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Title:

Seletive hydrolysis of α-lactalbumin by acid protease A offers potential for β-latoglobulin purification in whey proteins

Document type:
Zeitschriftenaufsatz
Author(s):
Cheison, S. C.; Bor, E. K.; Faraj, A. K.; Kulozik, U.
Abstract:
Whey protein (WP) purification exploits selective heat and salt stabilities. Proteins are denatured. WP α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) are resistant to trypsin (EC 3.4.21.4) and pepsin (EC 3.4.23.1), respectively. This work was to selectively hydrolyse α-La in WP isolate (WPI) using Acid Protease A in acid pH in order to selectively remove α-La while retaining high amounts of native β-Lg. WPI was hydrolysed over a range of temperature (30 °C, 37.5 °C and 45 °C) and pH (2.5, 3.0...     »
Keywords:
Acid Protease A; a-lactalbumin; Selective Hydrolysis; ß-Lactoglobulin
Journal title:
LWT - Food Science and Technology
Year:
2012
Journal volume:
49
Pages contribution:
117--122
Fulltext / DOI:
doi:10.1016/j.lwt.2012.03.022
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