The University of Tennessee at Martin

Soy protein hydrolyzates have been proven to have ice recrystallization inhibition (IRI) activity, and the presence of minor quantity of polar lipids played an important role as shown in our previous study.The objective of this study was to investigate how polar lipid content, processing condition, and hydrolyzate′s mol. weight (MW) impact the IRI activity of soy hydrolyzates.Soy hydrolyzate complexes were produced in two ways: complexing defatted soy protein isolate (SPI) with lecithin and then hydrolyzing with Alcalase (i.e. P-complexes) and hydrolyzing fully defatted SPI and then complexing the hydrolyzate with lecithin (i.e. H-complexes).The SPI hydrolyzate was also separated by ultrafiltration to create larger (>2 kDa) and smaller peptide (<2 kDa) mixturesA higher IRI activity was observed when complexes were produced with peptides of larger mols.After complexation, strong IRI activity was observed with 1 % lecithin for P-complex, and 5 % lecithin for H-complex.A decrease in intrinsic fluorescence indicates a quenching of tryptophan fluorescence by hydrophobic interactions.Confocal microscopy revealed the lipid and peptides assembled to form fibril structures, and such behaviors maybe crucial for the IRI activity of soy hydrolyzates.This study demonstrates for the first time that complexing plant protein hydrolyzate with polar lipid can lead to IRI activity, and this offers an innovative approach for feasibly making cryoprotective additives for food and biomedical applications.

In this study, tin (Sn) nanoparticles are demonstrated to effectively catalyze the reduction of CO₂ to formate in an alk. medium.Catalytically active Sn-based nanoparticles, supported on carbon black (Sn/C) and highly conductive graphene nanosheets (Sn/GN), present a promising approach to mitigating atm. CO₂ emissions when integrated with capture technologies.Cyclic voltammetry and electrochem. impedance spectroscopy (EIS) were employed to evaluate the prepared catalysts in CO₂-saturated 0.5 M KHCO₃ using a three-electrode rotating disk electrode (RDE) configuration.The results revealed a significantly lower charge-transfer resistance for graphene-supported tin compared to carbon black-supported tin.The CO₂ reduction to formate was further demonstrated in a full electrochem. cell setup resembling the architecture of a low-temperature polymer electrolyte fuel cell (PEFC) operating in an alk. medium with an anion exchange membrane (AEM).Performance tests were conducted with both triple-serpentine and parallel flow field architectures, showing flow rate-dependent behavior.Addnl., an ex-situ RDE technique was utilized to detect and quantify formate production during CO₂ reduction in the full-cell configuration.This work highlights the importance of catalyst support materials and flow field design in optimizing CO₂ electroreduction systems.

Tobacco rattle virus (TRV) is a bipartite single-stranded RNA virus that encodes a replicase, movement protein, and silencing suppressor on TRV1 and a capsid protein on TRV2. Researchers typically insert target silencing sequences into TRV2 and coexpress this with TRV1 to achieve virus-induced gene silencing (VIGS). However, TRV1 does not require TRV2 for mobility or replication within a plant host. With this knowledge, we engineer TRV1 alone as a self-replicating RNA (srRNA) that moves systemically throughout plants for targeted gene repression of up to 89%. As TRV1 is encapsidated in trans by the capsid protein encoded on TRV2, we demonstrate the ability to encapsidate our TRV1 srRNAs for application to target plants by coexpression of the capsid protein off a nonviral expression vector. The subsequent encapsidated TRV1 srRNA can then be harvested and applied to new plants by using a simple spray-on application. Since the RNA for the capsid does not accompany the TRV1 srRNA, our srRNAs are incapable of spreading from plant to plant after the initial application. Minimal to no phenotypic penalties were observed when we used our spray-on srRNA approach. To our knowledge, this is the first demonstration of engineering a sprayable TRV1-based srRNA that is highly capable of repressing target genes. As TRV has a broad host range and our encapsidated srRNAs are unlikely to persist in the environment, we envision that this platform can be used for targeted gene silencing in agriculture.