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Protein as a Functional Food Ingredient for Optimizing Weight Loss and Body Composition
Published in Robert E.C. Wildman, Richard S. Bruno, Handbook of Nutraceuticals and Functional Foods, 2019
Paul J. Arciero, Michael J. Ormsbee, Robert E.C. Wildman, Donald K. Layman
Dietary protein sources vary within different foods, such as gluten in wheat, albumin in eggs, and casein and whey in milk. Specifically, these proteins are made up of a group of proteins or chemically associated protein molecules. The protein in egg albumin includes ovalbumin, ovotransferrin, ovomucoid, ovomucin, and lysozyme. In the case of milk whey protein, it includes β-lactoglobulin, α-lactalbumin, immunoglobulins, bovine serum albumin, lactoferrin, and lactoperoxidase, as well as glycomacropeptide (GMP), a casein-derived protein in cheese whey, whereas the principal milk casein fractions are α(s1) and α(s2)-caseins, β-casein, and kappa-casein.
Sialylated milk oligosaccharides alter neurotransmitters and brain metabolites in piglets: an In vivo magnetic resonance spectroscopic (MRS) study
Published in Nutritional Neuroscience, 2021
Hong Xin Wang, Yue Chen, Ziaul Haque, Michael de Veer, Gary Egan, Bing Wang
Acidic oligosaccharides containing sialic acid (Sia) glycans are found in rich abundance in human milk but are not found in significant quantities in cow’s milk or infant formulas. α2,3-sialyllactose (3′SL) and α2,6-sialyllactose (6′SL) are the major forms of sialylated milk oligosaccharides (SMOS) in human milk. Sia is a key sugar of SMOS. Approximately 73% of Sia in human milk is conjugated to oligosaccharides, whereas only ∼25% and 3% is present in conjugated protein and free form, respectively [1]. Neural cell membranes contain 20 times more Sia than other types of membranes, indicating that Sia has a clear role in neural structure [2,3]. The location and amount of Sia across the brain changes during development [3]. SMOS play important roles in supporting resistance to pathogens, immune function and promotes gut maturation [1]. Our previous study demonstrated that a dietary Sia-glycopeptide supplement, designated casein-glycomacropeptide and sialylated glycoprotein lactoferrin, increased learning and memory in piglets [4,5]. However, whether SMOS, e.g. SL has a more effective role in promoting neurodevelopment by altering the concentration of important brain metabolites and neurotransmitters remains unknown.
Regulatory T Cells in Bioactive Peptides-Induced Oral Tolerance; a Two-Edged Sword Related to the Risk of Chronic Diseases: A Systematic Review
Published in Nutrition and Cancer, 2021
Meisam Barati, Masoumeh Jabbari, Hamid Nickho, Mojgan Esparvarinha, Amirreza Javadi Mamaghani, Hasan Majdi, Anwar Fathollahi, Sayed Hossein Davoodi
As reported in Table 1, many researchers have tried to treat allergy using BPs mediated OT. The peptides used in these studies had a length from two to more than 100 amino acids with different origins (8, 9, 13, 15, 26, 28). In the summarized experimental studies either Ovalbumin (OVA) or Cow’s Milk Protein (CMP) has been used to induce allergy in animal models. As mentioned in the previous sections, OT is induced by several mechanisms including T-reg expansion, anergy and deletion of T cell clones (11). Although, the summarized studies did not evaluated factors related to anergy or deletion of T cell clones such as cluster of differentiation 152 (CD), Programed cell death protein 1 (PD1) and number of T cells (42); but according to the results of these studies, the main mechanism of OT seems to be T-reg induction. Moronta et al. in an animal model of IgE-mediated food allergy showed that oral administration of Amaranth seed-originated hepta-peptide SSEDIKE significantly improves clinical signs and symptoms of food allergy, which was attributed to T-reg expansion (8). In a similar study Jiménez et al. used orally administered Glycomacropeptide (GMP) with 64 amino acids to treat allergy and reported promising results again (9).
The management of phenylketonuria in adult patients in Italy: a survey of six specialist metabolic centers
Published in Current Medical Research and Opinion, 2021
Alberto Burlina, Vincenzo Leuzzi, Marco Spada, Maria Teresa Carbone, Sabrina Paci, Albina Tummolo
Genotyping has revealed more than 1000 mutations in the PAH gene, which are listed in a PKU-specific database (PAHvdb in BioPKU [http://www.biopku.org/]). Splicing, nonsense mutations, and out-of-frame insertions or deletions generally result in the loss of PAH (null mutations), while missense mutations and certain in-frame insertion-deletion mutations (indels) cause defective protein translation4. Null mutations in both alleles lead to classic PKU, which is characterized by blood Phe levels >1200 µmol/L if left untreated. These patients benefit from a low Phe diet combined with Phe-free L-amino acid-based protein substitutes, glycomacropeptide (GMP)-based protein substitutes and supplementation with slow-release large neutral amino acids (LNAAs)5,6. This diet prevents rises in blood Phe levels which, according to European guidelines3, should be continued to maintain blood Phe levels within the 120–360 µmol/L range when <12 years of age and during pregnancy, and in the 120–600 µmol/L range when >12 years of age. Conversely, American guidelines recommend the 120–360 µmol/L target throughout the patient’s life7.