Recently, the Food Enzyme Engineering Innovation Team of the Institute of Agricultural Products Processing, Chinese Academy of Agricultural Sciences identified a new type of ferulic acid esterase As FAE from Allobacterium serratia intestinal Substrate binding and catalytic mechanisms provide a scientific basis for in-depth understanding of the dietary fiber metabolism mechanism in the intestinal tract, as well as guidance for precise nutrition and precise medical regulation of intestinal enzymes. The related research results were published in the Journal of Agricultural and Food Chemistry in the form of a cover article with the title "The α-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket".
According to researcher Xin Fengjiao, the human intestinal flora is the core bridge that couples food metabolism and body nutrition regulation, and plays a vital role in human health and disease. Specific flora can release functional ferulic acid from dietary fiber by encoding specific ferulic acid esterase, and then exert functions such as anti-oxidation, anti-infection, anti-tumor, improving cardiovascular disease, and regulating brain cognition. In the previous study, seven ferulic acid esterase genes were up-regulated using in vitro fecal bacteria fermentation. In this study, the expression, purification and enzymatic properties of the ferulic acid esterase derived from S. intestinal bacteria were carried out. The optimal temperature of the enzyme is 40 °C, the optimal pH is 8.5, and it has a high substrate preference for short-chain fatty acid esters. The study further analyzed the three-dimensional structure of the enzyme, revealing that the unique "cap" domain plays an important role in the enzyme's substrate binding and catalysis.
