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Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. / Iametti, S.; Rasmussen, P.; Frøkiær, Hanne; Ferranti, P.; Addeo, F.; Bonomi, F.

In: European journal of biochemistry, Vol. 269, No. 5, 2002, p. 1362-1372.

Publication: Research - peer-reviewJournal article – Annual report year: 2002

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Iametti, S.; Rasmussen, P.; Frøkiær, Hanne; Ferranti, P.; Addeo, F.; Bonomi, F. / Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity.

In: European journal of biochemistry, Vol. 269, No. 5, 2002, p. 1362-1372.

Publication: Research - peer-reviewJournal article – Annual report year: 2002

Bibtex

@article{65b4a4b3fb974409bc2fb241b12fe478,
title = "Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity",
publisher = "Springer Verlag",
author = "S. Iametti and P. Rasmussen and Hanne Frøkiær and P. Ferranti and F. Addeo and F. Bonomi",
year = "2002",
volume = "269",
number = "5",
pages = "1362--1372",
journal = "European journal of biochemistry",
issn = "0014-2956",

}

RIS

TY - JOUR

T1 - Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity

A1 - Iametti,S.

A1 - Rasmussen,P.

A1 - Frøkiær,Hanne

A1 - Ferranti,P.

A1 - Addeo,F.

A1 - Bonomi,F.

AU - Iametti,S.

AU - Rasmussen,P.

AU - Frøkiær,Hanne

AU - Ferranti,P.

AU - Addeo,F.

AU - Bonomi,F.

PB - Springer Verlag

PY - 2002

Y1 - 2002

N2 - Bovine beta-lactoglobulin was hydrolyzed with trypsin or chymotrypsin in the course of heat treatment at 55, 60 and 65 C at neutral pH. At these temperatures beta-lactoglobulin undergoes significant but reversible structural changes. In the conditions used in the present study, beta-lactoglobulin was virtually insensitive to proteolysis by either enzyme at room temperature, but underwent extensive proteolysis when either protease was present during the heat treatment. High-temperature proteolysis occurs in a progressive manner. Mass spectrometry analysis of some large-sized breakdown intermediates formed in the early steps of hydrolysis indicated that both enzymes effectively hydrolyzed some regions of beta-lactoglobulin that were transiently exposed during the physical treatments and that were not accessible in the native protein. The immunochemical properties of the products of beta-lactoglobulin hydrolysis were assessed by using various beta-lactoglobulin-specific antibodies, and most epitopic sites were no longer present after attack of the partially unfolded protein by the two proteases.

AB - Bovine beta-lactoglobulin was hydrolyzed with trypsin or chymotrypsin in the course of heat treatment at 55, 60 and 65 C at neutral pH. At these temperatures beta-lactoglobulin undergoes significant but reversible structural changes. In the conditions used in the present study, beta-lactoglobulin was virtually insensitive to proteolysis by either enzyme at room temperature, but underwent extensive proteolysis when either protease was present during the heat treatment. High-temperature proteolysis occurs in a progressive manner. Mass spectrometry analysis of some large-sized breakdown intermediates formed in the early steps of hydrolysis indicated that both enzymes effectively hydrolyzed some regions of beta-lactoglobulin that were transiently exposed during the physical treatments and that were not accessible in the native protein. The immunochemical properties of the products of beta-lactoglobulin hydrolysis were assessed by using various beta-lactoglobulin-specific antibodies, and most epitopic sites were no longer present after attack of the partially unfolded protein by the two proteases.

JO - European journal of biochemistry

JF - European journal of biochemistry

SN - 0014-2956

IS - 5

VL - 269

SP - 1362

EP - 1372

ER -