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

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Standard

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

I: European Journal of Biochemistry, Bind 269, Nr. 5, 2002, s. 1362-1372.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Iametti, S, Rasmussen, P, Frøkiær, H, Ferranti, P, Addeo, F & Bonomi, F 2002, 'Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity', European Journal of Biochemistry, bind 269, nr. 5, s. 1362-1372. https://doi.org/10.1046/j.1432-1033.2002.02769.x

APA

Iametti, S., Rasmussen, P., Frøkiær, H., Ferranti, P., Addeo, F., & Bonomi, F. (2002). Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. European Journal of Biochemistry, 269(5), 1362-1372. https://doi.org/10.1046/j.1432-1033.2002.02769.x

Vancouver

Iametti S, Rasmussen P, Frøkiær H, Ferranti P, Addeo F, Bonomi F. Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. European Journal of Biochemistry. 2002;269(5):1362-1372. https://doi.org/10.1046/j.1432-1033.2002.02769.x

Author

Iametti, Stefania ; Rasmussen, Patrizia ; Frøkiær, Hanne ; Ferranti, Pasquale ; Addeo, Francesco ; Bonomi, Francesco. / Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. I: European Journal of Biochemistry. 2002 ; Bind 269, Nr. 5. s. 1362-1372.

Bibtex

@article{a24a1195f3714d338d70414774044eec,
title = "Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity",
abstract = "Bovine β-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 β-lactoglobulin undergoes significant but reversible structural changes. In the conditions used in the present study, β-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 β-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 βb-lactoglobulin hydrolysis were assessed by using various β-lactoglobulin-specific antibodies, and most epitopic sites were no longer present after attack of the partially unfolded protein by the two proteases.",
keywords = "Bovine β-lactoglobulin, Limited proteolysis, Partial unfolding, Reduced immunoreactivity, Thermal treatment",
author = "Stefania Iametti and Patrizia Rasmussen and Hanne Fr{\o}ki{\ae}r and Pasquale Ferranti and Francesco Addeo and Francesco Bonomi",
year = "2002",
doi = "10.1046/j.1432-1033.2002.02769.x",
language = "English",
volume = "269",
pages = "1362--1372",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Springer Verlag",
number = "5",

}

RIS

TY - JOUR

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

AU - Iametti, Stefania

AU - Rasmussen, Patrizia

AU - Frøkiær, Hanne

AU - Ferranti, Pasquale

AU - Addeo, Francesco

AU - Bonomi, Francesco

PY - 2002

Y1 - 2002

N2 - Bovine β-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 β-lactoglobulin undergoes significant but reversible structural changes. In the conditions used in the present study, β-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 β-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 βb-lactoglobulin hydrolysis were assessed by using various β-lactoglobulin-specific antibodies, and most epitopic sites were no longer present after attack of the partially unfolded protein by the two proteases.

AB - Bovine β-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 β-lactoglobulin undergoes significant but reversible structural changes. In the conditions used in the present study, β-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 β-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 βb-lactoglobulin hydrolysis were assessed by using various β-lactoglobulin-specific antibodies, and most epitopic sites were no longer present after attack of the partially unfolded protein by the two proteases.

KW - Bovine β-lactoglobulin

KW - Limited proteolysis

KW - Partial unfolding

KW - Reduced immunoreactivity

KW - Thermal treatment

UR - http://www.scopus.com/inward/record.url?scp=0036124772&partnerID=8YFLogxK

U2 - 10.1046/j.1432-1033.2002.02769.x

DO - 10.1046/j.1432-1033.2002.02769.x

M3 - Journal article

C2 - 11874450

AN - SCOPUS:0036124772

VL - 269

SP - 1362

EP - 1372

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 5

ER -

ID: 331794176