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Ultrasonics Sonochemistry May 2023The purpose of this study was to investigate effect of physical treatment (ultrasound, U/high pressure homogenization, H/combined treatment, UH or HU) and surfactant...
The purpose of this study was to investigate effect of physical treatment (ultrasound, U/high pressure homogenization, H/combined treatment, UH or HU) and surfactant (Mogroside V, Mog) on air/water interface adsorption and foaming properties of α-lactalbumin (ALa). Firstly, the binding of Mog and all physical-treated ALa was a static quenching process. Mog had the greatest binding affinity for HU-ALa among all treated samples. U or H treatment could change surface hydrophobicity of ALa/Mog complex. Secondly, at the molar ratio (ALa:Mog) of 1:50, foaming ability (FA) of all ALa samples got the maximum. The sequence of FA in ALa and ALa/Mog complex was listed as follow: HU > U > H > UH. Moreover, foaming stability (FS) of HU-ALa was the highest, followed by H-ALa, U-ALa and UH-ALa. Meanwhile, low concentration Mog increased FS of ALa or UH-ALa, but it reduced FS of H-ALa, U-ALa and HU-ALa. Quartz crystal microbalance with dissipation monitoring (QCM-D) experiment indicated that ALa/Mog complex after U or H treatment was quickly absorbed at air/water interface, compared with the treated ALa, and HU-ALa/Mog had the largest frequency shift. In addition, HU-ALa had the thickest bubble membrane and the highest dissipation shift in all samples, indicating that the absorbed membrane thickness and viscoelasticity of samples was correlated with foam stability. Therefore, U and H treatment synergism with Mog was an effective approach to enhance foam properties of ALa, which indicated that HU-treated ALa/Mog complex could be viewed as the safe and efficient foaming agent applied in food processing.
Topics: Lactalbumin; Surface-Active Agents; Water
PubMed: 36965313
DOI: 10.1016/j.ultsonch.2023.106369 -
Food Science & Nutrition Jan 2021This systematic review aimed at investigating longitudinal changes in human milk bioactive protein concentrations in Chinese population. Both English and Chinese... (Review)
Review
This systematic review aimed at investigating longitudinal changes in human milk bioactive protein concentrations in Chinese population. Both English and Chinese databases were searched. The data were pooled into six defined lactation stages. Weighted means of protein concentrations in each stage and the statistical significance of means of different lactation stages were calculated. The data of 11 bioactive proteins were retrieved. Concentrations of sIgA, IgM, and IgG decreased sharply during the first 14 days of lactation. The levels of α-lactalbumin, lactoferrin, and β-casein also decreased throughout lactation. Conversely, lysozyme levels increased over lactation. The changing patterns of the serum albumin, osteopontin, and bile salt-stimulated lipase (BSSL) were not conclusive. This study represents the most comprehensive summary of bioactive proteins in Chinese human milk. In the future, mass spectrometry-based analysis of human milk proteomics may be used to investigate the longitudinal changes of many more bioactive proteins.
PubMed: 33473267
DOI: 10.1002/fsn3.2061 -
Food Science of Animal Resources Jul 2023Whey protein (WP) has nutritional value, but the presence of β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) cause allergic reactions. In this study, hypoallergenic...
Whey protein (WP) has nutritional value, but the presence of β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) cause allergic reactions. In this study, hypoallergenic whey protein hydrolyate (HWPH) was prepared by decomposing β-LG and α-LA of WP using exo- and endo-type proteases. The enzyme mixing ratio and reaction conditions were optimized using response surface methodology (RSM). Degradation of α-LA and β-LG was confirmed through gel electrophoresis, and digestion, and absorption rate, and immunostimulatory response were measured using and systems. Through RSM analysis, the optimal hydrolysis conditions for degradation of α-LA and β-LG included a 1:1 mixture of Alcalase and Prozyme reacted for 10 h at a 1.0% enzyme concentration relative to substrate. The molecular weight of HWPH was <5 kDa, and leucine was the prominent free amino acid. Both and tests showed that digestibility and intestinal permeability were higher in HWPH than in WP. In BALB/c mice, as compared to WP, HWPH reduced allergic reactions by inducing elevated Type 1/Type 2 helper T cell ratio in the blood, splenocytes, and small intestine. Thus, HWPH may be utilized in a variety of low allergenicity products intended for infants, adults, and the elderly.
PubMed: 37484001
DOI: 10.5851/kosfa.2023.e21 -
Journal of Animal Science and... 2016Milk is synthesized by mammary epithelial cells of lactating mammals. The synthetic capacity of the mammary gland depends largely on the number and efficiency of... (Review)
Review
Milk is synthesized by mammary epithelial cells of lactating mammals. The synthetic capacity of the mammary gland depends largely on the number and efficiency of functional mammary epithelial cells. Structural development of the mammary gland occurs during fetal growth, prepubertal and post-pubertal periods, pregnancy, and lactation under the control of various hormones (particularly estrogen, growth hormone, insulin-like growth factor-I, progesterone, placental lactogen, and prolactin) in a species- and stage-dependent manner. Milk is essential for the growth, development, and health of neonates. Amino acids (AA), present in both free and peptide-bound forms, are the most abundant organic nutrients in the milk of farm animals. Uptake of AA from the arterial blood of the lactating dam is the ultimate source of proteins (primarily β-casein and α-lactalbumin) and bioactive nitrogenous metabolites in milk. Results of recent studies indicate extensive catabolism of branched-chain AA (leucine, isoleucine and valine) and arginine to synthesize glutamate, glutamine, alanine, aspartate, asparagine, proline, and polyamines. The formation of polypeptides from AA is regulated not only by hormones (e.g., prolactin, insulin and glucocorticoids) and the rate of blood flow across the lactating mammary gland, but also by concentrations of AA, lipids, glucose, vitamins and minerals in the maternal plasma, as well as the activation of the mechanistic (mammalian) target rapamycin signaling by certain AA (e.g., arginine, branched-chain AA, and glutamine). Knowledge of AA utilization (including metabolism) by mammary epithelial cells will enhance our fundamental understanding of lactation biology and has important implications for improving the efficiency of livestock production worldwide.
PubMed: 27042295
DOI: 10.1186/s40104-016-0078-8 -
Nature Communications Jun 2021Partially unfolded alpha-lactalbumin forms the oleic acid complex HAMLET, with potent tumoricidal activity. Here we define a peptide-based molecular approach for... (Randomized Controlled Trial)
Randomized Controlled Trial
Partially unfolded alpha-lactalbumin forms the oleic acid complex HAMLET, with potent tumoricidal activity. Here we define a peptide-based molecular approach for targeting and killing tumor cells, and evidence of its clinical potential (ClinicalTrials.gov NCT03560479). A 39-residue alpha-helical peptide from alpha-lactalbumin is shown to gain lethality for tumor cells by forming oleic acid complexes (alpha1-oleate). Nuclear magnetic resonance measurements and computational simulations reveal a lipid core surrounded by conformationally fluid, alpha-helical peptide motifs. In a single center, placebo controlled, double blinded Phase I/II interventional clinical trial of non-muscle invasive bladder cancer, all primary end points of safety and efficacy of alpha1-oleate treatment are reached, as evaluated in an interim analysis. Intra-vesical instillations of alpha1-oleate triggers massive shedding of tumor cells and the tumor size is reduced but no drug-related side effects are detected (primary endpoints). Shed cells contain alpha1-oleate, treated tumors show evidence of apoptosis and the expression of cancer-related genes is inhibited (secondary endpoints). The results are especially encouraging for bladder cancer, where therapeutic failures and high recurrence rates create a great, unmet medical need.
Topics: Amino Acid Sequence; Apoptosis; Cell Line, Tumor; Endocytosis; Endpoint Determination; Gene Expression Regulation, Neoplastic; Humans; Oleic Acids; Peptides; Placebos; Protein Conformation; Proton Magnetic Resonance Spectroscopy; Thermodynamics; Urinary Bladder Neoplasms
PubMed: 34103518
DOI: 10.1038/s41467-021-23748-y -
Molecules (Basel, Switzerland) Jun 2020Identifying DPP-IV inhibitory peptides from dietary protein has attracted increased attention. In the present study, bovine α-lactalbumin hydrolysates were generated by...
Identifying DPP-IV inhibitory peptides from dietary protein has attracted increased attention. In the present study, bovine α-lactalbumin hydrolysates were generated by alcalase for various hydrolysis times, and DPP-IV inhibitory activity of these hydrolysates was determined. The 4 h hydrolysates displayed the most potent DPP-IV inhibitory activity, with DPP-IV inhibition rate of 82.30 ± 1.39% at concentration of 1.0 mg/mL. DPP-IV inhibitory peptides were isolated from the 4 h-hydrolysates with gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). Using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI MS/MS), two DPP-IV inhibitory peptides were identified, and their amino acid sequences were Glu-Leu-Lys-Asp-Leu-Lys-Gly-Tyr (ELKDLKGY) and Ile-Leu-Asp-Lys-Val-Gly-Ile-Asn-Tyr (ILDKVGINY), respectively. Furthermore, molecular docking analysis showed that peptides ELKDLKGY and ILDKVGINY could form hydrogen bonds, pi-cation interactions, and salt bridges with DPP-IV. These findings indicated that bovine α-lactalbumin may be a potential source of natural DPP-IV inhibitor.
Topics: Animals; Cattle; Dipeptidyl Peptidase 4; Dipeptidyl-Peptidase IV Inhibitors; Lactalbumin; Peptide Fragments
PubMed: 32630113
DOI: 10.3390/molecules25133009 -
Ultrasonics Sonochemistry Mar 2021α-lactalbumin was modified by ultrasound (US, 20 kHz, 43 ± 3.4 W/cm) pre-treatments (0, 15, 30 and 60 min) and laccase cross-linking of sonicated α-lactalbumin...
α-lactalbumin was modified by ultrasound (US, 20 kHz, 43 ± 3.4 W/cm) pre-treatments (0, 15, 30 and 60 min) and laccase cross-linking of sonicated α-lactalbumin was used to evaluate the physical and oxidative stability of conjugated linoleic acid (CLA) emulsions. The emulsions prepared with laccase cross-linking US-α-lactalbumin (α-lactalbumin treated with US pre-treatment) and US-α-lactalbumin were scrutinized for oxidative and physical stability at room temperature for two weeks of storage. Laccase cross-linking US-α-lactalbumin (Lac-US-α-lactalbumin) revealed improved physical stability in comparison with US-α-lactalbumin, specified by droplet size, structural morphology, adsorbed protein, emulsifying properties and creaming index. SDS-PAGE analysis showed that there was formation of polymers in Lac-US-α-lactalbumin emulsion. Surface hydrophobicity of Lac-US-α-lactalbumin was higher than that of US-α-lactalbumin, and gradually enhanced with the increase of ultrasound time. More importantly, the measurements of peroxide values and conjugated dienes were used to study the oxidative stability of the CLA emulsions. The Lac-US-α-lactalbumin emulsion proved to be reducing the synthesis of fatty acid hydroperoxides and less conjugated dienes compared to the native and US-α-lactalbumin emulsions. This study revealed that the combination of US pre-treatment and laccase cross-linking might be an effective technique for the modification of CLA emulsions.
Topics: Adsorption; Electric Conductivity; Emulsions; Hydrogen-Ion Concentration; Laccase; Lactalbumin; Linoleic Acids, Conjugated; Oils; Oxidation-Reduction; Sonication; Temperature; Water
PubMed: 33125963
DOI: 10.1016/j.ultsonch.2020.105365 -
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 -
Food Science & Nutrition Apr 2021α-Dicarbonyl compounds (α-DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α-DCs were endowed with the...
Effect of methylglyoxal on the alteration in structure and digestibility of α-lactalbumin, and the formation of advanced glycation end products under simulated thermal processing.
α-Dicarbonyl compounds (α-DCs) are a class of compounds generated during the thermal processing of food. Due to the high reactivity, α-DCs were endowed with the ability to react with food components thus lowering nutrition value and even leading to a potential risk for food safety. In this study, methylglyoxal (MG), the most abundant α-DCs, was selected to investigate the alteration effects on the structure and digestibility of α-lactalbumin (αLA) under thermal processing (60-100°C). The results showed that the modification degree of αLA by MG increased with the rise of processing temperature, accompanied by the significant changes in molecular weight, intrinsic fluorescence, and secondary structures of αLA. High-resolution mass spectrometry analysis identified that lysine (Lys) and arginine (Arg) are the modification sites, and N-(carboxyethyl)-L-lysine is the main modification type. Since the Lys and Arg are also the cleavage sites of trypsin, the digestibility of MG modified αLA (MG-αLA) by trypsin correspondingly decreased with an increase of processing temperature. The reacted Lys and Arg residues, and the protein-bound AGEs were quantified, and the contents were found to be highly dependent on the temperature.
PubMed: 33841846
DOI: 10.1002/fsn3.2211 -
Foods (Basel, Switzerland) Mar 2022Milk is a food of high nutritional value processed by heat treatment. Heat treatment of milk is a technological process designed to inhibit the growth of microorganisms...
Milk is a food of high nutritional value processed by heat treatment. Heat treatment of milk is a technological process designed to inhibit the growth of microorganisms and extend the shelf life of products. The heating process directly affects the molecular structure of whey proteins by the process of denaturation. It leads to the formation of a whey protein−casein polymer complex. Based on these facts, milk heat-treatment conditions should be controlled during milk processing. This work focuses on describing the whey protein denaturation process and formation of the complex of whey protein with casein. The effect of heat treatment on individual milk protein fractions alpha-casein (α-cas), beta-casein (β-cas), kappa-casein (κ-cas), beta-lactoglobulin (β-lg) and alpha-lactalbumin (α-la) was studied by SDS-PAGE. Formation of the whey protein−casein polymer complex increased significantly (p < 0.05) on increasing the temperature and duration of the heat treatment.
PubMed: 35407110
DOI: 10.3390/foods11071023