Page analysis of milk proteins altered by high thermal treatment
Апстракт
Changes that occur in milk proteins during heat treatment were studied. Milk was heat treated at 87 degrees C for 10 min. Samples of untreated milk, demineralised whey powder and heat treated milk were analysed by discontinuous PAGE and by densitometric analysis of destained gels. PAGE experiments showed that heat treatment induces changes on milk proteins. During heating at 87 degrees C for 10 min all amount of beta-lactoglobulin present in milk interacted with casein, while small amount of alpha-lactalbumin did not interact with casein. It could be hypothesised that heating of milk at 87 degrees C for 10 min influences complete denaturation of beta-lactoglobulin and formation of complex with casein, while alpha-lactalburnin denatures and interacts with beta-lactoglobulin when beta-lactoglobulin has already linked with casein micelles.
Кључне речи:
heat treatment / milk proteins / PAGEИзвор:
Acta Alimentaria, 2005, 34, 2, 105-112Издавач:
- Akademiai Kiado Zrt, Budapest
DOI: 10.1556/AAlim.34.2005.2.2
ISSN: 0139-3006
WoS: 000230414100002
Scopus: 2-s2.0-20844452181
Институција/група
Poljoprivredni fakultetTY - JOUR AU - Jovanović, S AU - Barać, Miroljub AU - Maćej, Ognjen AU - Djurdjević, JD PY - 2005 UR - http://aspace.agrif.bg.ac.rs/handle/123456789/1025 AB - Changes that occur in milk proteins during heat treatment were studied. Milk was heat treated at 87 degrees C for 10 min. Samples of untreated milk, demineralised whey powder and heat treated milk were analysed by discontinuous PAGE and by densitometric analysis of destained gels. PAGE experiments showed that heat treatment induces changes on milk proteins. During heating at 87 degrees C for 10 min all amount of beta-lactoglobulin present in milk interacted with casein, while small amount of alpha-lactalbumin did not interact with casein. It could be hypothesised that heating of milk at 87 degrees C for 10 min influences complete denaturation of beta-lactoglobulin and formation of complex with casein, while alpha-lactalburnin denatures and interacts with beta-lactoglobulin when beta-lactoglobulin has already linked with casein micelles. PB - Akademiai Kiado Zrt, Budapest T2 - Acta Alimentaria T1 - Page analysis of milk proteins altered by high thermal treatment EP - 112 IS - 2 SP - 105 VL - 34 DO - 10.1556/AAlim.34.2005.2.2 ER -
@article{ author = "Jovanović, S and Barać, Miroljub and Maćej, Ognjen and Djurdjević, JD", year = "2005", abstract = "Changes that occur in milk proteins during heat treatment were studied. Milk was heat treated at 87 degrees C for 10 min. Samples of untreated milk, demineralised whey powder and heat treated milk were analysed by discontinuous PAGE and by densitometric analysis of destained gels. PAGE experiments showed that heat treatment induces changes on milk proteins. During heating at 87 degrees C for 10 min all amount of beta-lactoglobulin present in milk interacted with casein, while small amount of alpha-lactalbumin did not interact with casein. It could be hypothesised that heating of milk at 87 degrees C for 10 min influences complete denaturation of beta-lactoglobulin and formation of complex with casein, while alpha-lactalburnin denatures and interacts with beta-lactoglobulin when beta-lactoglobulin has already linked with casein micelles.", publisher = "Akademiai Kiado Zrt, Budapest", journal = "Acta Alimentaria", title = "Page analysis of milk proteins altered by high thermal treatment", pages = "112-105", number = "2", volume = "34", doi = "10.1556/AAlim.34.2005.2.2" }
Jovanović, S., Barać, M., Maćej, O.,& Djurdjević, J.. (2005). Page analysis of milk proteins altered by high thermal treatment. in Acta Alimentaria Akademiai Kiado Zrt, Budapest., 34(2), 105-112. https://doi.org/10.1556/AAlim.34.2005.2.2
Jovanović S, Barać M, Maćej O, Djurdjević J. Page analysis of milk proteins altered by high thermal treatment. in Acta Alimentaria. 2005;34(2):105-112. doi:10.1556/AAlim.34.2005.2.2 .
Jovanović, S, Barać, Miroljub, Maćej, Ognjen, Djurdjević, JD, "Page analysis of milk proteins altered by high thermal treatment" in Acta Alimentaria, 34, no. 2 (2005):105-112, https://doi.org/10.1556/AAlim.34.2005.2.2 . .