Detection of advanced glycation end-products (AGEs) during dry-state storage of ß-lactoglobulin/lactose

Sisse Jongberg; Michael Rasmussen; Leif Horsfelt Skibsted; Karsten Olsen

doi:10.1071/ch12442

Detection of advanced glycation end-products (AGEs) during dry-state storage of ß-lactoglobulin/lactose

Sisse Jongberg, Michael Rasmussen, Leif Horsfelt Skibsted, Karsten Olsen

LUKKET: Institut for Immunologi og Mikrobiologi

10 Citationer (Scopus)

Abstract

Glycation of whey proteins is primarily affected by temperature, water activity, and pH, and leads to changes of the functional and nutritional properties of the proteins. In the case of prolonged storage of mixtures of lactose and -lactoglobulin as a model for dried dairy products under mild heat treatment (60-70°C) in a restricted water environment (a_w 0.64) at pH 7, N^ε-(carboxymethyl)lysine (CML) and furosine were formed concomitant with glycation of β-lactoglobulin. Indirect ELISA using polyclonal antibodies against advanced glycation end products (AGEs) was shown to correlate with analyses of CML using HPLC and may be used for quality control of dried dairy products. The glycation changed the solubility properties of the protein by forming polymeric carbohydrate products of β-lactoglobulin and AGEs as characterised by SDS-PAGE.

Originalsprog	Engelsk
Tidsskrift	Australian Journal of Chemistry
Vol/bind	65
Udgave nummer	12
Sider (fra-til)	1620-1624
Antal sider	5
ISSN	0004-9425
DOI	https://doi.org/10.1071/ch12442
Status	Udgivet - 2012

Adgang til dokumentet

10.1071/ch12442

Citationsformater

@article{b8f9983995fd4acdbf3574b6c228b2bf,

title = "Detection of advanced glycation end-products (AGEs) during dry-state storage of {\ss}-lactoglobulin/lactose",

abstract = "Glycation of whey proteins is primarily affected by temperature, water activity, and pH, and leads to changes of the functional and nutritional properties of the proteins. In the case of prolonged storage of mixtures of lactose and -lactoglobulin as a model for dried dairy products under mild heat treatment (60-70°C) in a restricted water environment (aw 0.64) at pH 7, Nε-(carboxymethyl)lysine (CML) and furosine were formed concomitant with glycation of β-lactoglobulin. Indirect ELISA using polyclonal antibodies against advanced glycation end products (AGEs) was shown to correlate with analyses of CML using HPLC and may be used for quality control of dried dairy products. The glycation changed the solubility properties of the protein by forming polymeric carbohydrate products of β-lactoglobulin and AGEs as characterised by SDS-PAGE.",

author = "Sisse Jongberg and Michael Rasmussen and Skibsted, {Leif Horsfelt} and Karsten Olsen",

year = "2012",

doi = "10.1071/ch12442",

language = "English",

volume = "65",

pages = "1620--1624",

journal = "Australian Journal of Chemistry",

issn = "0004-9425",

publisher = "C S I R O Publishing",

number = "12",

}

TY - JOUR

T1 - Detection of advanced glycation end-products (AGEs) during dry-state storage of ß-lactoglobulin/lactose

AU - Jongberg, Sisse

AU - Rasmussen, Michael

AU - Skibsted, Leif Horsfelt

AU - Olsen, Karsten

PY - 2012

Y1 - 2012

N2 - Glycation of whey proteins is primarily affected by temperature, water activity, and pH, and leads to changes of the functional and nutritional properties of the proteins. In the case of prolonged storage of mixtures of lactose and -lactoglobulin as a model for dried dairy products under mild heat treatment (60-70°C) in a restricted water environment (aw 0.64) at pH 7, Nε-(carboxymethyl)lysine (CML) and furosine were formed concomitant with glycation of β-lactoglobulin. Indirect ELISA using polyclonal antibodies against advanced glycation end products (AGEs) was shown to correlate with analyses of CML using HPLC and may be used for quality control of dried dairy products. The glycation changed the solubility properties of the protein by forming polymeric carbohydrate products of β-lactoglobulin and AGEs as characterised by SDS-PAGE.

AB - Glycation of whey proteins is primarily affected by temperature, water activity, and pH, and leads to changes of the functional and nutritional properties of the proteins. In the case of prolonged storage of mixtures of lactose and -lactoglobulin as a model for dried dairy products under mild heat treatment (60-70°C) in a restricted water environment (aw 0.64) at pH 7, Nε-(carboxymethyl)lysine (CML) and furosine were formed concomitant with glycation of β-lactoglobulin. Indirect ELISA using polyclonal antibodies against advanced glycation end products (AGEs) was shown to correlate with analyses of CML using HPLC and may be used for quality control of dried dairy products. The glycation changed the solubility properties of the protein by forming polymeric carbohydrate products of β-lactoglobulin and AGEs as characterised by SDS-PAGE.

U2 - 10.1071/ch12442

DO - 10.1071/ch12442

M3 - Journal article

SN - 0004-9425

VL - 65

SP - 1620

EP - 1624

JO - Australian Journal of Chemistry

JF - Australian Journal of Chemistry

IS - 12

ER -

Detection of advanced glycation end-products (AGEs) during dry-state storage of ß-lactoglobulin/lactose

Abstract

Adgang til dokumentet

Fingeraftryk

Citationsformater