scholarly journals Effects of Microwaves, Ultrasonication, and Thermosonication on the Secondary Structure and Digestibility of Bovine Milk Protein

Foods ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 138
Author(s):  
Jin Wang ◽  
Rachit Saxena ◽  
Sai Kranthi Vanga ◽  
Vijaya Raghavan

Cow’s milk is considered an excellent protein source. However, the digestibility of milk proteins needs to be improved. This study aimed to evaluate the relationship between the functional properties of milk proteins and their structure upon microwave, ultrasound, and thermosonication treatments. The protein content, digestibility, and secondary-structure changes of milk proteins were determined. The results demonstrated that almost 35% of the proteins in the untreated samples had a α-helix structure and approximately 29% a β-sheet and turns structure. Regarding the untreated samples, the three treatments increased the α-helices and correspondingly decreased the β-sheets and turns. Moreover, the highest milk protein digestibility was observed for the ultrasound-treated samples (90.20–94.41%), followed by the microwave-treated samples (72.56–93.4%), whereas thermosonication resulted in a lower digestibility (68.76–78.81%). The milk protein content was reduced as the microwave processing time and the temperature increased. The final milk protein available in the sample was lower when microwave processing was conducted at 75 °C and 90 °C compared to 60 °C, whereas the ultrasound treatment significantly improved the protein content, and no particular trend was observed for the thermosonicated samples. Thus, ultrasound processing shows a potential application in improving the protein quality of cow’s milk.

Dairy ◽  
2021 ◽  
Vol 2 (2) ◽  
pp. 191-201
Author(s):  
Young W. Park ◽  
George F. W. Haenlein

A new type of cow’s milk, called A2 milk, has appeared in the dairy aisles of supermarkets in recent years. Cows’ milk generally contains two major types of beta-casein as A1 and A2 types, although there are 13 genetic variants of β-casein: A1, A2, A3, A4, B, C, D, E, F, H1, H2, I and G. Studies have shown that A1 β-casein may be harmful, and A2 β-casein is a safer choice for human health especially in infant nutrition and health. The A2 cow milk is reportedly easier to digest and better absorb than A1 or other types of milk. The structure of A2 cow’s milk protein is more comparable to human breast milk, as well as milk from goats, sheep and buffalo. Digestion of A1 type milk produces a peptide called β-casomorphin-7 (BCM-7), which is implicated with adverse gastrointestinal effects on milk consumption. In addition, bovine milk contains predominantly αs1-casein and low levels or even absent in αs2-casein, whereby caprine milk has been recommended as an ideal substitute for patients suffering from allergies against cow milk protein or other food sources. Since goat milk contains relatively low levels of αs1-casein or negligible its content, and αs2-casein levels are high in the milk of most dairy goat breeds, it is logical to assume that children with a high milk sensitivity to αs1-casein should tolerate goat milk well. Cow milk protein allergy (CMPA) is considered a common milk digestive and metabolic disorder or allergic disease with various levels of prevalence from 2.5% in children during the first 3 years of life to 12–30% in infants less than 3 months old, and it can go up to even as high as 20% in some countries. CMPA is an IgE-mediated allergy where the body starts to produce IgE antibodies against certain protein (allergens) such as A1 milk and αs1-casein in bovine milk. Studies have shown that ingestion of β-casein A1 milk can cause ischemic heart disease, type-1 diabetes, arteriosclerosis, sudden infant death syndrome, autism, schizophrenia, etc. The knowledge of bovine A2 milk and caprine αs2-casein has been utilized to rescue CMPA patients and other potential disease problems. This knowledge has been genetically applied to milk production in cows or goats or even whole herds of the two species. This practice has happened in California and Ohio, as well as in New Zealand, where this A2 cow milk has been now advanced commercially. In the USA, there have been even promotions of bulls, whose daughters have been tested homozygous for the A2 β-casein protein.


PEDIATRICS ◽  
1964 ◽  
Vol 33 (2) ◽  
pp. 308-309
Author(s):  
ARMOND S. GOLDMAN ◽  
D. W. ANDERSON ◽  
S. R. HALPERN ◽  
W. A. SELLARS

In the study of oral challenge of allergic patients with milk, the inclusion of patients with milk sugar intolerance was minimized by using lactose-free purified milk proteins for confirmatory oral challenge tests. These purified milk proteins did contain sucrose, but the possibility of sucrose intolerance was excluded because the soybean milk used during the asymptomatic periods of milk elimination also contained sucrose. We agree with Dr. Ingall that in the absence of oral challenge with purified milk proteins, it is difficult to distinguish between milk protein hypersensitivity and lactose intolerance in those patients exhibiting solely gastrointestinal reactions when challenged with lactose-containing cow's milk.


1979 ◽  
Vol 46 (2) ◽  
pp. 187-191 ◽  
Author(s):  
Pierre Jollès

SUMMARYk-Casein is the main glycoprotein of cow's milk. Its polysaccharide part is O-glycosidically linked to threonine residue 133. It contains only 3 different sugars (Gal, GalNAc, NeuNAc), but a microheterogeneity has been detected at the sugar level. Two main polysaccharides have so far been characterized. The structure of the trisaccharide is NeuNAc α → 3 Gal β1 →3 GalNAc; the tetrasaccharide contains one additional sialic acid. The polysaccharide part of ovine k-casein resembles that of bovine k-casein, but contains also N-glycolyl neuraminic acid. Human k-casein contains 3 times more carbohydrate than bovine k-casein with 2 additional sugars, GlcNAc and Fuc. The various polysaccharide parts isolated from bovine colostrum k-caseinoglycopeptide are much more complex than those obtained from the normal glycopeptide, indicating an evolution of the sugar part as a function of time after parturition. Some aspects of the secondary structure of k-casein and the role of the sugar part are discussed. The carbohydrate moiety of another milk protein, human lactotransferrin, is also discussed briefly. It is comprised of 2 identical glycan groups, N-glycosidically linked to the protein, and quite different from the k-casein carbohydrate moiety.


Author(s):  
Oksana Matsyura ◽  
◽  
Lesya Besh ◽  
Natalia Lukyanenko ◽  
Oksana Kovalska ◽  
...  

Background. Cow's milk protein allergy is a topical issue in pediatrics. This disease affects 2-3% of young children. Methods. The study included 30 children with a confirmed cow’s milk protein allergy and a prescribed milk elimination diet. The children were observed for 36 months. The molecular profile was evaluated by detecting the major components of milk (Bos d 8, Bos d 5, Bos d 4), minor (Bos d 6), and cross-reactive with serum albumin (Fel d 2, Can f 3). Results. The study group included 46.7% of boys. The mean age of the subjects was 14.5±3.18 months. Nine of the 25 analyzed factors were identified in the course of our work by the method of logistic regression with progressive selection, which in combined action affect the formation of tolerance to cow's milk proteins in allergic children. There are three clinical examples of calculating the prediction of the complete tolerance development in the elimination diet in children with cow's milk protein allergy. Conclusions. Independent predictors that reduce the likelihood of the tolerance development in the elimination diet, have identified: skin test to milk, Bos d 8, Bos d 5, Bos d 4, Bos d 6. Independent predictors of the tolerance development in the elimination diet are: milk-specific IgE, total IgE, Fel d 2, Can f 3. Low probability of tolerance development by elimination therapy is a recommendation for prescribing treatment to a patient by specific oral tolerance induction.


1990 ◽  
Vol 29 (2) ◽  
pp. 122-128 ◽  
Author(s):  
C. Kaiser ◽  
H. Reibisch ◽  
R. Fölster-Holst ◽  
H. Sick

2019 ◽  
Vol 29 (2) ◽  
pp. 97
Author(s):  
Santiananda Arta Asmarasari ◽  
C Sumantri ◽  
A Gunawan ◽  
E Taufik ◽  
A Anggraeni

The objective of this paper is to explore some efforts to increase milk protein of dairy cows through a milk protein control gene selection approach. Improving the quality of cow's milk has shifted to increase milk protein levels, due to nutritional and economic interest. The breeding process in producing dairy cattle with the advantage of having high milk protein content is more effectively carried out by molecular biotechnology approaches. The content of cow's milk protein is controlled by cow's milk protein control genes. In the process to produce dairy cattle with the advantage of having high milk protein content, it can be done with a selection approach based on milk protein control genes, namely CSN1S1, CSN2, CSN1S2, and CSN3. Once known, the main controller gene that causes high levels of cow's milk protein, it will be easy to identify dairy cattle that have these advantages, so that the selection of dairy cattle can be done since at early age.


2020 ◽  
pp. 33-37
Author(s):  
A. A. Galimova ◽  
E. E. Emelyashenkov ◽  
S. G. Makarova ◽  
N. N. Murashkin ◽  
A. P. Fisenko ◽  
...  

Relevance. Dairy-free diet is the basis of cow’s milk allergy (CMA) patient’s management. Duration of the diet is individual, but some children don’t develop tolerance.The aim of the study was to investigate health and growth indices in children with CMA depending on tolerance development by the age of five. Materials and methods. 153 children from 1 to 18 months with diagnosed CMA were included in the prospective study (76.5% with IgE-mediated form). The tolerance was determined after 6–12 months of a milk-free diet and at the age of 5 using an open challenge test. Anthropometry indices (Anthro Plus), levels of specific IgE (Immuno CAP 250) and IgG4 (ELISA) to dietary proteins and the presence of allergic diseases in children also were assessed.Results. 50.3% of children developed tolerance to cow’s milk protein after 6–12 months of a milk-free diet. By the age of 5 63.3% of patients had complete tolerance of dairy products. Partially formed tolerance was observed in 22.9%. 13.8% of patients still had clinical reactions to cow’s milk proteins. Patients with persistent CMA typically had IgE-mediated form, lower growth indices and multiple allergic pathology.Conclusion. The consideration of tolerance development predictors can allow to personalize the management of CMA. Additional researches are needed to clarify the causes of growth indices decline in children with persistent CMA. 


2017 ◽  
pp. 150-155
Author(s):  
Thi Huyen Nguyen ◽  
Thi Minh Phuong Phan ◽  
Galleri Grazia

Background: Cow’s milk protein allergy (CMPA) is the most common food allergy, especially, in infants and young children. In this case, milk from other mammalian species has been suggested as a possible nutritional alternative to cow’s milk. Goat’s milk is used quite popular to replace for cow’s milk. In the goat species, αS1casein (αS1-CN), coded by the CSN1S1 gene, is characterized by qualitative and quantitative polymorphisms extensively. This aim of this study is to evaluate allergenicity of goat’s milk containing differentk kinds of αS1CN. Methods: Individual milk samples from 26 selected goats with different CSN1S1 genotypes were analyzed by SDS-PAGE and immunoblotting by using sera from children allergic to cow’s milk with IgE specific to CN and/or serum protein. Results: The absence of reactivity for the αs1-CN highlighted with immunoblotting for all goat milk samples. Conclusions: The goat’s milk with particular genotype for CSN1S1 could be used as a source protein alternative in the case of αs1-CN awareness. Furthermore, these tests could be useful for evaluating from time to time the reactivity of patients with CMPA against milk proteins of these goats selected to establish the safety of its use in the specific subject. Key words: Allergenicity, milk protein, goat, alphaS1-Casein, CSN1S1gene


Sign in / Sign up

Export Citation Format

Share Document