MATERIALS AND METHODS Products. Milk was collected from a single cow, homozygous for the four caseins (aSl-B, aa-A, &Al, KA), skimmed, lyophilized, and stored frozen (-20" C). It was reconstituted just before use with deionized... more
MATERIALS AND METHODS Products. Milk was collected from a single cow, homozygous for the four caseins (aSl-B, aa-A, &Al, KA), skimmed, lyophilized, and stored frozen (-20" C). It was reconstituted just before use with deionized water. Liquid rennet (520 mg of ...
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MATERIALS AND METHODS Diets. Three types of test meal were prepared from the same fresh bovine skim milk source:(1) raw milk,(2) pasteurized milk, and (3) yoghurt. To obtain diets 2 and 3, milk was heated to 95 OC during 45 s. For diet 3,... more
MATERIALS AND METHODS Diets. Three types of test meal were prepared from the same fresh bovine skim milk source:(1) raw milk,(2) pasteurized milk, and (3) yoghurt. To obtain diets 2 and 3, milk was heated to 95 OC during 45 s. For diet 3, the milk was then ...
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The in vivo action of gastric proteinases on bovine milk proteins was studied in rats fed with skim-milk, by analysing gastric contents after 30, 60 and 240 min of digestion. Gastric proteolysis was already marked after 30 min of... more
The in vivo action of gastric proteinases on bovine milk proteins was studied in rats fed with skim-milk, by analysing gastric contents after 30, 60 and 240 min of digestion. Gastric proteolysis was already marked after 30 min of digestion and liberated a large number of peptides with different molecular weights. alpha S1-Casein and beta-casein were still the main components of the stomach contents together with alpha-lactalbumin and beta-lactoglobulin, which were little degraded, even after 240 min of digestion. A statistical analysis (multivariate method), made on several parameters (such as pH, N, and NPN) showed changes in the stomach contents during the digestion. The amino acid composition of the protein fraction was close to that of the diet, whilst that of the non-protein fraction was very different, being between the amino acid composition of the endogenous proteins and that of the diet.
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Analysis of elution profiles of enzymatic and CNBr digests of kappa-caseins C and E, and sequencing of most relevant peptides allowed the chemical characterization of both genetic variants. They differ from their B and A allelic... more
Analysis of elution profiles of enzymatic and CNBr digests of kappa-caseins C and E, and sequencing of most relevant peptides allowed the chemical characterization of both genetic variants. They differ from their B and A allelic counterparts by a single substitution, His97/Arg and Gly155/Ser, respectively. Electrophoretic behaviour of the investigated C and E variants was in good agreement with the observed amino acid replacements.
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Research Interests: Dairy Science, Dairy Economics, Dairy Science and Technology, Dairy Nutrition, Advanced Dairy Farming Techniques, Constraints in Dairy Farming, and 27 moreProbiotics in Dairy Foods, Dairy Technology &Food Technology, Dairy Engineering, Dairy Microbiology, Milking Managment of Dairy Buffaloes, Dairy, Dairy Calves, Ruminant nutrition and Dairy science, Dairy Technology, Dairy cattle nutrition, Dairy Cattle Breeding, Peternakan, Dairy Cattle, Sosial Ekonomi Peternakan, Dairy Products, Ilmu Peternakan (S2), Dairy production, Milk and Dairy Chemistry, Dairy industry, Dairy Food Market, Dairy Economy, Laporan Ternak Perah, Dairy Development in Asia and Africa, Teknologi Peternakan, Fakultas Peternakan Dan Pertanian, Makalah Bangsa Ternak Perah, and Teknologi Dan Manajemen Peternakan
Abstract Text: A new genetic variant of ovine αS2-casein (named αs2-CN*H) was identified at the protein level and further characterized at the genome level. The molecular mass of the 12-phosphate αs2-CN*H isoform was measured as... more
Abstract Text: A new genetic variant of ovine αS2-casein (named αs2-CN*H) was identified at the protein level and further characterized at the genome level. The molecular mass of the 12-phosphate αs2-CN*H isoform was measured as 25,586.984 Da by electrospray ionization mass spectrometry (ESI-MS). Compared with variant A, two nucleotide substitutions were found in exon 11 (A65G) and exon 15 (G64A) leading to the amino acid substitutions: I105V and R161H, respectively. The comparative analysis of nucleotide sequences for alleles present in the Lacaune dairy breed suggests an evolutionary relatedness between CSN1S2*D and H allele. Hence, a possible phylogeny relationship is proposed for CSN1S2alleles in sheep. Keywords: ovine αs2-casein, genetic polymorphism, nucleotide sequence
The structural and quantitative variability of caprine alpha(s1)-casein induced by the extensive polymorphism recorded at the corresponding locus strongly influences the composition (proteins as well as lipids) and the technological... more
The structural and quantitative variability of caprine alpha(s1)-casein induced by the extensive polymorphism recorded at the corresponding locus strongly influences the composition (proteins as well as lipids) and the technological behaviour of milk. Immuno-histo-chemistry studies coupled with electron microscopy analysis have shown that a dysfunction exists in the intracellular transport of caseins when alpha(s1)-casein is lacking. Casein accumulation in the endoplasmic reticulum leads to a dilation of the cisternae that could disturb the whole secretion process (including lipids). Despite a long controversy, goat milk secretion is still considered to occur through an apocrine process contrary to the merocrine process described for cow's milk. We suggest that the apocrine pathway of secretion described in the goat could be the consequence of the dysfunction observed in the intracellular transport of caseins when alpha(s1)-casein is lacking. To obtain further clues in the favou...
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Research Interests: Mass Spectrometry, Proteomics, Biological Sciences, Humans, Sequence alignment, and 13 moreFemale, Animals, Peptides, Horses, Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis, Milk, High Pressure Liquid Chromatography, Goats, Cattle, Molecular weight, Two-Dimensional Gel Electrophoresis, Amino Acid Sequence, and Milk proteins
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From hydrolysis experiments carried out on alpha s1-caseins A and F at pH 5.2 in the presence of 30 g NaCl/l, i.e. the conditions encountered in many young goats' cheeses, it was found that minima of 19 and 9 bonds were sensitive... more
From hydrolysis experiments carried out on alpha s1-caseins A and F at pH 5.2 in the presence of 30 g NaCl/l, i.e. the conditions encountered in many young goats' cheeses, it was found that minima of 19 and 9 bonds were sensitive to chymosin in variants A and F respectively. Variant A was hydrolysed faster than variant F and the proteolytic pattern (reversed-phase HPLC and polyacrylamide agarose gel electrophoresis) differed between the variants. Hydrolysates from both variants had a number of cleavage sites in common (Leu20-Leu21, Phe23-Ala24 and Phe32-Arg33 in both variants, Leu101-Lys102 and Leu64-Lys65, Leu120-His121 and Leu83-His84, Leu142-Ala143 and Leu105-Ala106, Leu149-Phe150 and Leu112-Phe113, Leu156-Asp157 and Leu119-Asp120, Trp164-Tyr165 and Trp127-Tyr128 in variants A and F respectively), while other bonds were split only in variant A (Leu16-Asn17, Glu18-Asn19, Phe28-Pro29, Ile44-Gly45, Tyr80-Ile81, Gln82-Lys83, Tyr91-Leu92, Tyr94-Leu95, Leu109-Glu110 and Phe179-Ser180). Major cleavage sites appeared to be at Phe23-Val24, Leu142-Ala143 and Trp164-Tyr165 for variant A, and Phe23-Val24 and Leu64-Lys65 for variant F. Cleavage site Phe23-Val24 could be the origin of the first breakdown product from goat alpha s1-caseins A and F visible in polyacrylamide agarose gel electrophoresis.
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Research Interests: Bacteriology, Sensitivity Analysis, Time-of-flight mass spectrometry, Biological Sciences, Gram Positive, and 10 morePeptides, Structure Analysis, High Performance Liquid Chromatography, High Pressure Liquid Chromatography, Carboxypeptidases, Base Sequence, Cell Wall, Peptidoglycan, Life Span, and Lactococcus lactis
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Research Interests: Genetics, Genomics, Polymorphism, Molecular Evolution, Proteomics, and 22 moreBiological Sciences, Mice, Female, Animals, Protein structure, Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis, High Pressure Liquid Chromatography, Single Nucleotide Polymorphism, Model System, Quantitative Trait Loci, Two-Dimensional Gel Electrophoresis, Milk Protein Concentrate, Amino Acid Sequence, Base Sequence, Amino Acid Substitution Rates, Complex Traits, Two dimensional Gel Electrophoresis, Milk Protein, Mus Musculus, Nucleotides, Milk proteins, and Protein Splicing
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The PRM/Alf inbred mice exhibit a huge intestinal lengthening. Since milk contains bioactive factors implied in numerous biological processes, one hypothesis is that PRM/Alf milk contains intestinotrophic factors contributing to this... more
The PRM/Alf inbred mice exhibit a huge intestinal lengthening. Since milk contains bioactive factors implied in numerous biological processes, one hypothesis is that PRM/Alf milk contains intestinotrophic factors contributing to this remarkable phenotype. A comparison between the milk from PRM/Alf and C57BL/6J (as a control) strains could be helpful in the identification of such factors, including proteins. However, a complete description of the mouse milk major protein fraction is still missing. Hence we adapted a reliable technique to separate and identify the major mouse milk proteins. This approach was achieved through the protein study of milk from C57BL/6J and PWK/Pas strains representative of two Mus musculus subspecies, M. m. domesticus and M. m. musculus respectively. C57BL/6J milk samples were first skimmed and fractionated by reverse phase-HPLC (RP-HPLC). The protein content of each chromatographic peak was analysed by SDS-PAGE and identified by mass spectrometry. This me...