Home |  English version |  Mappa |  Commenti |  Sondaggio |  Staff |  Contattaci Cerca nel sito  
Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2005

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Caseinomacropeptide self-association is dependent on whether the peptide is free or restricted in kappa-casein.

Anno di pubblicazione: 2005

Autori: Mikkelsen TL, Frokiaer H, Topp C, Bonomi F, Iametti S, Picariello G, Ferranti P, Barkholt V.

Autori CNR:

  • PASQUALE FERRANTI

Abstract: There is a general agreement that the experimentally determined molecular weight (MW) of caseinomacropeptide (CMP) is greater than the theoretical MW. Some studies suggest that this is due to a pH-dependent aggregation of monomeric CMP. How this aggregation is influenced by pH is not understood. This study was carried out to study the nature of CMP aggregates and to clarify which conditions affect aggregation of CMP. The apparent MW of CMP at different pH values was determined using size-exclusion chromatography. Caseinomacropeptide was further characterized by immunochemical analysis, sodium dodecyl sulfate-PAGE, N-terminal sequencing, and mass spectrometry. The hydrophobicity of CMP was studied by means of 1-anilino-naphthalene-8-sulfonic acid binding experiments. Four CMP products prepared by different methods were studied: CMP produced by enzymatic (chymosin or pepsin) hydrolysis of kappa-casein (CN), and 2 commercial CMP products. Both commercial products and CMP resulting from chymosin-hydrolysis of kappa-CN (at pH 6.6) had elution volumes with a MW corresponding to 35 kDA at pH 8.0 and 3.4. Caseinomacropeptide prepared from pepsin-hydrolysis of kappa-CN (at pH 2.5) eluted as multiple peaks with apparent MW of 35, 18, and 9 kDa, again independently of pH. Hydrolysis of kappa-CN with chymosin or pepsin at different pH values (pH 2.5, 3.4, and 6.6) produced differently sized aggregates of CMP, largely depending on the pH of the hydrolysis. These results indicate that, whereas CMP molecules are irreversibly associated, CMP in kappa-CN may associate reversibly in a pH-dependent manner. We suggest that interactions between para-kappa-CN parts of the kappa-CN molecules may be a requisite for the pH-dependent dissociation/association.

Pagine da: 4228

Pagine a: 4238

Rivista:

Journal of dairy science s. n.]
Paese di pubblicazione: Stati Uniti d'America
Lingua: inglese
ISSN: 0022-0302

Numero volume: 88

Altre informazioni: 2

Strutture CNR:

Moduli:

 
Torna indietro Richiedi modifiche Invia per email Stampa
Home Il CNR  |  I servizi News |   Eventi | Istituti |  Focus