Production of whey protein isolate hydrolysate fractions with enriched ACE-inhibitory activity

I. B. O'Loughlin; B. A. Murray; A. Brodkorb; R. J. FitzGerald; P. M. Kelly

doi:10.1016/j.idairyj.2013.12.008

Production of whey protein isolate hydrolysate fractions with enriched ACE-inhibitory activity

I. B. O'Loughlin
, B. A. Murray
, A. Brodkorb
, R. J. FitzGerald
, P. M. Kelly

Research output: Contribution to journal › Article › peer-review

Abstract

A study on the enrichment of angiotensin-converting enzyme (ACE) inhibitory activity in whey protein isolate (WPI) hydrolysate fractions is presented. A previously identified low molecular mass fraction (1 kDa permeate) of an enzymatically hydrolysed heat-treated WPI with elevated ACE-inhibition (IC₅₀ = 0.23 g L^-1) was subjected to cascade membrane ultrafiltration (UF) and diafiltration steps at lab-scale. Assaying for ACE-inhibition revealed that the 1 kDa retentate demonstrated the highest ACE-inhibitory activity (IC₅₀ = 0.17 g L^-1). Isoelectric focussing (IEF) of the hydrolysate fraction further increased ACE-inhibition in fractions collected within the pH range 6.1-6.6. Overall, both UF and IEF enriched the ACE inhibitory activity in the original fraction by ~52%, demonstrating the potential for enrichment of bio-functional activities in enzymatic hydrolysates of whey proteins.

Original language	English
Pages (from-to)	101-103
Number of pages	3
Journal	International Dairy Journal
Volume	38
Issue number	2
DOIs	https://doi.org/10.1016/j.idairyj.2013.12.008
Publication status	Published - 1 Oct 2014

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title = "Production of whey protein isolate hydrolysate fractions with enriched ACE-inhibitory activity",

abstract = "A study on the enrichment of angiotensin-converting enzyme (ACE) inhibitory activity in whey protein isolate (WPI) hydrolysate fractions is presented. A previously identified low molecular mass fraction (1 kDa permeate) of an enzymatically hydrolysed heat-treated WPI with elevated ACE-inhibition (IC50 = 0.23 g L-1) was subjected to cascade membrane ultrafiltration (UF) and diafiltration steps at lab-scale. Assaying for ACE-inhibition revealed that the 1 kDa retentate demonstrated the highest ACE-inhibitory activity (IC50 = 0.17 g L-1). Isoelectric focussing (IEF) of the hydrolysate fraction further increased ACE-inhibition in fractions collected within the pH range 6.1-6.6. Overall, both UF and IEF enriched the ACE inhibitory activity in the original fraction by \textasciitilde{}52\%, demonstrating the potential for enrichment of bio-functional activities in enzymatic hydrolysates of whey proteins.",

author = "O'Loughlin, \{I. B.\} and Murray, \{B. A.\} and A. Brodkorb and FitzGerald, \{R. J.\} and Kelly, \{P. M.\}",

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doi = "10.1016/j.idairyj.2013.12.008",

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T1 - Production of whey protein isolate hydrolysate fractions with enriched ACE-inhibitory activity

AU - O'Loughlin, I. B.

AU - Murray, B. A.

AU - Brodkorb, A.

AU - FitzGerald, R. J.

AU - Kelly, P. M.

PY - 2014/10/1

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N2 - A study on the enrichment of angiotensin-converting enzyme (ACE) inhibitory activity in whey protein isolate (WPI) hydrolysate fractions is presented. A previously identified low molecular mass fraction (1 kDa permeate) of an enzymatically hydrolysed heat-treated WPI with elevated ACE-inhibition (IC50 = 0.23 g L-1) was subjected to cascade membrane ultrafiltration (UF) and diafiltration steps at lab-scale. Assaying for ACE-inhibition revealed that the 1 kDa retentate demonstrated the highest ACE-inhibitory activity (IC50 = 0.17 g L-1). Isoelectric focussing (IEF) of the hydrolysate fraction further increased ACE-inhibition in fractions collected within the pH range 6.1-6.6. Overall, both UF and IEF enriched the ACE inhibitory activity in the original fraction by ~52%, demonstrating the potential for enrichment of bio-functional activities in enzymatic hydrolysates of whey proteins.

AB - A study on the enrichment of angiotensin-converting enzyme (ACE) inhibitory activity in whey protein isolate (WPI) hydrolysate fractions is presented. A previously identified low molecular mass fraction (1 kDa permeate) of an enzymatically hydrolysed heat-treated WPI with elevated ACE-inhibition (IC50 = 0.23 g L-1) was subjected to cascade membrane ultrafiltration (UF) and diafiltration steps at lab-scale. Assaying for ACE-inhibition revealed that the 1 kDa retentate demonstrated the highest ACE-inhibitory activity (IC50 = 0.17 g L-1). Isoelectric focussing (IEF) of the hydrolysate fraction further increased ACE-inhibition in fractions collected within the pH range 6.1-6.6. Overall, both UF and IEF enriched the ACE inhibitory activity in the original fraction by ~52%, demonstrating the potential for enrichment of bio-functional activities in enzymatic hydrolysates of whey proteins.

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VL - 38

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ER -

Production of whey protein isolate hydrolysate fractions with enriched ACE-inhibitory activity

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