The total proteose-peptone fraction (TPP) is defined as a heat-stable soluble fraction of milk, representing about 10% of the whey protein. TPP is divided into two classes according to its origin. The first class consists of proteolysis fragments of the β-casein from the N-terminal region. These are non-hydrophobic fractions, which are the highly soluble β-CN-5P (f1-105/107); β-CN-4P (f1-28) and β-CN-1P (f29-105/107) respectively called PP5 (14.3 kDa), PP8S (9.9 kDa), and PP8F (4 kDa). The second class includes the hydrophobic fractions of glycoproteins, whose major constituents are a glycoprotein LP28, the highly hydrophobic glycoprotein LP18 and a hydrophobic peptide with apparent Mr, respectively 28 kDa, 18 kDa and 11 kDa. TPP has numero...
End of Project ReportMilk proteins can be hydrolysed (i.e. fragmented) using proteolytic enzymes to ...
Milk whey proteins carry out a number of important biological functions and also they are precursors...
The peptidic profile and the allergenicity of the peptides obtained from eight commercial hypoallerg...
The development of knowledge regarding the characteristics of the proteose peptone fraction of milk:...
The total proteose-peptone fractions are complex heterogeneous mixture of thermoresistant proteins o...
Les protéose-peptones préparées par thermo coagulation du lait sont séparées par fplc d'interactions...
Recovery of the proteose peptone component 3 from cheese whey was optimal using a 16% (w/w) Reppal P...
Since proteose-peptone is a mixture of heterogeneous proteins and peptides, its functional propertie...
Proteose-peptone is a heat-stable and acid-soluble protein fraction of milk that has important funct...
Extraction of proteose-peptones (PPs) was carried out from fresh milk, from milk after prolonged inc...
Proteose-peptone is a heat-stable and acid-soluble protein fraction of milk that has important funct...
An important source of bioactive peptides is hydrolyzed products based on milk whey: hypoallergenic ...
Surface properties of a nonhydrophobic fraction of proteose-peptone (NHFPP) and a hydrophobic fracti...
Total proteose-peptone (TPP) fractions were extracted from skimmed milk (UHT) and whey protein con...
Extraction of proteose\u2013peptones (PPs) was carried out from fresh milk, from milk after prolonge...
End of Project ReportMilk proteins can be hydrolysed (i.e. fragmented) using proteolytic enzymes to ...
Milk whey proteins carry out a number of important biological functions and also they are precursors...
The peptidic profile and the allergenicity of the peptides obtained from eight commercial hypoallerg...
The development of knowledge regarding the characteristics of the proteose peptone fraction of milk:...
The total proteose-peptone fractions are complex heterogeneous mixture of thermoresistant proteins o...
Les protéose-peptones préparées par thermo coagulation du lait sont séparées par fplc d'interactions...
Recovery of the proteose peptone component 3 from cheese whey was optimal using a 16% (w/w) Reppal P...
Since proteose-peptone is a mixture of heterogeneous proteins and peptides, its functional propertie...
Proteose-peptone is a heat-stable and acid-soluble protein fraction of milk that has important funct...
Extraction of proteose-peptones (PPs) was carried out from fresh milk, from milk after prolonged inc...
Proteose-peptone is a heat-stable and acid-soluble protein fraction of milk that has important funct...
An important source of bioactive peptides is hydrolyzed products based on milk whey: hypoallergenic ...
Surface properties of a nonhydrophobic fraction of proteose-peptone (NHFPP) and a hydrophobic fracti...
Total proteose-peptone (TPP) fractions were extracted from skimmed milk (UHT) and whey protein con...
Extraction of proteose\u2013peptones (PPs) was carried out from fresh milk, from milk after prolonge...
End of Project ReportMilk proteins can be hydrolysed (i.e. fragmented) using proteolytic enzymes to ...
Milk whey proteins carry out a number of important biological functions and also they are precursors...
The peptidic profile and the allergenicity of the peptides obtained from eight commercial hypoallerg...