Bovidae-based gelatin: Extractions method,physicochemical and functional properties,applications, and future trends

Gelatin is one of the most important multifunctional biopolymers and is widely used as an essential ingredient in food, pharmaceutical, and cosmetics. Porcine gelatin is regarded as the leading source of gelatin globally then followed by bovine gelatin. Porcine sources are favored over other sources since they are less expensive. However, porcine gelatin is religiously prohibited to be consumed by Muslims and the Jewish community. It is predicted that the global demand for gelatin will increase significantly in the future. Therefore, a sustainable source of gelatin with efficient production and free of disease transmission must be developed. The highest quality of Bovidae-based gelatin (BG) was acquired through alkaline pretreatment, which displayed excellent physicochemical and rheological properties. The utilization of mammalian- and plant-based enzyme significantly increased the gelatin yield. The emulsifying and foaming properties of BG also showed good stability when incorporated into food and pharmaceutical products. Manipulation of extraction conditions has enabled the development of custom-made gelatin with desired properties. This review highlighted the various modifications of extraction and processing methods to improve the physicochemical and functional properties of Bovidae-based gelatin. An in-depth analysis of the crucial stage of collagen breakdown is also discussed, which involved acid, alkaline, and enzyme pretreatment, respectively. In addition, the unique characteristics and primary qualities of BG including protein content, amphoteric property, gel strength, emulsifying and viscosity properties, and foaming ability were presented. Finally, the applications and prospects of BG as the preferred gelatin source globally were outlined.     

Improved aqueous solubility,bioaccessibility and cellular uptake of quercetin following pH-driven encapsulation in whey protein isolate

The purpose of this study was to increase the water solubility and potential bioavailability of quercetin by encapsulation in whey protein isolate (WPI) based on a green, efficient pH-driven method. According to the results, the water solubility of quercetin increased by 346.9: times after loading into WPI nanoparticles. When the initial quercetin concentration was 0.25 mg mL⁻¹ and WPI was 2% w/v, the encapsulation efficiency reached 94.1%, the Z-average diameter was 36.63 nm, and the zeta potential was −36.4 mV at pH 7.0. The fluorescence spectroscopy assay suggested the molecular complexation of quercetin and WPI at pH 12.0. X-ray diffraction assay indicated the enclosure of amorphous quercetin in WPI. Correspondingly, the bioaccessibility increased from 2.76% to 31.23% and the Caco-2 cell monolayer uptake increased from 0% to 2.12% after nanoencapsulation. This work confirmed that the pH-driven method is an effective approach to prepare WPI–quercetin nanocapsules to improve physical and potentially biological properties of quercetin.     

Polysorbate identity and quantity dictate the extensional flow properties of protein-excipient solutions

While protein medications are promising for treatment of cancer and autoimmune diseases, challenges persist in terms of development and injection stability of high-concentration formulations. Here, the extensional flow properties of protein-excipient solutions are examined via dripping-onto-substrate extensional rheology, using a model ovalbumin (OVA) protein and biocompatible excipients polysorbate 20 (PS20) and 80 (PS80). Despite similar PS structures, differences in extensional flow are observed based on PS identity in two regimes: at moderate total concentrations where surface tension differences drive changes in extensional flow behavior, and at small PS:OVA ratios, which impact the onset of weakly elastic flow behavior. Undesirable elasticity is observed in ultra-concentrated formulations, independent of PS identity; higher PS contents are required to observe these effects than in analogous polymeric excipient solutions. These studies reveal novel extensional flow behaviors in protein-excipient solutions, and provide a straightforward methodology for assessing the extensional flow stability of new protein-excipient formulations.     

Organofluorine Hydrazone Derivatives as Multifunctional Anti-Alzheimer's Agents with CK2 Inhibitory and Antioxidant Features

A set of novel hydrazone derivatives were synthesized and analyzed for their biological activities. The compounds were tested for their inhibitory effect on the phosphorylating activity of the protein kinase CK2, and their antioxidant activity was also determined in three commonly used assays. The hydrazones were evaluated for their radical scavenging against the DPPH, ABTS and peroxyl radicals. Several compounds have been identified as good antioxidants as well as potent protein kinase CK2 inhibitors. Most hydrazones containing a 4-N(CH₃)₂ residue or perfluorinated phenyl rings showed high activity in the radical-scavenging assays and possess nanomolar IC₅₀ values in the kinase assays.     

Enhanced wide-activated residual network for efficient and accurate image deblocking

To save bandwidth and storage space as well as speed up data transmission, people usually perform lossy compression on images. Although the JPEG standard is a simple and effective compression method, it usually introduces various visually unpleasing artifacts, especially the notorious blocking artifacts. In recent years, deep convolutional neural networks (CNNs) have seen remarkable development in compression artifacts reduction. Despite the excellent performance, most deep CNNs suffer from heavy computation due to very deep and wide architectures. In this paper, we propose an enhanced wide-activated residual network (EWARN) for efficient and accurate image deblocking. Specifically, we propose an enhanced wide-activated residual block (EWARB) as basic construction module. Our EWARB gives rise to larger activation width, better use of interdependencies among channels, and more informative and discriminative non-linearity activation features without more parameters than residual block (RB) and wide-activated residual block (WARB). Furthermore, we introduce an overlapping patches extraction and combination (OPEC) strategy into our network in a full convolution way, leading to large receptive field, enforced compatibility among adjacent blocks, and efficient deblocking. Extensive experiments demonstrate that our EWARN outperforms several state-of-the-art methods quantitatively and qualitatively with relatively small model size and less running time, achieving a good trade-off between performance and complexity.     

The dynamic effect of Micro-MHD convection on bubble grown at a horizontal microelectrode

Relatively low efficiency is the biggest obstacle to the popularization of water electrolysis, which is a particularly feasible way to produce super-pure hydrogen. Imposing a magnetic field can increase the hydrogen production efficiency of water electrolysis. However, the enhancement's detailed mechanism still lacks an insightful understanding of the bubbles' micro vicinity. Our recent work aims to understand why the micro-magnetohydrodynamic (MHD) convection hinders single bubbles' detachment on the microelectrode. A water electrolysis experiment by microelectrode is performed under an electrode-normal magnetic field, and dynamic analysis of the single bubble growing on microelectrodes is performed. The variation of bubble diameter with time in the presence or absence of the magnetic field was measured, and the forces acting on the bubble were quantified. The result shows that the micro-MHD convection, induced by Lorentz force, can give rise to a downward hydrodynamic pressure force that will not appear in large-scale MHD convection. This force can be of the same magnitude as the surface tension, so it dramatically hinders bubbles' detachment. Besides, the Kelvin force provides a new potential way for further improving the efficiency of water electrolysis.     

Effects of feed composition,protein denaturation and storage of milk serum protein/lactose powders on lactosylation

During whey powder production, the feed is subjected to several heat treatments which can cause lactosylation of proteins. In this study, lactosylation of whey proteins was evaluated in spray-dried powders before and after storage by varying the native protein fraction as well as the serum protein/lactose ratio in the powders. The lactosylation of native α-lactalbumin and β-lactoglobulin in the powders before storage was not affected to a large extent by the protein denaturation or if the feed had been heat treated in a high or low lactose environment. After storage (relative humidity of 23.5%, 30 °C, 25 days), the kinetic of lactosylation tended to increase with increasing native protein fraction and bulk protein content in the powders. An explanation could be that proteins dissolved in the lactose glassy structure might have a lower reactivity, while proteins present in the protein glassy structure with dissolved lactose may display higher lactosylation reactivity.     

Transglycosylation Activity of Engineered Bifidobacterium Lacto-N-Biosidase Mutants at Donor Subsites for Lacto-N-Tetraose Synthesis

The health benefits of human milk oligosaccharides (HMOs) make them attractive targets as supplements for infant formula milks. However, HMO synthesis is still challenging and only two HMOs have been marketed. Engineering glycoside hydrolases into transglycosylases may provide biocatalytic routes to the synthesis of complex oligosaccharides. Lacto-N-biosidase from Bifidobacterium bifidum (LnbB) is a GH20 enzyme present in the gut microbiota of breast-fed infants that hydrolyzes lacto-N-tetraose (LNT), the core structure of the most abundant type I HMOs. Here we report a mutational study in the donor subsites of the substrate binding cleft with the aim of reducing hydrolytic activity and conferring transglycosylation activity for the synthesis of LNT from p-nitrophenyl β-lacto-N-bioside and lactose. As compared with the wt enzyme with negligible transglycosylation activity, mutants with residual hydrolase activity within 0.05% to 1.6% of the wild-type enzyme result in transglycosylating enzymes with LNT yields in the range of 10–30%. Mutations of Trp394, located in subsite -1 next to the catalytic residues, have a large impact on the transglycosylation/hydrolysis ratio, with W394F being the best mutant as a biocatalyst producing LNT at 32% yield. It is the first reported transglycosylating LnbB enzyme variant, amenable to further engineering for practical enzymatic synthesis of LNT.