β-Lactoglobulin (BLG) and α-lactalbumin (ALA) are the primary allergens in whey protein. However, gastrointestinal digestion can induce structural rearrangements of their IgE-binding epitopes, complicating the precise evaluation of allergenicity. This study developed a novel approach to identify digestion-resistant antigenic epitopes of BLG and ALA through simulated in vitro infant digestion.
View Article and Find Full Text PDFOleanolic acid (OA) is a terpenoid compound with anti-inflammatory and antioxidant effects, while its low stability and bioavailability limit the wide application. In this study, OA was incorporated into liposomes (OA-LIP), chitosan (CHI) coated liposomes (CHI-OA-LIP), and CHI-polygalacturonic acid (PGA)-double-layered (PGA-CHI-OA-LIP). The in vitro semi-dynamic digestion, cell absorption and pre-protective function for the liver-injured mouse of liposomes were evaluated.
View Article and Find Full Text PDFAlgal oil is rich in docosahexaenoic acid, which is beneficial for infant development, but its susceptibility to oxidation necessitates microencapsulation. This study investigated the effects of incorporating varying ratios of octenyl succinic anhydride-modified starch (OSA-MS) into a base wall system comprising extensively hydrolyzed whey protein (eWPH) and maltodextrin (MD) to produce algal oil microcapsules with reduced allergenicity and high nutritional value, replacing whey protein isolate (WPI). The residual antigenicity of α-lactalbumin and β-lactoglobulin in eWPH was 3.
View Article and Find Full Text PDFWater-oil-water (W/O/W) double emulsions have been widely studied and applied in probiotic encapsulation. However, challenges remain in enhancing emulsion stability, protecting encapsulated probiotics from adverse environmental conditions, and improving their viability. This study aimed to optimize the functional components of each phase of the W/O/W emulsion to address these issues.
View Article and Find Full Text PDFBackground: Sturgeon cartilage type II collagen peptides (SHCPs) can self-assemble and be used to prepare collagen peptide assemblies. Self-assembled peptides have great potential for applications in the food industry. In the present study, self-assembled peptides were prepared from sturgeon cartilage and then characterized.
View Article and Find Full Text PDFCrit Rev Food Sci Nutr
October 2024
Type II collagen is a homologous super-helical structure consisting of three identical α1(II) chains. It is a major component of animal cartilage, and is widely used in the food industry. Type II collagen can be extracted by acids, salts, enzymes, and auxiliary methods and can be further hydrolyzed chemically and enzymatically to produce collagen peptides.
View Article and Find Full Text PDFBackground: Porcine nasal cartilage type II collagen-derived peptides (PNCPs) may be complexed with calcium to provide a highly bioavailable, low-cost, and effective calcium food supplement. However, the calcium-binding characteristics of PNCPs have not yet been investigated. In the present study, calcium-binding peptides were derived from porcine nasal cartilage type II collagen and the resulting PNCPs-Ca complex was characterized.
View Article and Find Full Text PDFJ Agric Food Chem
August 2021
There are still many challenges in understanding the absorption and transport mechanism of liposomes in the gastrointestinal tract of infants, especially for liposome-coentrapped two or more substances. In this study, novel docosahexaenoic acid (DHA)-anthocyanidin-codelivery liposomes (DA-LPs) were fabricated and characterized, and their digestive and absorptive behaviors were evaluated using the infant digestive method combined with the Caco-2 cell model. The liposomal bilayer structure remained intact with the particles aggregated in simulated infant gastric fluid, while their phospholipid membrane underwent enzymatic lipolysis under simulated intestinal conditions.
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