Influence of Calcium on Milk Protein Aggregation and Binding Dynamics Between Binder of Sperm (BSP) Proteins and Milk Proteins.

2012 ◽  
Vol 87 (Suppl_1) ◽  
pp. 557-557
Author(s):  
Erika Bezerra de Menezes ◽  
Marie-France Lusignan ◽  
Arlindo Moura ◽  
Puttaswamy Manjunath
Keyword(s):  
Protein Aggregation ◽  
Milk Protein ◽  
Milk Proteins ◽  
Bsp Proteins

scholarly journals Development of Immunohistochemical Methods for Casein Detection in Meat Products

Foods ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 28
Author(s):  
Ludmila Kalčáková ◽  
Matej Pospiech ◽  
Bohuslava Tremlová ◽  
Zdeňka Javůrková ◽  
Irina Chernukha
Keyword(s):  
Milk Protein ◽  
Production Efficiency ◽  
Raw Materials ◽  
Meat Products ◽  
Milk Proteins ◽  
Increase Production Efficiency ◽  
Allergenic Potential ◽  
Significant Difference ◽  
Dairy Ingredients ◽  
Immunohistochemical Methods

To increase production efficiency of meat products, milk protein additives are often used. Despite a number of advantages, use of dairy ingredients involves a certain risk, namely the allergenic potential of milk proteins. A number of methods have been developed to detect milk-origin raw materials in foodstuffs, including immunological reference methods. This study presents newly developed immunohistochemical (IHC) methods for casein detection in meat products. Casein was successfully detected directly in meat products where sensitivity was determined at 1.21 and specificity at 0.28. The results obtained from the IHC were compared with the Enzyme-Linked Immuno Sorbent Assay (ELISA) and there was no statistically significant difference between the IHC and ELISA methods (p > 0.05). The correspondence between the methods was 72% in total. The highest correspondence was reached in frankfurters (90%), the lowest in canned pâté (44%).

Letters to the Editor

PEDIATRICS ◽  
1964 ◽  
Vol 33 (2) ◽  
pp. 308-309
Author(s):  
ARMOND S. GOLDMAN ◽  
D. W. ANDERSON ◽  
S. R. HALPERN ◽  
W. A. SELLARS
Keyword(s):  
Milk Protein ◽  
Lactose Intolerance ◽  
Milk Proteins ◽  
Oral Challenge ◽  
Cow’S Milk ◽  
Letters To The Editor ◽  
Soybean Milk ◽  
Cow's Milk ◽  
Milk Sugar ◽  
Challenge Tests

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.

Attachment of Listeria innocua to Polystyrene: Effects of Ionic Strength and Conditioning Films from Culture Media and Milk Proteins

2014 ◽  
Vol 77 (3) ◽  
pp. 427-434 ◽  
Author(s):  
GILLES ROBITAILLE ◽  
SÉBASTIEN CHOINIÈRE ◽  
TIMOTHY ELLS ◽  
LOUISE DESCHÈNES ◽  
AKIER ASSANTA MAFU
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bacterial Adhesion ◽  
Bovine Serum ◽  
Biofilm Formation ◽  
Milk Protein ◽  
Milk Proteins ◽  
Listeria Innocua ◽  
Conditioning Films ◽  
Β Lactoglobulin

It is recognized that bacterial adhesion usually occurs on conditioning films made of organic macromolecules absorbed to abiotic surfaces. The objectives of this study were to determine the extent to which milk protein–coated polystyrene (PS) pegs interfere with biofilm formation and the synergistic effect of this conditioning and hypertonic growth media on the bacterial adhesion and biofilm formation of Listeria innocua, used as a nonpathogenic surrogate for Listeria monocytogenes. PS pegs were uncoated (bare PS) or individually coated with whey proteins isolate (WPI), β-lactoglobulin, bovine serum albumin, or tryptic soy broth (TSB) and were incubated in bacterial suspensions in modified Welshimer's broth. After 4 h, the number of adherent cells was dependent on the coating, as follows: TSB (107 CFU/ml) > bare PS > β-lactoglobulin > bovine serum albumin ≈ WPI (104 CFU/ml). The sessile cell counts increased up to 24 h, reaching >107 CFU per peg for all surfaces (P > 0.1), except for WPI-coated PS; this indicates that the inhibitory effects of milk protein conditioning films are transient, slowing down the adhesion process. The 4-h bacterial adhesion on milk protein–coated PS in modified Welshimer's broth supplemented with salt (0 to 10% [wt/vol]) did not vary (P > 0.1), indicating that conditioning with milk proteins was the major determinant for inhibition of bacterial adhesion and that the synergetic effect of salt and milk proteins on adhesion was minimal. Moreover, the presence of 5 to 10% salt significantly inhibited 24-h biofilm formation on the TSB-coated and bare PS, with a decrease of >3 log at 10% (wt/vol) NaCl and almost completely depleted viable sessile bacteria on the milk protein–coated PS.

scholarly journals Relative distribution of post-nuclear poly(A)-containing RNA abundance groups within the nuclear and post-nuclear polyadenylated and non-polyadenylated RNA populations of the lactating guinea-pig mammary gland

1980 ◽  
Vol 192 (2) ◽  
pp. 489-498 ◽  
Author(s):  
Ian C. Bathurst ◽  
Roger K. Craig ◽  
David G. Herries ◽  
Peter N. Campbell
Keyword(s):  
Mammary Gland ◽  
Guinea Pig ◽  
Milk Protein ◽  
Regulation Of Gene Expression ◽  
Milk Proteins ◽  
Relative Distribution ◽  
Free System ◽  
Low Salt ◽  
Nuclear Rna ◽  
System 2

1. RNA isolated from the post-nuclear supernatant of the lactating guinea-pig mammary gland was fractionated with oligo(dT)–cellulose into three populations; those that bound at ‘low salt’ [long poly(A) tracts, 78–32 nucleotides]; those that bound at ‘high salt’ [shorter poly(A) tracts, 48–21 nucleotides]; and those that did not bind [no poly(A) or short poly(A) tracts, <20 nucleotides]. Nuclear RNA was fractionated into two populations, those that bound in ‘low salt’ and those that did not bind. All the post-nuclear RNA fractions directed the synthesis of milk proteins in a Krebs II ascites cell-free system. 2. 3H-labelled DNA complementary to the post-nuclear poly-(A)-containing RNA population (low-salt fraction) was fractionated into abundant (milk-protein mRNA), moderately abundant and scarce sequences. This complementary DNA was then used to investigate the distribution of the mRNA sequences in the different RNA populations. This showed that all sequences were present in polyadenylated and non-polyadenylated fractions, but that major quantitative differences were apparent. The abundant milk-protein mRNA sequences predominated in the ‘low-salt’ post-nuclear poly(A)-containing RNA fraction, whereas the moderately abundant sequences predominated in the non-polyadenylated post-nuclear RNA fraction. In total cellular RNA, those sequences deemed initially to be moderately abundant within the ‘low-salt’ poly(A)-containing RNA population were present at a concentration very similar to those of the abundant milk-protein mRNA (approx. 6×105 copies of each sequence/cell). Similarly, analysis of the nuclear RNA populations showed that the ‘abundant’ and so-called ‘moderately abundant’ sequences were present in essentially identical concentrations (2×103 copies of each sequence/cell). The majority of these (90–95%) were non-polyadenylated. 3. The results are discussed in terms of the post-transcriptional mechanisms involved in the regulation of gene expression in the lactating guinea-pig mammary gland.

Antibody response to milk proteins in patients with milk-protein intolerance documented by challenge

1990 ◽  
Vol 85 (5) ◽  
pp. 921-927 ◽  
Author(s):  
A.W. Burks ◽  
L.W. Williams ◽  
H.B. Casteel ◽  
S.C. Fiedorek ◽  
C.A. Connaughton
Keyword(s):  
Antibody Response ◽  
Milk Protein ◽  
Milk Proteins ◽  
Protein Intolerance

Dietary treatment of cows' milk protein allergy in childhood: a commentary by the Committee on Nutrition of the French Society of Paediatrics

2011 ◽  
Vol 107 (3) ◽  
pp. 325-338 ◽  
Author(s):  
C. Dupont ◽  
J. P. Chouraqui ◽  
D. de Boissieu ◽  
A. Bocquet ◽  
J. L. Bresson ◽  
...  
Keyword(s):  
Milk Protein ◽  
Milk Proteins ◽  
Food Challenge ◽  
Dietary Treatment ◽  
Elimination Diet ◽  
Soya Protein ◽  
French Society ◽  
Suitable Alternative ◽  
Breast Feed ◽  
First Choice

The diagnosis of cows' milk protein allergy (CMPA) requires first the suspicion of diagnosis based on symptoms described in the medical history, and, second, the elimination of cows' milk proteins (CMP) from the infant's diet. Without such rigorous analysis, the elimination of CMP is unjustified, and sometimes harmful. The elimination diet should be strictly followed, at least until 9–12 months of age. If the child is not breast fed or the mother cannot or no longer wishes to breast feed, the first choice is an extensively hydrolysed formula (eHF) of CMP, the efficacy of which has been demonstrated by scientifically sound studies. If it is not tolerated, an amino acid-based formula is warranted. A rice protein-based eHF can be an alternative to a CMP-based eHF. Soya protein-based infant formulae are also a suitable alternative for infants >6 months, after establishing tolerance to soya protein by clinical challenge. CMPA usually resolves during the first 2–3 years. However, the age of recovery varies depending on the child and the type of CMPA, especially whether it is IgE-mediated or not, with the former being more persistent. Once the child reaches the age of 9–12 months, an oral food challenge is carried out in the hospital ward to assess the development of tolerance and, if possible, to allow for the continued reintroduction of CMP at home. Some children with CMPA will tolerate only a limited daily amount of CMP. The current therapeutic options are designed to accelerate the acquisition of tolerance thereof, which seems to be facilitated by repeated exposure to CMP.

scholarly journals Interaction of milk proteins and Binder of Sperm (BSP) proteins from boar, stallion and ram semen

2015 ◽  
Vol 13 (1) ◽  
Author(s):  
Geneviève Plante ◽  
Marie-France Lusignan ◽  
Michel Lafleur ◽  
Puttaswamy Manjunath
Keyword(s):  
Milk Proteins ◽  
Bsp Proteins

Utilization of milk proteins as starting materials for other foodstuffs

1979 ◽  
Vol 46 (2) ◽  
pp. 369-376 ◽  
Author(s):  
Charles V. Morr
Keyword(s):  
Functional Properties ◽  
Food Processing ◽  
Milk Protein ◽  
Milk Proteins ◽  
Food Processing Industry ◽  
Processing Industry ◽  
Whey Protein Concentrates ◽  
Wide Range ◽  
Utilization Of Protein ◽  
The Subject

SUMMARYThe modern food-processing industry is placing more and more emphasis upon the utilization of protein ingredients to provide specific functional properties to a wide range of formulated foods. Isolated milk protein products represent an important and valuable source of protein ingredients due to their recognized superior nutritional, organoleptic and functional properties. This paper provides up-to-date information on the quantities, production processes, composition, general properties, and specific functional properties of the major milk protein products, e.g. caseinates, co-precipitates, lactalbumin, whey protein concentrates and milk blends. The subject of chemical and enzymic modification to improve certain functional properties of milk proteins is considered briefly.

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