Arginine Butyrate

There is a need to explore the influence of particle size of sweet potato flour on physicochem. properties and in vitro starch digestibility of gluten free sweet potato noodles.The aim of this work was to examine the influence of purple-fleshed sweet potato flour (PFSPF) having different particle size distribution (355 μm to 75μ m) on physicochem. properties and in vitro starch digestibility of gluten-free purple sweet potato noodles.Pasting properties and sugar contents were pos. correlated toward the finest particle fraction.The hardness of noodles was pos. and significantly correlated to the finest particle size fraction.Sweet potato flour (SPF) noodles prepared with particle size of 75 μm retained lower hardness 5.74 N.An abrupt increase in yellowness was observed with decreasing particle size that might be attributed to the reduction of protein.The results of FTIR suggested that with the reduction of particle size, protein and carbohydrates decreased that much associated with crystallization and retrogradation of starch.Among all the amino acids, aspartic acid and glutamic acid were observed to be more abundant, i.e. approx. 13.33 and 29.05‰, resp.In this way, PFSPF with particle size 75 μm exhibited significant application potential for producing gluten free noodles due to high resistant starch and lower hardness.It may be concluded that particle sizes of sweet potato flour influenced pasting properties, textural characteristics, sugar contents, protein contents, amino acid contents, carbohydrate contents of prepared noodles.

Antibody repurposing is the process of changing a known antibody so that it binds to a mutated antigen. One of the findings to emerge from the Coronavirus Disease 2019 (COVID-19) pandemic was that it was possible to repurpose neutralizing antibodies for Severe Acute Respiratory Syndrome, a related disease, to work for COVID-19. Thus, antibody repurposing is a possible pathway to prepare for and respond to future pandemics, as well as personalizing cancer therapies. For antibodies to be successfully repurposed, it is necessary to know both how antigen mutations disrupt their binding and how they should be mutated to recover binding, with this work describing an analysis to address the first of these topics. Every possible antigen point mutation in the interface of 246 antibody-protein complexes were analyzed using the Rosetta molecular mechanics force field. The results highlight a number of features of how antigen mutations affect antibody binding, including the effects of mutating critical hotspot residues versus other positions, how many mutations are necessary to be likely to disrupt binding, the prevalence of indirect effects of mutations on binding, and the relative importance of changing attractive versus repulsive energies. These data are expected to be useful in guiding future antibody repurposing experiments.