Objective: To analyze the clinical features of IgE-mediated cow's milk protein allergy (CMPA) in children aged 0-5 years. Methods: This cross-sectional study collected the data on children diagnosed with CMPA in the Department of Allergy at the Children's Hospital of the Capital Institute of Pediatrics from October 2019 to November 2020 and improved peripheral blood routine,total IgE defection, milk specific IgE (sIgE) defection,SPT and milk component defection,diagnosis of severe anaphylaxis based on clinical manifestations. Rank-sum test and chi-square test are used for statistical analysis of clinical characteristics between groups. Results: A total of 106 children (67 boys and 39 girls) were enrolled with the age of 15 (8, 34) months, including 42 cases (≤ 1 year of age), 39 cases (>1-<3 years of age) and 25 cases(≥3 years of age), the onset age of 6 (5, 8) months. Among them, 95 cases (89.6%) were reacted after consuming milk or its products, 42 cases (39.6%) had reaction due to skin contact and 11 cases (10.4%) reacted after exclusive breastfeeding. The onset time of milk product consumption was 45 (1, 120) min, skin contact pathway was 10 (5, 30) min and symptoms in breastfeeding pathway was 121 (61, 180) min. There was statistical difference among the time of symptoms (χ²=77.01, P<0.001).The cutaneous reaction was most common (100 cases, 94.3%), followed by digestive (20 cases, 18.9%) and respiratory (16 cases, 15.1%), and the nervous symptoms (1 case, 0.9%) were uncommon and 24 cases (22.6%) had at least one episode of anaphylaxis. There were 87 cases (82.1%) also diagnosed with other food allergies, 94 cases (88.7%) with previous eczema, 57 cases (53.8%) with history of rhinitis, and 23 cases (21.7%) with history of wheezing. The total IgE level was 191.01 (64.71, 506.80) kU/L, and the cow's milk sIgE level was 3.03 (1.11, 15.24) kU/L. The maximum diameter of the wheal in SPT was 8.2 (4.0, 12.0) mm. Component resolved diagnosis showed that 77 cases (81.9%) were sensitized to at least one out of 4 main components, including casein, α lactalbumin, β lactoglobulin and bovine serum albumin.The possibility of anaphylaxis in children with milk sIgE grade Ⅳ-Ⅵ was higher than that in children with grade 0-Ⅲ (57.7% (15/26) vs. 12.5% (10/80), OR=9.545, 95%CI 3.435-26.523). Children with milk SPT ≥+++ had a higher probability of anaphylaxis than those with milk SPT ≤++ (34.4% (11/32) vs. 11.5% (3/26), OR=4.016, 95%CI 0.983-16.400). Anaphylaxis were more common in α lactalbumin positive children than in negative children (34.3% (13/38) vs. 14.2% (8/56), χ²=1.23，P=0.042). Conclusions: CMPA in children has early onset and diversified clinical manifestations, which are mainly cutaneous symptoms. Most children are sensitized to at least one allergen component. Serum sIgE level, SPT reaction and allergen components play important roles in the diagnosis and evaluation of CMPA, and higher milk sIgE level may predict a higher risk of anaphylaxis.
Allergens ; Anaphylaxis/etiology* ; Animals ; Cattle ; Child ; Cross-Sectional Studies ; Female ; Humans ; Immunoglobulin E ; Lactalbumin ; Male ; Milk Hypersensitivity/diagnosis* ; Skin Tests

Lactoferrin is a natural protein with various physiological activities, which has the function of regulating immunity, anti-microbial, regulating iron absorption, promoting the proliferation of intestinal cells, and multiple pathophysiological processes. In recent years, lactoferrin has been widely used in infants, pregnant women, and the elderly. In order to more comprehensively understand the clinical application of lactoferrin and establish the method and index system of lactoferrin application in different populations, clinical nutritionists, together with experts from multiple disciplines, used the evidence grading method of GRADE Collaboration Network Ⅱ under the principle of evidence-based medicine to search for clinical evidence and repeatedly discuss. The experts group reached a consensus on the effect of lactoferrin reducing the risk of infection in premature infants, the incidence of respiratory and gastrointestinal diseases in infants, improving the anemia status of infants and pregnant women, improving the eradication rate of Helicobacter pylori in children and adults, and improving the immune function of the elderly, which could be used as a reference for medical professionals in clinical work.
Adult ; Infant ; Child ; Humans ; Female ; Pregnancy ; Aged ; Helicobacter Infections ; Lactoferrin ; Consensus ; East Asian People

Protein self-assemblies at the micro- and nano-scale are of great interest because of their morphological diversity and good biocompatibility. High-throughput screening of protein self-assembly at different scales and morphologies using protein crystallization screening conditions is an emerging method. When using this method to screen protein self-assembly conditions, some apparently transparent droplets are often observed, in which it is not clear whether self-assembly occurs. We explored the interaction between β-lactoglobulin and the protein crystallization kit Index™ C10 and observed the presence of micro- and nano-scale protein self-assemblies in the transparent droplets. The diverse morphology of the micro- and nano-scale self-assemblies in the transparent droplets formed by mixing different initial concentrations of β-lactoglobulin and Index™ C10 was further investigated by scanning electron microscope. Self-assembly process of fluorescence-labelled β-lactoglobulin was monitored continuously by laser confocal microscope, allowing real-time observation of the liquid-liquid phase separation phenomenon and the morphology of the final self-assemblies. The internal structure of the self-assemblies was gradually ordered over time by in-situ X-ray diffraction. This indicates that the self-assembly phenomenon within transparent droplets, observed in protein self-assembly condition screening experiments, is worthy of further in-depth exploration.
Crystallization ; Lactoglobulins

Athletes ; Flavones/administration & dosage* ; Humans ; Hydrocortisone/blood* ; Seasons ; Sports Nutritional Physiological Phenomena ; Testosterone/blood* ; Whey Proteins/administration & dosage*

OBJECTIVE: To establish an amino acid assay for the determination of β-lactoglobulin in Anti-HPV biological protein dressing. METHODS: Under acidic conditions, β-lactoglobulin is hydrolyzed into free amino acids, separated by cation exchange chromatography, and derivatived after ninhydrin column. The chromatogram at 570 nm is collected. The content of β-lactoglobulin in the sample is indirectly determined by measuring the lysine content obtained by hydrolysis. RESULTS: β-lactoglobulin has a good linear relationship in the concentration range of 77.28~309.12 μg/mL ( CONCLUSIONS The method is simple, specific, accurate and reproducible, which is suitable for the quantitative analysis of β-lactoglobulin in anti-HPV biological protein dressing.
Amino Acids ; Bandages ; Lactoglobulins

Autoantigens ; metabolism ; Glycoproteins ; metabolism ; Humans ; Immunity, Innate ; immunology ; Lactoferrin ; metabolism ; Nasopharyngeal Carcinoma ; immunology ; metabolism ; Nasopharyngeal Neoplasms ; immunology ; metabolism ; Phosphoproteins ; metabolism ; Proteins ; metabolism

PURPOSE: The aim of this study was to evaluate the clinical significance of inflammatory biomarkers in acute infectious diarrhea among children. METHODS: Clinical parameters including fever, bacterial and viral etiology based on stool culture and multiplex polymerase chain reaction, and nine biomarkers including C-reactive protein (CRP), erythrocyte sedimentation rate (ESR) and leukocytes in blood and calprotectin, lactoferrin, myeloperoxidase, polymorphonuclear elastase, leukocytes, and occult blood in feces were evaluated in children who were hospitalized due to acute diarrhea without underlying disease. RESULTS: A total of 62 patients were included. Among these patients, 33 had fever, 18 showed bacterial infections, and 40 patients were infected with 43 viruses. Of all the biomarkers, CRP was significantly correlated with fever (p<0.001). CRP, ESR, calprotectin, lactoferrin, myeloperoxidase, fecal leukocytes, and occult blood were significantly associated with infection with bacterial pathogens (p<0.001, p=0.04, p=0.03, p=0.003, p=0.02, p=0.03, p=0.002, respectively). The combination of CRP and fecal lactoferrin at their best cut-off values (13.7 mg/L and 22.8 µg/mL, respectively) yielded a sensitivity of 72.2%, and a specificity of 95.5% for bacterial etiology compared with their individual use. CONCLUSION: Blood CRP is a useful diagnostic marker for both fever and bacterial etiology in acute pediatric diarrhea. The combination of CRP and fecal lactoferrin yields better diagnostic capability for bacterial etiology than their use alone for acute diarrhea in children without underlying gastrointestinal disease.
Bacterial Infections ; Biomarkers ; Blood Sedimentation ; C-Reactive Protein ; Child ; Diarrhea ; Feces ; Fever ; Gastrointestinal Diseases ; Humans ; Lactoferrin ; Leukocyte L1 Antigen Complex ; Leukocytes ; Multiplex Polymerase Chain Reaction ; Occult Blood ; Pancreatic Elastase ; Peroxidase ; Sensitivity and Specificity

Postprandial hyperglycemia is associated with the risk of diabetes mellitus, cardiovascular disease, and mortality. Nutrition therapy is an important component of the management of postprandial hyperglycemia. Postprandial glucose levels are determined by several factors, such as the quantity and composition of nutrients, gastric emptying rates, secretion of incretin hormones, insulin secretion, glucose uptake by peripheral tissues, and endogenous glucose production. Nutrient preload and food order (or meal sequence) are dietary approaches targeting these factors. Nutrient preload reduces postprandial glucose excursion by enhancing insulin secretion, augmenting the secretion of glucagonlike peptide-1, and delaying gastric emptying. Carbohydrates-last food order improves glycemic control, increases the secretion of glucagon-like peptide-1, and decreases insulin requirements. Therefore, both nutrient preload and manipulation of food order can be an effective, safe, and feasible strategy for treating hyperglycemia in individuals with diabetes mellitus.
Carbohydrates ; Cardiovascular Diseases ; Diabetes Mellitus ; Gastric Emptying ; Gastrointestinal Hormones ; Glucagon-Like Peptide 1 ; Glucose* ; Hyperglycemia ; Incretins ; Insulin* ; Meals ; Mortality ; Nutrition Therapy ; Whey Proteins

Introduction: It is important to wean mechanically-ventilated patients as early as possible to avoid complications such as ventilator-associated pneumonia. Supplementing the diet with additional protein may help to stimulate muscle protein synthesis which may enhance respiratory muscle function and ventilator drive. This study aims to determine the effect of whey protein supplementation on the duration of mechanical ventilation in intensive care unit patients of Ospital ng Makati. Methods: We enrolled forty eligible patients in this openlabel randomized controlled trial and were assigned into two groups: Group A (N=20): patients were given enteral feeding using commercial formula with added whey protein, given as one serving every eight hours (equivalent to 18 g of additional protein per day) and Group B (N=20): patients were given enteral feeding using commercial formula alone. Weaning was started as soon as the patient fulfilled the criteria of spontaneous breathing trial and was considered successful if the patient maintained these criteria for 48 hours after extubation. Results: Our study’s results showed that the mechanically intubated patients in Group A have lesser ventilatordependent days with an average of 5.4 days as compared to those in Group B with an average of 7.45 days (p=0.00). Patients in Group A were also noted to have statistically significant higher increase in serum albumin, mid-arm circumference and triceps skin fold from baseline. Twentyfive percent of patients in Group B developed ventilator acquired pneumonia and none in Group A. No mortality was noted in both groups. Conclusion Whey protein supplementation in mechanically ventilated patients can be recommended to facilitate early weaning because of its effect on early muscle protein synthesis leading to improvement of lung function and ventilator drive. It can also help in preventing malnutrition and nosocomial infections during critical illness. With all these benefits of whey protein, its use can potentially lead to shorter duration of mechanical ventilation and hospital stay which can also mean less cost of care delivery.
Whey Proteins ; Weaning ; Respiration, Artificial ; Intensive Care Units ; Randomized Controlled Trial

Milk proteins are composed of casein, further classified into αS1-casein, αS2-casein, β-casein, and κ-casein, and whey protein, which is separated into α-lacatalbumin, β-lactoglobulin, serum albumin, and some minor proteins, such as lactoferrin and immunoglobulin. To reduce the allergenicity of protein, heat treatment and enzymatic protein hydrolysis by endopeptidase are necessarily required. Additionally, membrane technology should be applied to produce a protein hydrolyzate, which has consistent molecular weight of peptide and low in free amino acid without allergenic peptide or protein. Extensive casein hydrolyzate and whey protein hydrolyzate are used for protein source of mainly extensively hydrolyzed protein formula (eHF) intended for the treatment of cow's milk allergy. Also, partially hydrolyzed formula (pHF) is developed, which is using a single protein source e.g., whey protein hydrolyzate. The allergenicity of infant formula can be determined according to molecular weight profile and antigenicity reduction compared to intact protein. More than 90% peptides are present in eHF have a molecular weight of <3,000 Da. Peptide molecular weight profiles of pHF range mainly between 3,000 and 10,000 Da, but have a small percentage of >10,000 Da. Generally, antigenicity reduction in eHF and pHF is 10-6 and 10-3, respectively. Even if protein hydrolyzate is manufactured under strict quality control, there is still a risk of cross contamination of allergenic milk components through environmental conditions and the shared manufacturing process. Thus, quality assessment of protein hydrolyzate formula must be performed routinely.
Caseins ; Hot Temperature ; Humans ; Hydrolysis ; Immunoglobulins ; Infant Formula* ; Infant* ; Lactoferrin ; Membranes ; Milk ; Milk Hypersensitivity ; Milk Proteins ; Molecular Weight ; Peptides ; Quality Control ; Serum Albumin ; Whey Proteins