Passive Wireless Porous Biopolymer Sensors for At-Home Monitoring of Oil and Fatty Acid Nutrition.

Dietary oils─rich in omega-3, -6, and -9 fatty acids─exhibit critical impacts on health parameters such as cardiovascular function, bodily inflammation, and neurological development. There has emerged a need for low-cost, accessible method to assess dietary oil consumption and its health implications. Existing methods typically require specialized, complex equipment and extensive sample preparation steps, rendering them unsuitable for home use. Addressing this gap, herein, we study passive wireless, biocompatible biosensors that can be used to monitor dietary oils directly from foods either prepared or cooked in oil. This design uses broad-coupled split ring resonators interceded with porous silk fibroin biopolymer (requiring only food-safe materials, such as aluminum foil and biopolymer). These porous biopolymer films absorb oils at rates proportional to their viscosity/fatty acid composition and whose response can be measured wirelessly without any microelectronic components touching food. The engineering and mechanism of such sensors are explored, alongside their ability to measure the oil presence and fatty acid content directly from foods. Its simplicity, portability, and inexpensiveness are ideal for emerging needs in precision nutrition─such sensors may empower individuals to make informed dietary decisions based on direct-from-food measurements.

Expression Patterns and Functional Analysis of Three SmTAT Genes Encoding Tyrosine Aminotransferases in Salvia miltiorrhiza.

Tyrosine aminotransferase (TAT, E.C. 2.6.1.5) is a pyridoxal phosphate-dependent aminotransferase that is widely found in living organisms. It catalyzes the transfer of the amino group on tyrosine to α-ketoglutarate to produce 4-hydroxyphenylpyruvic acid (4-HPP) and is the first enzyme for tyrosine degradation. Three SmTATs have been identified in the genome of Salvia miltiorrhiza (a model medicinal plant), but their information is very limited. Here, the expression profiles of the three SmTAT genes (SmTAT1, SmTAT2, and SmTAT3) were studied. All three genes expressed in different tissues and responded to methyl jasmonate stimuli. SmTAT proteins are localized in the cytoplasm. The recombinant SmTATs were subjected to in vitro biochemical properties. All three recombinant enzymes had TAT activities and SmTAT1 had the highest catalytic activity for tyrosine, followed by SmTAT3. Also, SmTAT1 preferred the direction of tyrosine deamination to 4-HPP, while SmTAT2 preferred transamination of 4-HPP to tyrosine. In parallel, transient overexpression of SmTATs in tobacco leaves revealed that all three SmTAT proteins catalyzed tyrosine to 4-HPP in vivo, with SmTAT1 exhibiting the highest enzymatic activity. Overall, our results lay a foundation for the production of tyrosine-derived secondary metabolites via metabolic engineering or synthetic biology in the future.