NDLI: Reduction of aggregation of ß-lactoglobulin during heating by dihydrolipoic acid.

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Reduction of aggregation of ß-lactoglobulin during heating by dihydrolipoic acid.

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Reduction of aggregation of ß-lactoglobulin during heating by dihydrolipoic acid.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wijayanti, Heni B. Oh, H. Eustina Sharma, Ranjan Deeth, Hilton C.
Description	Country affiliation: Australia Author Affiliation: Wijayanti HB ( School of Agriculture and Food Sciences, The University of Queensland, Brisbane QLD 4072, Australia.)
Abstract	Prevention of the heat-induced aggregation of ß-lactoglobulin (ß-Lg) would improve the heat stability of whey proteins. The effects of lipoic acid (LA, or thioctic acid), in both its oxidised and reduced form (dihydrolipoic acid, DHLA), on heat-induced unfolding and aggregation of ß-Lg were investigated. LA/DHLA was added to native ß-Lg and the mixture was heated at 70, 75, 80 or 85 °C for up to 30 min at pH 6·8. The samples were analysed by Polyacrylamide Gel Electrophoresis (PAGE) and Size-exclusion HPLC (SE-HPLC). LA was not as effective as DHLA in reducing the formation of aggregates of heated ß-Lg. Heating ß-Lg with DHLA resulted in formation of more ß-Lg monomers (due to dissociation of native dimers) and significantly less ß-Lg aggregates, compared with heating ß-Lg alone. The aggregates formed in the presence of DHLA were both covalently linked, via disulphide bonds, and non-covalently (hydrophobically) linked, but the amount of covalently linked aggregates was much less than when ß-Lg was heated alone. The results suggest that DHLA was able to partially trap the reactive ß-Lg monomer containing a free sulphydryl (-SH) group, by forming a 'modified monomer', and to prevent some sulphydryl-sulphydryl and sulphydryl-disulphide interactions that lead to the formation of covalently linked protein aggregates. The effects of DHLA were similar to those of N-ethylmaleimide (NEM) and dithio(bis)-p-nitrobenzoate (DTNB). However, the advantage of using DHLA over NEM and DTNB to lessen aggregation of ß-Lg is that it is a food-grade compound which occurs naturally in milk.
File Format	HTM / HTML
ISSN	00220299
Issue Number	4
Volume Number	80
e-ISSN	14697629
Journal	Journal of Dairy Research
Language	English
Publisher	Cambridge University Press
Publisher Date	2013-11-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Veterinary Medicine Heating Lactoglobulins Chemistry Thioctic Acid Analogs & Derivatives Animals Cattle Dithionitrobenzoic Acid Ethylmaleimide Milk Milk Proteins Protein Denaturation Whey Proteins Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Animal Science and Zoology Food Science

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