• Pediatric Gastroenterology, Hepatology & Nutrition
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• v.26 no.5
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• pp.277-283
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• 2023

Purpose: Cow's milk protein allergy (CMPA) is a common condition in infants, but little is known about healthcare providers' clinical experience treating infants with CMPA. To address this gap, we analyzed prospectively collected data from healthcare providers (HCPs) who treated infants under six months old with suspected CMPA using hypoallergenic formulas. The study focused on a commercial extensively hydrolyzed formula containing Lactobacillus rhamnosus GG (ATCC53103) (eHF-LGG) or a commercial amino acid formula (AAF). Methods: In this secondary analysis of prospectively collected survey data, 52 HCPs treated 329 infants under six months old with suspected CMPA using hypoallergenic formulas. A series of two de-identified surveys per patient were collected by HCPs to assess short-term symptom relief in the patients and HCP's satisfaction with the management strategies. The initial survey was completed at the initiation of treatment of CMPA, and the second survey was completed at a follow-up visit. Results: The majority of HCPs (87%) in the study were general pediatricians, and most saw 2 to 10 CMPA patients weekly. Results showed that clinicians reported satisfaction with treatment in 95% of patients in the EHF cohort and 97% of patients in the AAF cohort and achieved expected clinical results in 93% and 97% of patients using eHF and AAF, respectively. Furthermore, few patients were switched from the hypoallergenic formula once initiated. Conclusion: The study provides new insights into HCP perspectives on treating infants with CMPA and supports using hypoallergenic formulas to manage this condition. However, additional prospective controlled studies are needed to confirm these initial findings.

• Journal of Dairy Science and Biotechnology
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• v.26 no.1
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• pp.27-36
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• 2008

This review was written to introduce updated data on the structure and function of the major milk proteins identified as allergens, the characterization of their epitopes in each allergenic milk proteins, and the reduction of milk protein allergenicity. Most mammalian milk protein, even protein present at low concentration, are potential allergens. Epitopes identified in milk proteins are both conformational(structured epitope) and sequential epitopes(linear epitope), throughout the protein molecules. Epitopes on casein and whey proteins are reported to be sequential epitope and conformational epitopes, respectively. Conformational epitopes on whey protein are changed into sequential epitope by heat denaturation during heat treatment. Several methods have been proposed to reduce allergenicity of milk proteins. Most ideal and acceptable method to make hypoallergenic milk or formula, so far, is the hydrolysis of allergenic milk proteins by enzymes that has substrate specificity, such as pepsin, trypsin, or chymotrypsin. Commercial formulas based on milk protein hydrolysate are available for therapeutic purpose, hypoantigenic formula for infants from families with a history of milk allergy and hypoallergenic formula for infants with existing allergic symptoms.

• Food Science of Animal Resources
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• v.37 no.6
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• pp.940-947
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• 2017

Goat milk has a protein composition similar to that of breast milk and contains abundant nutrients, but its use in functional foods is rather limited in comparison to milk from other sources. The aim of this study was to prepare a goat A2 ${\beta}$-casein fraction with improved digestibility and hypoallergenic properties. We investigated the optimal conditions for the separation of A2 ${\beta}$-casein fraction from goat milk by pH adjustment to pH 4.4 and treating the casein suspension with calcium chloride (0.05 M for 1 h at $25^{\circ}C$). Selective reduction of ${\beta}$- lactoglobulin and ${\alpha}_s$-casein was confirmed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography. The hypoallergenic property of A2 ${\beta}$-casein fraction was examined by measuring the release of histamine and tumor necrosis factor alpha from HMC-1 human mast cells exposed to different proteins, including A2 ${\beta}$-casein fraction. There was no significant difference in levels of both indicators between A2 ${\beta}$-casein treatment and the control (no protein treatment). The A2 ${\beta}$-casein fraction is abundant in essential amino acids, especially, branched-chain amino acids (leucine, valine, and isoleucine). The physicochemical properties of A2 ${\beta}$-casein fraction, including protein solubility and viscosity, are similar to those of bovine whole casein which is widely used as a protein source in various foods. Therefore, the goat A2 ${\beta}$-casein fraction may be useful as a food material with good digestibility and hypoallergenic properties for infants, the elderly, and people with metabolic disorders.

• 축산식품과학과 산업
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• v.10 no.2
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• pp.11-18
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• 2021

• Pediatric Gastroenterology, Hepatology & Nutrition
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• v.11 no.sup1
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• pp.7-14
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• 2008

Special formulas are those in which one of the basic nutrients (usually the protein and/or carrbohydrate) has been changed to an alternative nutrient that an individual baby may better tolerate. The following are specialized formulas : Soy formulas, hypoallergenic formulas, Lactose free formulas, Premature baby formulas, Low phosphate formulas, Formulas for inborn errors of metabolism. Less is known about the long-term effects of feeding babies these special formulas and each formula has its unique properties and indications. The pediatrician must acquaint themselves with all commercially available infant formulas so as to provide the parent with reliable and unbiased information about them.

• Food Science and Industry
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• v.52 no.1
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• pp.60-67
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• 2019

Protein is a major nutrient of food and has long been studied for nutritional and utility value. Among them, rice protein is attracting attention because of its hypoallergenic characteristics and nutritional value. Rice proteins are divided into endosperm protein and bran protein depending on their location. The two proteins differ in their nutritional characteristics and applications. The endosperm protein is an insoluble protein and has an advantage of digestion and absorption. Rice bran protein dissolves well in water. Its amino acid value is high enough to be comparable to that of soy protein, and it has strong antioxidant ability. Rice protein is a healthy vegetable protein because of its health and hypoallergenic properties. It has been widely used in children's or patients' food, and recently for muscle supplement and health food. Rice protein is considered to be a very effective and useful material as it has been discovered so far.

• Journal of Plant Biotechnology
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• v.42 no.2
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• pp.123-128
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• 2015

Pregermination treatment of cocoa beans either with the testa, group PCB (+T), or without the testa, group PCB (-T), was studied here to determine whether this treatment (incubation up to 120 h at $25^{\circ}C$) has any effect on the levels of allergenic proteins or on chemical composition. Our proximate analysis included carbohydrates, proteins, and lipids. We used western blotting to measure changes in the amounts of allergenic proteins in the cocoa beans during the pregermination treatment. The protein and carbohydrate content of both groups (with or without the testa) decreased slightly during this treatment, whereas lipid content increased. Group PCB (-T) showed more rapid metabolic processes than did group PCB (+T) during the pregermination treatment. Western blot analysis showed that the cocoa beans contained an allergenic protein of ~28 kDa. Removal of the testa strongly reduced the amount of this allergenic protein after 72 h of the pregermination treatment. Generally, the pregermination treatment increased antioxidant activity in both groups. Significant differences in the antioxidant activity were observed between groups PCB (-T) and PCB (+T). Particularly, group PCB (-T) showed high antioxidant activity at 72 h of the pregermination treatment. Thus, the combination of cocoa beans without the testa and pregermination treatment (72 h) seems to be the optimal method for production of hypoallergenic cocoa beans rich in antioxidants for patients with allergic disorders.

• Food Science of Animal Resources
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• v.43 no.4
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• pp.594-611
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• 2023

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 in vitro and in vivo 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 in vitro and in vivo 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.

• Journal of Dairy Science and Biotechnology
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• v.31 no.1
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• pp.67-73
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• 2013

Food allergy is defined as adverse reactions toward food mediated by aberrant immune mechanisms. Cow's milk allergy is one of the most common food allergies in childhood. This allergy is normally outgrown in the first year of life, however 15% of allergic children remain allergic. Cow's milk allergy seem to be associated with casein (${\alpha}_{s1}$-CN), ${\beta}$-lactoglobulin and whey protein. In addition to this, many other milk proteins are antigenic and capable of inducing immune responses. Various food processing affects the stability, structure and intermolecular interactions of cow milk proteins, as a result reduction the allergenic capacity. Heating, hydrolysis, chemical, proteolytic and other processes such as gamma-ray irradiation, high pressure, using probiotics treatments of milk to obtain hypoallergenic milk have been developed to reduce allergic reactions.

• Food Science of Animal Resources
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• v.36 no.4
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• pp.516-522
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• 2016

Goat milk is highly nutritious and is consumed in many countries, but the development of functional foods from goat milk has been slow compared to that for other types of milk. The aim of this study was to develop a goat milk protein hydrolysate (GMPH) with enhanced digestibility and better hypoallergenic properties in comparison with other protein sources such as ovalbumin and soy protein. Goat milk protein was digested with four commercial food-grade proteases (separately) under various conditions to achieve the best hydrolysis of α_s -casein and β-lactoglobulin. It was shown that treatment with alcalase (0.4%, 60℃ for 30 min) effectively degraded these two proteins, as determined by SDS-PAGE, measurement of nonprotein nitrogen content, and reverse-phase high-performance liquid chromatography. Hydrolysis with alcalase resulted in a significant decrease in β-lactoglobulin concentration (almost to nil) and a ~40% reduction in the level of α_s-casein. Quantification of histamine and TNF-α released from HMC-1 cells (human mast cell line) showed that the GMPH did not induce an allergic response when compared to the control. Hence, the GMPH may be useful for development of novel foods for infants, the elderly, and convalescent patients, to replace cow milk.