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Microorganisms in grape skins play vital roles in grapevine health, productivity, wine quality and organoleptic properties. To investigate microbial diversity of muscadine grape skins, 16S and ITS sequences of 30 samples from six muscadine (Muscadinia rotundifolia Michx.) cultivars grown in Guangxi, China, were sequenced using Illumina Novaseq platform. A total of 7,317 bacterial operational taxonomic units (OTUs) and 1,611 fungal OTUs were obtained, and clustered into 38 bacterial and 7 known fungal phyla. The dominant bacterial phyla were Proteobacteria, Firmicutes, Bacteroidetes, Planctomycetes, Actinobacteria, Verrucomicrobia, Acidobacteria, and Patescibacteria, and the dominant genera were Lelliottia, Prevotella_9, Escherichia-Shigella, Lactobacillus, Pseudomonas, Akkermansia, Faecalibacterium, Rahnella, and Acinetobacter. For fungi, the dominant phyla were Ascomycota, Basidiomycota, and Mortierellomycota, and the dominant genera were Acaromyces, Uwebraunia, Penicillium, Zygosporium, Ilyonectria, Aspergillus, Neodevriesia, Strelitziana, Mortierella, and Fusarium. Alpha diversity analysis and Kruskal-Wallis H test demonstrated that microbial diversity and composition were affected by the cultivar. The Pearson correlation analysis of species revealed complex interactions among microbes. PICRUSt2 predicted that the metabolism of carbohydrates, cofactors, vitamins, amino acids, terpenoids, polyketides, lipids and biosynthesis of other secondary metabolites were abundant. These results contribute to understanding the uniqueness of muscadine grapes and the links among microorganisms in grape skins.Recently an approach has been developed to structure plant-based lipids with the intention to mimic animal fat tissue in processed meat products or analogues. This study investigated the comminution behavior in a bowl chopper of such structured lipids with varying mechanical properties. For products like salami-type sausages these systems need to withstand comminution to yield particles for inclusion in product matrices. Therefore, samples were prepared from protein suspensions with 6%, 8%, 10%, and 12% soy protein isolate (SPI) and 70% (w/w) total fat with varying solid fat contents (0-30%, w/w). The hardness of samples prepared with 6% and 8% SPI varied between 4.5 and 35.9 N. When comminuted in a bowl chopper, these structures had insufficient mechanical strengths to facilitate the formation of small particles and yielded a coarse paste. Higher concentrations of protein increased hardness (15.9-76.2 N and 15.6-96.1 N, for 10% and 12% SPI, respectively). These samples retained their structural integrity upon comminution yielding individual intact particles. The size of these particles increased with sample firmness, i.e. with increasing amount of protein. The shape of the particles was more elongated the higher the solid fat content as indicated by a higher aspect ratio. Taken together, results show that structural characteristics of the gelled emulsions can be tuned to yield desired fat particles after comminution.Heat treatment is an effective method for ensuring food safety and quality by controlling microbial contamination. However, food poisoning outbreaks have continuously occurred in heat-treated products due to improper thermal treatment and/or post-contamination of foodborne pathogens. This study proposes a novel strategy combining thermostable bacteriophages with thermal processing of food production plants to control foodborne pathogens and even bacterial contamination. Typically, bacteriophages' susceptibility to heat is a major challenge to their application with thermal processing, we isolated thermostable bacteriophages by a modified isolation method of applying heat to samples and characterized the thermostable bacteriophages. Etomoxir ic50 Furthermore, we optimized the bacteriophage cocktail components to expand the controllable host range and reduce the risk of bacteriophage resistance development. Finally, we verified this antibacterial strategy by combining heat treatment with thermostable bacteriophages in model systems, including milk and chicken breast. After the phage cocktail and heat treatment, we artificially contaminated the food products to mimic the post-contamination event. Surprisingly, the remaining bacteriophages that withstood heat treatment significantly reduced the number of post-contaminated Salmonella. Altogether, thermostable phages could be applied as complementary tools to control post-contamination after thermal processing of food products.This study aimed to explore nutritional compositions and proteomics of soft-shelled turtle (SST) egg, as well as identify potential antidiabetic oligopeptides with α-glucosidase inhibitory property. Results revealed that SST egg is a promising source of highly nutritious proteins and minerals (54.64% and 5.81% of dry matter, respectively). Further proteomic analysis showed SST egg proteins contained at least 9 protein families, such as transferrin/iron binding protein and immunoregulation-related protein. Hydrolysis by different enzymes, especially papain, remarkably increased α-glucosidase inhibitory activity and scavenging activity for ABTS, DPPH, hydroxyl and oxygen radicals of SST egg proteins. Peptides from papain hydrolysate were fractionated using ultrafiltration followed by reverse phase chromatography, and 16 peptides were identified in the most active fraction by LC-QTOF-MS/MS. Molecular docking revealed that 14 of these peptides could easily dock into the substrate-binding pocket and/or inhibitor binding sites of α-glucosidase with the docking score below -150 kcal/mol, indicating their potential α-glucosidase inhibitory properties. The five most abundant oligopeptides with potent interaction with α-glucosidase were further synthesized, and oligopeptides HNKPEVEVR, ARDASVLK and SGTLLHK strongly inhibited the activity of α-glucosidase (IC50 of 56, 195 and 289 µmol/L, respectively). Therefore, oligopeptides from enzymatic hydrolysate of SST egg protein exhibit potential antidiabetic activity, making it a promising functional food ingredient.The gastrointestinal hydrolysis of food proteins has been portrayed in scientific literature to predominantly depend on the activity and specificity of proteolytic enzymes. Human bile has not been considered to facilitate proteolysis in the small intestine, but rather to assist in intestinal lipolysis. However, human bile can potentially influence proteins that are largely resistant to gastric digestion, and which are mainly hydrolysed after they have been transferred to the small intestine. We used purified and food-grade bovine milk β-lactoglobulin (βLg) to assess the impact of bile salts (BS) on the in vitro gastrointestinal digestion of this protein. Quantitative analysis showed that the proteolysis rate increased significantly with increasing BS concentration. The effect was consistent regardless of whether individual BS or real human bile samples, varying in BS concentrations, were used. The total BS content of bile was more important than its BS composition in facilitating the proteolysis of βlg. We also show that the impact of human bile observed during the digestion of purified βLg and βLg-rich whey protein isolate can be closely replicated by the use of individual BS mixed with phosphatidylcholine.
Homepage: https://www.selleckchem.com/products/etomoxir-na-salt.html
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