The development of knowledge regarding the characteristics of the proteose peptone fraction of milk: Techno-functional and biological properties. A review
[en] 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 numerous interesting characteristics such as techno-functional properties (emulsifying and foaming actions) and biological properties (lipolysis inhibition and antimicrobial activities), making TPP usable as a potential functional ingredient for industry. In addition, these functional properties are partly governed by the major components including glycoproteins, such as LP28, due to their hydrophobic nature.
Blecker, Christophe ; Université de Liège - ULiège > Chimie et bio-industries > Science des alim. et formul.
Language :
English
Title :
The development of knowledge regarding the characteristics of the proteose peptone fraction of milk: Techno-functional and biological properties. A review
Alternative titles :
[fr] Évolution des connaissances sur les fonctionnalités de la fraction protéose-peptone du lait: Propriétés techno-fonctionnelles et biologiques (synthèse bibliographique)
Publication date :
2013
Journal title :
Biotechnologie, Agronomie, Société et Environnement
ISSN :
1370-6233
eISSN :
1780-4507
Publisher :
Presses Agronomiques de Gembloux, Gembloux, Belgium
Andrews A.T. & Alichanidis E., 1983. Proteolysis of caseins and the proteose-peptone fraction of bovine milk. J. Dairy Res., 50, 275-290.
Andrews A.T. et al., 2006. β-CN-5P and β-CN-4P component of bovine milk proteose-peptone: large preparation and influence on the growth of cariogenic microorganisms. Food Chem., 96, 234-241.
Aschaffenburg R., 1946. Surface activity and proteins of milk. J. Dairy Res., 50, 316-329.
Campagna S. et al., 1998. Conformational studies of a synthetic peptide from the putative lipid-binding domain of bovine milk component PP3. J. Dairy Sci., 81, 3139-3148.
Campagna S. et al., 2004. Antibacterial activity of lactophoricin, a synthetic 23-residues peptide derived from the sequence of bovine milk component-3 of proteose-peptone. J. Dairy Sci., 87, 1621-1626.
Corradini C. & Innocente N., 1994. Influenza della frazione dei proteoso-peptoni sulla formazione della schiuma del latte. Sci. Tecn. Lattiero-Casearia, 45(2), 107-113.
Courthaudon J.L. et al., 1995. Surface activity and competitive adsorption of milk component 3 and porcine pancreatic lipase at the dodecane-water interface. In: Dickinson E. & Lorient D., eds. Food macromolecules and colloid. Cambridge, UK: Royal Society of Chemistry, 58-70.
Danthine S., Blecker C. & Deroanne C., 2004. Lipolysis inhibition by proteose-peptone: an interfacial study. In: Proceedings of the Be PCIS seminar: Surfactants self assembly and surfactant at interfaces, 11 February 2004, Gembloux, Belgium.
Egito A.S. et al., 2002. Separation and characterization of mare's milk αs1-, β-,-caseins, γ-casein-like, and proteose-peptone component 5-like peptides. J. Dairy Sci., 85, 697-706.
Eigel W.N. & Keeman T.W., 1979. Identification of proteose-peptone component 8-slow as a plasmin-derived fragment of bovine β-casein. Int. J. Biochem., 10, 529-535.
Eigel W.N. et al., 1984. Nomenclature of proteins of cow's milk: fifth revision. J. Dairy Sci., 67, 1599-1631.
Etienne L., Girardet J.M. & Linden G., 1994. Growth promotion of Bifidobacterium animalis by bovine milk proteose-peptone. Lait, 74, 313-323.
Girardet J.M., 1992. Le composant PP3 des protéose-peptones du lait bovin: obtention, origine, étude de sa partie glycannique, rôle dans la lipolyse. Thèse de doctorat: Université de Nancy I (France).
Girardet J.M. et al., 1993. Study of mechanism of lipolysis inhibition by bovine milk proteose-peptone component 3. J. Dairy Sci., 76, 2156-2163.
Girardet J.M. et al., 1995. Structure of glycoproteins isolated from bovine milk component PP3. Eur. J. Biochem., 234, 939-946.
Girardet J.M. & Linden G., 1996. PP3 component of bovine milk: a phosphorylated whey glycoprotein. J. Dairy Res., 63, 333-350.
Grenby T.H., Andrews A.T., Mistry M. & Williams R.J.H., 2001. Dental caries-protective agents in milk and milk products: investigations in vitro. J. Dent., 29, 83-92.
Inagaki M. et al., 2010a. The multiplicity of n-glycan structures of bovine milk 18 k Da lactophorin (milk gly CAM-1). Biosci. Biotechnol. Biochem., 74(2), 447-450.
Inagaki M. et al., 2010b. The bovine lactophorin C-terminale fragment and PAS6/7 were both potent in the inhibition of human rotavirus replication in cultured epithelial cells and the prevention of experimental gastroenteritis. Biosci. Biotechnol. Biochem., 74(7), 1386-1390.
Innocente N., Corradini C., Blecker C. & Paquot M., 1998a. Dynamic surface properties of proteose-peptone fraction of bovine milk. J. Dairy Sci., 81, 1833-1839.
Innocente N., Corradini C., Blecker C. & Paquot M., 1998b. Emulsifying properties of the total fraction and hydrophobic fraction of bovine milk proteose-peptone. Int. Dairy J., 8, 981-985.
Innocente N., Comparin C. & Corradini C., 2002. Proteose-peptone whey fraction as emulsifier in ice-cream preparation. Int. Dairy J., 12, 69-74.
Innocente N., Biasutti M. & Blecker C., 2011a. HPLC profile and dynamic properties of the proteose-peptone fraction from bovine milk and whey protein concentrate. Int. Dairy J., 21, 222-228.
Innocente N., Marchesini G. & Biasutti M., 2011b. Feasibility of the SPME method for the determination of the aroma retention. Food Chem., 124, 1249-1257.
Johnsen L.B., Sørensen E.S., Petersen T.E. & Berglund L., 1995. Characterization of a bovine mammary gland PP3 cDNA reveals homology with mouse and rat adhesion molecule Gly CAM-1. Biochim. Biophys. Acta, 1620, 171-182.
Jouenne E. & Crouzet J., 2000. Effect of pH on retention of aroma compounds by β-lactoglobulin. J. Agric. Food. Chem., 48, 1273-1277.
Kanno C., 1989. Purification and separation of multiple forms of lactophorin from bovine milk whey and their immunological and electrophoresis properties. J. Dairy Sci., 79, 883-891.
Larsen B.L., Wedholm-Pallas A., Lindmark-Mansson H. & Andren A., 2010. Different proteomic profiles of sweet whey and rennet casein obtained after preparation from raw versus heat-treated skimmed milk. Dairy Sci. Techn., 90, 641-656.
Mati A., Girardet J.M., Xenakis D. & Linden G., 1991. Isolement et caractérisation de la fraction hydrophobe des protéose-peptones des laits bovin, ovin et caprin. Lait, 71, 259-273.
Meisel H., 2004. Multifunctional peptides encrypted in milk proteins. Bio Factors, 21, 55-61.
Merin U., Fleminger G. & Komanovsky J., 2008. Subclinical udder infection with Streptococcus dysgalactiae impairs milk coagulation proprerties: the emerging role of proteose-peptone. Dairy Sci. Techn., 88, 407-419.
Nejjar J., Pâquet D. & Linden G., 1990. The PP3 component of the proteose-peptone. Extraction from unheated skim milk. Milchwissenschaft, 45, 84-87.
Osborne T.B. & Wakeman A.J., 1918. The protein of cow's milk. J. Biol. Chem., 33, 7-17.
Pâquet D., 1989. Revue bibliographique: la fraction protéose-peptone du lait. Lait, 69, 1-21.
Pâquet D., Nejjar Y. & Linden G., 1988. Study of a hydrophobic protein fraction isolated from milk proteose-peptone. J. Dairy Sci., 71, 1464-1471.
Park T.J., Kim J.S., Choi S.S. & Kim Y., 2009. Cloning, expression, isotope labeling, purification, and characterization of bovine antimicrobial peptide, lactophoricin in Escherichia coli. Protein Expression Purif., 65(1), 23-29.
Pearce K.N. & Kinsella J.E., 1978. Emulsifying properties of proteins: evaluation of turbidimetric technique. J. Agric. Food Chem., 26, 716-723.
Pedersen L.R.L. et al., 2012. PP3 forms stable tetrameric structures through hydrophobic interactions via the C-terminal amphipathic helix and undergoes reversible thermal dissociation and denaturation. FEBS J., 279, 336-347.
Rowland S.J., 1938. The precipitation of the proteins in milk. I. Casein. II. Total proteins. III. Globulin. IV. Albumin and Proteose-peptone. J. Dairy Res., 9, 30-41.
Sheng-Hua H. et al., 2012. Effects of proteose-peptone fractions from yak milk on lipoprotein lipase lipolysis. Int. J. Dairy Technol., 65(1), 32-37.
Shimizu M., Yamauchi K. & Saito M., 1989. Emulsifying properties of the proteose-peptone fraction obtained from bovine milk. Milchwissenschaft, 44(8), 497-500.
Sørensen E.S. & Petersen T.E., 1993. Purification and characterization of three proteins isolated from the proteose-peptone fraction of bovine milk. J. Dairy Res., 60, 189-192.
Sørensen E.S., Rasmussen L.K., Moller L. & Petersen T.E., 1997. The localization and multimeric nature of component PP3 in bovine milk: purification and characterization of PP3 from caprine and ovine milks. J. Dairy Sci., 80, 3176-3181.
Swaisgood H.E., 1993. Symposium: genetic perspectives on milk protein: comparative studies and nommenclature. J. Dairy Sci., 76(10), 3054-3061.
Tornberg E., 1978. The application of the drop volume technique to measurements of the adsorption of proteins at interfaces. J. Colloid Interface Sci., 64(3), 391-402.
Vanderghem C., Danthine S., Blecker C. & Deroanne C., 2007. Effect of proteose-peptone addition on some physcio-chemical characteristics of recombined dairy creams. Int. Dairy J., 17, 889-895.
Weinstein B.R., Duncan C.W. & Trout G.M., 1951a. The solar activated flavor of homogenized milk. IV. Isolation and characterization of a whey constituent capable of producing the solar-activated flavour. J. Dairy Sci., 34, 570-576.
Zhu H. & Damodaran S., 1994. Proteose-peptone and physical factors affect foaming properties of whey protein isolate. J. Food Sci., 59(3), 554-560.
Similar publications
Sorry the service is unavailable at the moment. Please try again later.
This website uses cookies to improve user experience. Read more
Save & Close
Accept all
Decline all
Show detailsHide details
Cookie declaration
About cookies
Strictly necessary
Performance
Strictly necessary cookies allow core website functionality such as user login and account management. The website cannot be used properly without strictly necessary cookies.
This cookie is used by Cookie-Script.com service to remember visitor cookie consent preferences. It is necessary for Cookie-Script.com cookie banner to work properly.
Performance cookies are used to see how visitors use the website, eg. analytics cookies. Those cookies cannot be used to directly identify a certain visitor.
Used to store the attribution information, the referrer initially used to visit the website
Cookies are small text files that are placed on your computer by websites that you visit. Websites use cookies to help users navigate efficiently and perform certain functions. Cookies that are required for the website to operate properly are allowed to be set without your permission. All other cookies need to be approved before they can be set in the browser.
You can change your consent to cookie usage at any time on our Privacy Policy page.