential antibiotic agents for many human pathogenic microbes like Streptococcus mutans. A study by Huang, 2019, shows that cinnamaldehyde at sub-MIC stages depleted the bacterial activity and aggregation of S. mutans biofilm, and halted the development and resistance of acid (He, Huang, 2019). The focus of this study, Cinnamate (Cinnamic Acid), and its metabolic pathway has been identified in Stenotrophomonas sp. TRMK2 (Monisha, 2018) and Clostridium sporogenes (Dickert 2000). By conducting 16s rRNA phylogenetic analysis, the identification of organisms related to Stenotrophomonas sp. TRMK2 were revealed and used to gain more insight into the key protein, Cinnamate Reductase. The Cinnamate Reductase enzyme plays a crucial role in the degradation of Cinnamic Acid. The fldZ gene is responsible for encoding Cinnamate Reductase and will be used as an identification template for other bacteria able to metabolize cinnamic acid. With the successful identification of homologous genes to fldZ using primers synthesized from the template gene, detection of related genes in other species could reveal antimicrobial capabilities for cinnamon and its active components.