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|Title: ||Pilot-scale Production of Hydrolysates with Altered Bio-functionalities based on Thermally-denatured Whey Protein Isolate|
|Authors: ||O'Loughlin, Ian B.|
Murray, Brian A.
FitzGerald, Richard J.
Kelly, Philip M.
|Issue Date: ||13-Aug-2013|
|Citation: ||I.B. O'Loughlin, B.A. Murray, R.J. FitzGerald, A. Brodkorb, P.M. Kelly. Pilot-scale production of hydrolysates with altered bio-functionalities based on thermally-denatured whey protein isolate. International Dairy Journal, 2014, 34(1), 146-152. DOI: 10.1016/j.idairyj.2013.07.009.|
|Series/Report no.: ||International Dairy Journal;vol 34|
|Abstract: ||Whey protein isolate (WPI) solutions (100 g L−1 protein) were subjected to a heat-treatment of 80 °C for 10 min. Unheated and heat-treated WPI solutions were hydrolysed with Corolase® PP at pilot-scale to either 5 or 10% degree of hydrolysis (DH). Hydrolysates were subsequently processed via cascade membrane fractionation using 0.14 μm, and 30, 10, 5 and 1 kDa cut-off membranes. The compositional and molecular mass distribution profiles of the substrate hydrolysates and membrane processed fractions were determined. Whole and fractionated hydrolysates were assayed for both angiotensin-I-converting enzyme (ACE) inhibitory activity and ferrous chelating capabilities. A strong positive correlation (P < 0.01) was established between the average molecular mass of the test samples and the concentration needed to chelate 50% of the iron (CC50) in solution. The lowest ACE inhibition concentration (IC50 = 0.23 g L−1 protein) was determined for the 1 kDa permeate of the heat-treated 10% DH hydrolysate|
The work herein was funded by Enterprise Ireland as part of the Food for Health Ireland project, grant number; CC20080001. I. B. O’Loughlin was funded by Enterprise Ireland under the Teagasc Walsh Fellowship Scheme.
|Appears in Collections:||Food Chemistry & Technology|
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