Fuzzy Time Series Models Using Pliant- and Asymptotically Pliant Arithmetic-Based Inference

Neural Processing Letters - The fuzzy time series modeling techniques proposed in this study are based on a fuzzy inference method in which the fuzzy output is either a so-called pliant or quasi...     

Co-products of beef processing enhance non-haem iron absorption in an in vitro digestion/caco-2 cell model

Beef processing produces high volumes of protein rich, low value, ‘waste’ co-products such as offal. Beef improves uptake of low bioavailable non-haem iron (found in vegetables, fortificants, supplements) and this effect is dubbed the ‘meat-factor’, although the underlying mechanism is not fully understood. Here, we investigate whether bovine co-products (kidney, lung, heart) not previously studied share this enhancing potential. This was determined by coupled in vitro digestion of co-products and subsequent caco-2 cell ferritin formation (an intracellular iron storage protein). In this study we show that bovine co-products significantly increase caco-2 cells’ response to non-haem iron from infant rice cereal. The presence of these co-products, (kidney, lung and heart), increased relative uptake (by 207.13%, 171.21%, 265.28%, respectively), to a greater extent than beef (30.23%). Our findings present a novel function for co-products of beef processing that may have potential as food ingredients to improve non-haem iron bioavailability, thus adding value.     

DPP-4 Cleaves α/β-Peptide Bonds: Substrate Specificity and Half-Lives

The incorporation of β-amino acids into a peptide sequence has gained particular attention as β- and α/β-peptides have shown remarkable proteolytic stability, even after a single homologation at the scissile bond. Several peptidases have been shown to cleave such bonds with high specificity but at a much slower rate compared to α-peptide bonds. In this study, a series of analogs of dipeptidyl peptidase-4 (DPP-4) substrate inhibitors were synthesized in order to investigate whether β-amino acid homologation at the scissile bond could be a valid approach to improving peptide stability towards DPP-4 degradation. DPP-4 cleaved the α/β-peptide bond after the N-terminal penultimate Pro with a broad specificity and retained full activity regardless of the β³-amino acid side chain and peptide length. Significantly improved half-lives were observed for β³Ile-containing peptides. Replacing the penultimate Pro with a conformationally constrained Pro mimetic led to proteolytic resistance. DPP-4 cleavage of α/β-peptide bonds with a broad promiscuity represents a new insight into the stability of peptide analogs containing β-amino acids as such analogs were thought to be stable towards enzymatic degradation.     

Towards Diastereomeric Pure Salts with Antisolvent Methods

Chiral molecules, especially enantiomers and diastereomers of purity > 99 %, present a significant market share within the chemical, pharmaceutical, and flavor industries. Antisolvent precipitations, both batch and semicontinuous operations to serve the current trends in flow chemistry were demonstrated to be environmentally benign and efficient tools in achieving high optical purities. Although salts are known to be insoluble in supercritical CO₂, instabilities of the nascent salts were detected and applied for increasing efficiency. Diastereomeric excess values of the crystalline products exceeded 99 % in maximum of three consecutive steps both by repeated resolution with half molar equivalent of the amine to the acid and by direct recrystallization of the salts.