-
Journal of Agricultural and Food... Jun 2024Numerous studies have highlighted the potential of Lactic acid bacteria (LAB) fermentation of whey proteins for alleviating allergies. Nonetheless, the impact of...
Numerous studies have highlighted the potential of Lactic acid bacteria (LAB) fermentation of whey proteins for alleviating allergies. Nonetheless, the impact of LAB-derived metabolites on whey proteins antigenicity during fermentation remains uncertain. Our objective was to elucidate the impact of small molecular metabolites on the antigenicity of α-lactalbumin (α-LA) and β-lactoglobulin (β-LG). Through metabolomic analysis, we picked 13 bioactive small molecule metabolites from subsp. DLPU F-36 for coincubation with α-LA and β-LG, respectively. The outcomes revealed that valine, arginine, benzoic acid, 2-keto butyric acid, and glutaric acid significantly diminished the sensitization potential of α-LA and β-LG, respectively. Moreover, chromatographic analyses unveiled the varying influence of small molecular metabolites on the structure of α-LA and β-LG, respectively. Notably, molecular docking underscored that the primary active sites of α-LA and β-LG involved in protein binding to IgE antibodies aligned with the interaction sites of small molecular metabolites. In essence, LAB-produced metabolites wield a substantial influence on the antigenic properties of whey proteins.
PubMed: 38941263
DOI: 10.1021/acs.jafc.3c08874 -
Scientific Reports Jun 2024Milk is a good source of nutrition but is also a source of allergenic proteins such as α-lactalbumin, β-lactoglobulin (BLG), casein, and immunoglobulins. The Clustered...
Milk is a good source of nutrition but is also a source of allergenic proteins such as α-lactalbumin, β-lactoglobulin (BLG), casein, and immunoglobulins. The Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)/Cas technology has the potential to edit any gene, including milk allergens. Previously, CRISPR/Cas has been successfully employed in dairy cows and goats, but buffaloes remain unexplored for any milk trait. In this study, we utilized the CRISPR/Cas9 system to edit the major milk allergen BLG gene in buffaloes. First, the editing efficiency of designed sgRNAs was tested in fibroblast cells using the T7E assay and Sanger sequencing. The most effective sgRNA was selected to generate clonal lines of BLG-edited cells. Analysis of 15 single-cell clones, through TA cloning and Sanger sequencing, revealed that 7 clones exhibited bi-allelic (-/-) heterozygous, bi-allelic (-/-) homozygous, and mono-allelic (-/+) disruptions in BLG. Bioinformatics prediction analysis confirmed that non-multiple-of-3 edited nucleotide cell clones have frame shifts and early truncation of BLG protein, while multiple-of-3 edited nucleotides resulted in slightly disoriented protein structures. Somatic cell nuclear transfer (SCNT) method was used to produce blastocyst-stage embryos that have similar developmental rates and quality with wild-type embryos. This study demonstrated the successful bi-allelic editing (-/-) of BLG in buffalo cells through CRISPR/Cas, followed by the production of BLG-edited blastocyst stage embryos using SCNT. With CRISPR and SCNT methods described herein, our long-term goal is to generate gene-edited buffaloes with BLG-free milk.
Topics: Animals; Lactoglobulins; Buffaloes; Gene Editing; CRISPR-Cas Systems; RNA, Guide, CRISPR-Cas Systems; Milk; Fibroblasts
PubMed: 38937564
DOI: 10.1038/s41598-024-65359-9 -
Nutrients Jun 2024Depression represents a widespread and devastating psychiatric public health challenge globally. It is particularly prevalent among young adults in Korea. Certain foods...
Depression represents a widespread and devastating psychiatric public health challenge globally. It is particularly prevalent among young adults in Korea. Certain foods may have medicinal properties that alleviate depressive symptoms. This study aimed to examine the association between specific foods and depressive symptoms among young adults, exploring their bioactive effects and possible mechanisms. We conducted a cross-sectional study involving 1000 Korean young adults aged 18-39 years. Food frequency questionnaires were used to assess diets and their associations with depressive symptoms. Results from multivariable logistic regression analysis indicated associations between several specific foods and their effects: milk (odds ratio = 0.58, 95% confidence interval: 0.36-0.94), eggs (0.55, 0.35-0.87), bananas (0.58, 0.36-0.94), oranges (0.62, 0.40-0.96), sweet potatoes (0.60, 0.37-0.97), mushrooms (0.53, 0.31-0.92, females only), and kimchi (0.40, 0.17-0.95, males only). Furthermore, molecular docking indicated that hesperidin had the highest docking score of 5.86 in oranges. Several bioactive compounds identified as potentially beneficial in combatting depression include calcium, casein, alpha-lactalbumin, tryptophan (TRP), vitamin B6 and B12, magnesium, flavonoids (especially hesperidin), carotenoids, ergothioneine, fiber, and probiotics. To recommend these foods in the management of depression among young adults, further clinical intervention studies are necessary.
Topics: Humans; Female; Young Adult; Male; Adult; Depression; Cross-Sectional Studies; Adolescent; Republic of Korea; Diet; Molecular Docking Simulation
PubMed: 38931173
DOI: 10.3390/nu16121818 -
Food Chemistry Jun 2024The research explored the role of γ-oryzanol (γs) on stabilization behavior of Pickering emulsion gels (PEGs) loaded by α-lactalbumin (α-LA) or β-lactoglobulin...
The research explored the role of γ-oryzanol (γs) on stabilization behavior of Pickering emulsion gels (PEGs) loaded by α-lactalbumin (α-LA) or β-lactoglobulin (β-LG), being analyzed by experimental and computer methods (molecular dynamic simulation, MD). Primarily, the average particle size of β-LG-γS was expressed 100.07% decrease over that of α-LA-γS. In addition, γs decreased the dynamic interfacial tension of two proteins with the order of β-LG < α-LA. Meanwhile, quartz crystal microbalance with dissipation proved that β-LG-γS exhibited higher adsorption mass and denser rigid interface layer than α-LA-γS. Moreover, the hydrophobic group of γS had electrostatic repulsion with polar water molecules in the aqueous phase, which spread to the oil phase. β-LG-γS had lower RMSD/Rg value and narrower fluctuation compared with α-LA-γS. This work strength the exploration of interfacial stabilization mechanism of whey protein-based PEGs, which enriched its theoretical research for industrial-scale production as the replacement of trans fat and cholesterol.
PubMed: 38905830
DOI: 10.1016/j.foodchem.2024.140096 -
Nutrients May 2024Milk bioactivity refers to the specific health effects of milk components beyond nutrition. The science of milk bioactivity involves the systematic study of these... (Review)
Review
Milk bioactivity refers to the specific health effects of milk components beyond nutrition. The science of milk bioactivity involves the systematic study of these components and their health effects, as verified by empirical data, controlled experiments, and logical arguments. Conversely, 'faith in milk bioactivity' can be defined as personal opinion, meaning, value, trust, and hope for health effects that are beyond investigation by natural, social, or human sciences. Faith can be strictly secular, but also influenced by spirituality or religion. The aim of this paper is to show that scientific knowledge is frequently supplemented with faith convictions to establish personal and public understanding of milk bioactivity. Mammalian milk is an immensely complex fluid containing myriad proteins, carbohydrates, lipids, and micronutrients with multiple functions across species, genetics, ages, environments, and cultures. Human health includes not only physical health, but also social, mental, and spiritual health, requiring widely different fields of science to prove the relevance, safety, and efficacy of milk interventions. These complex relationships between milk feeding and health outcomes prevent firm conclusions based on science and logic alone. Current beliefs in and understanding of the value of breast milk, colostrum, infant formula, or isolated milk proteins (e.g., immunoglobulins, α-lactalbumin, lactoferrin, and growth factors) show that both science and faith contribute to understand, stimulate, or restrict the use of milk bioactivity. The benefits of breastfeeding for infants are beyond doubt, but the strong beliefs in its health effects rely not only on science, and mechanisms are unclear. Likewise, fear of, or trust in, infant formula may rely on both science and faith. Knowledge from science safeguards individuals and society against 'milk bioactivity superstition'. Conversely, wisdom from faith-based convictions may protect science from unrealistic 'milk bioactivity scientism'. Honesty and transparency about the potentials and limitations of both scientific knowledge and faith convictions are important when informing individuals and society about the nutritious and bioactive qualities of milk.
Topics: Humans; Milk, Human; Infant; Infant Nutritional Physiological Phenomena; Breast Feeding; Infant Formula; Infant, Newborn; Female; Colostrum; Health Knowledge, Attitudes, Practice; Animals; Milk Proteins; Religion
PubMed: 38892610
DOI: 10.3390/nu16111676 -
Veterinary Microbiology Jun 2024Bovine leukemia virus (BLV) is a widespread virus that decreases milk production and quality in dairy cows. As crucial components of BLV, BLV-encoded microRNAs...
Bovine leukemia virus (BLV) is a widespread virus that decreases milk production and quality in dairy cows. As crucial components of BLV, BLV-encoded microRNAs (BLV-miRNAs) affect BLV replication and may impact the synthesis of Lactoferrin (LTF), Lactoperoxidase (LPO), Alpha-lactalbumin (alpha-LA), and Beta-lactoglobulin (beta-LG). In this study, we investigated the targeting relationship between BLV-miRNAs and LTF, LPO, alpha-LA, and beta-LG in cow's milk. Additionally, we investigated the possible mechanisms by which BLV reduces milk quality. The results showed that cow's milk had significantly lower levels of LTF, LPO, and alpha-LA proteins in BLV-positive cows than in BLV-negative cows. BLV-△miRNAs (miRNA-deleted BLV) enhanced the reduction of LPO, alpha-LA, and beta-LG protein levels caused by BLV infection. Multiple BLV-miRNAs have binding sites with LTF and LPO mRNA; however, only BLV-miR-B1-5 P has a targeting relationship with LPO mRNA. The results revealed that BLV-miR-B1-5 P inhibits LPO protein expression by targeting LPO mRNA. However, BLV does not directly regulate the expression of LTF, alpha-LA, or beta-LG proteins through BLV-miRNAs.
PubMed: 38889618
DOI: 10.1016/j.vetmic.2024.110153 -
Food Research International (Ottawa,... Jul 2024Whey protein isolate (WPI) is mainly composed of β-lactoglobulin (β-LG), α-lactalbumin (α-LA) and bovine serum albumin (BSA). The aim of this study was to compare...
Whey protein isolate (WPI) is mainly composed of β-lactoglobulin (β-LG), α-lactalbumin (α-LA) and bovine serum albumin (BSA). The aim of this study was to compare and analyze the influence of WPI and its three main constituent proteins, as well as proportionally reconstituted WPI (R-WPI) on resveratrol. It was found that the storage stability of resveratrol was protected by WPI, not affected by R-WPI, but reduced by individual whey proteins at 45°C for 30 days. The rank of accelerated degradation of resveratrol by individual whey proteins was BSA > α-LA > β-LG. The antioxidant activity, localization of resveratrol and oxidation of carrier proteins were determined by ABTS, HO assay, synchronous fluorescence, carbonyl and circular dichroism. The non-covalent interactions and disulfide bonds between constituent proteins improved the antioxidant activity of the R-WPI-resveratrol complex, the oxidation stability of the carrier and the solvent shielding effect on resveratrol, which synergistically inhibited the degradation of resveratrol in R-WPI system. The results gave insight into elucidating the interaction mechanism of resveratrol with protein carriers.
Topics: Resveratrol; Whey Proteins; Lactalbumin; Antioxidants; Lactoglobulins; Serum Albumin, Bovine; Oxidation-Reduction; Circular Dichroism
PubMed: 38823871
DOI: 10.1016/j.foodres.2024.114485 -
Nutrients May 2024Human milk (HM) contains the essential macronutrients and bioactive compounds necessary for the normal growth and development of newborns. The milk collected by human...
Human milk (HM) contains the essential macronutrients and bioactive compounds necessary for the normal growth and development of newborns. The milk collected by human milk banks is stored frozen and pasteurized, reducing its nutritional and biological value. The purpose of this study was to determine the effect of hyperbaric storage at subzero temperatures (HS-ST) on the macronutrients and bioactive proteins in HM. As control samples, HM was stored at the same temperatures under 0.1 MPa. A Miris HM analyzer was used to determine the macronutrients and the energy value. The lactoferrin (LF), lysozyme (LYZ) and lactalbumin (LAC) content was checked using high-performance liquid chromatography, and an ELISA test was used to quantify secretory immunoglobulin A (sIgA). The results showed that the macronutrient content did not change significantly after 90 days of storage at 60 MPa/-5 °C, 78 MPa/-7 °C, 111 MPa/-10 °C or 130 MPa/-12 °C. Retention higher than 90% of LYZ, LAC, LF and sIgA was observed in the HM stored at conditions of up to 111 MPa/-10 °C. However, at 130 MPa/-12 °C, there was a reduction in LYZ and LF, by 39 and 89%, respectively. The storage of HM at subzero temperatures at 0.1 MPa did not affect the content of carbohydrates or crude and true protein. For fat and the energy value, significant decreases were observed at -5 °C after 90 days of storage.
Topics: Humans; Milk, Human; Nutritive Value; Lactoferrin; Food Storage; Muramidase; Lactalbumin; Immunoglobulin A, Secretory; Nutrients; Milk Proteins; Female
PubMed: 38794693
DOI: 10.3390/nu16101455 -
ACS Applied Materials & Interfaces Jun 2024Protein adsorption on solid surfaces is a process relevant to biological, medical, industrial, and environmental applications. Despite this wide interest and advancement...
Protein adsorption on solid surfaces is a process relevant to biological, medical, industrial, and environmental applications. Despite this wide interest and advancement in measurement techniques, the complexity of protein adsorption has frustrated its accurate prediction. To address this challenge, here, data regarding protein adsorption reported in the last four decades was collected, checked for completeness and correctness, organized, and archived in an upgraded, freely accessible Biomolecular Adsorption Database, which is equivalent to a large-scale, ad hoc, crowd-sourced multifactorial experiment. The shape and physicochemical properties of the proteins present in the database were quantified on their molecular surfaces using an in-house program (ProMS) operating as an add-on to the PyMol software. Machine learning-based analysis indicated that protein adsorption on hydrophobic and hydrophilic surfaces is modulated by different sets of operational, structural, and molecular surface-based physicochemical parameters. Separately, the adsorption data regarding four "benchmark" proteins, i.e., lysozyme, albumin, IgG, and fibrinogen, was processed by piecewise linear regression with the protein monolayer acting as breakpoint, using the linearization of the Langmuir isotherm formalism, resulting in semiempirical relationships predicting protein adsorption. These relationships, derived separately for hydrophilic and hydrophobic surfaces, described well the protein concentration on the surface as a function of the protein concentration in solution, adsorbing surface contact angle, ionic strength, pH, and temperature of the carrying fluid, and the difference between pH and the isoelectric point of the protein. When applying the semiempirical relationships derived for benchmark proteins to two other "test" proteins with known PDB structure, i.e., β-lactoglobulin and α-lactalbumin, the errors of this extrapolation were found to be in a linear relationship with the dissimilarity between the benchmark and the test proteins. The work presented here can be used for the estimation of operational parameters modulating protein adsorption for various applications such as diagnostic devices, pharmaceuticals, biomaterials, or the food industry.
Topics: Adsorption; Surface Properties; Hydrophobic and Hydrophilic Interactions; Data Mining; Proteins; Muramidase; Databases, Protein; Machine Learning
PubMed: 38787331
DOI: 10.1021/acsami.4c06759 -
Journal of Food Science May 2024Cow milk allergy is one of the common food allergies. Our previous study showed that the allergenicity of fermented milk is lower than that of unfermented skimmed milk...
Cow milk allergy is one of the common food allergies. Our previous study showed that the allergenicity of fermented milk is lower than that of unfermented skimmed milk in vitro, and the antigenicity of β-lactoglobulin and α-lactalbumin in fermented milk was decreased by 67.54% and 80.49%, respectively. To confirm its effects in vivo, allergic BALB/C mice model was used to further study the allergenicity of fermented milk. It was found that compared with the skim milk (SM) group, the intragastrically sensitization with fermented milk had no obvious allergic symptoms and the fingers were more stable: lower levels of IgE, IgG, and IgA in serum, lower levels of plasma histamine and mast cell protein-1, and immune balance of Th1/Th2 and Treg/Th17. At the same time, intragastrically sensitization with fermented milk increased the α diversity of intestinal microbiota and changed the microbiota abundance: the relative abundance of norank-f-Muribaculaceae and Staphylococcus significantly decreased, and the abundance of Lachnospiraceae NK4A136 group, Bacteroides, and Turicibacter increased. In addition, fermented milk can also increase the level of short-chain fatty acids in the intestines of mice. It turns out that fermented milk is much less allergenicity than SM. PRACTICAL APPLICATION: Fermentation provides a theoretical foundation for reducing the allergenicity of milk and dairy products, thereby facilitating the production of low-allergenic dairy products suitable for individuals with milk allergies.
PubMed: 38778560
DOI: 10.1111/1750-3841.17136