Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

Effect of genetic variation on the tryptic hydrolysis of bovine beta-lactoglobulin A, B, and C

Författare

  • L K Creamer
  • H C Nilsson
  • Marie Paulsson
  • C J Coker
  • J P Hill
  • R Jimenez-Flores

Summary, in English

The structure, stability, and hydrolysis characteristics of beta-lactoglobulin (LG) A are different from those of either beta-LG B or beta-LG C. Purified samples of these proteins were hydrolyzed with trypsin and the rates of loss of native monomeric beta-LG structure were measured using sodium dodecyl sulfate PAGE. At the same time, the appearance of many individual peptides were identified and followed in time by HPLC, measuring their concentration as a function of solution pH, temperature, protein concentration, and added urea or palmitate. The identity of the peptides was confirmed by liquid chromatography-mass spectrometry. This semiquantitative exploration showed that the rate of hydrolysis was in the order beta-LG A > beta-LG B > beta-LG C under most circumstances, and that 12 of the 18 trypsin-susceptible bonds were cleaved at very similar rates that were governed by the variant type. Consequently, the rate of hydrolysis of the intact protein was related to the overall structural stability of the individual proteins and the accessibility of certain peptide bonds to the enzyme. The hydrolysis of mixtures of 2 or more variants or of denatured beta-LG gave more heterogeneous peptide mixtures.

Avdelning/ar

  • Department of Food Technology, Engineering and Nutrition

Publiceringsår

2004

Språk

Engelska

Sidor

4023-4032

Publikation/Tidskrift/Serie

Journal of Dairy Science

Volym

87

Issue

12

Dokumenttyp

Artikel i tidskrift

Förlag

American Dairy Science Association

Ämne

  • Food Engineering

Nyckelord

  • ß-lactoglobulin
  • tryptic hydrolysis
  • genetic variant
  • kinetics

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1525-3198