TY - JOUR
T1 - Selective enrichment of bioactive properties during ultrafiltration of a tryptic digest of β-lactoglobulin
AU - Power, O.
AU - Fernández, A.
AU - Norris, R.
AU - Riera, F. A.
AU - FitzGerald, R. J.
PY - 2014/7
Y1 - 2014/7
N2 - Whey proteins are rich sources of bioactive peptides which may play a role in the dietary management of chronic diseases. Fractionation via ultrafiltration (UF) was investigated for the enrichment of antioxidant, dipeptidyl peptidase IV (DPP-IV) and angiotensin converting enzyme (ACE) inhibitory activity in a tryptic hydrolysate of β-lactoglobulin (β-Lg TH). UF processing selectively enhanced the biofunctional properties of β-Lg TH with the permeate obtained using a 1 kDa polyethersulfone (HFP-1) membrane having highest in vitro multifunctional bioactivity. Compared to β-Lg TH, the antioxidant activity was 1.7-fold higher (46,765 ± 2504 vs. 77,251 ± 5124 μmol Trolox equivalent/100 g dw; P < 0.05), DPP-IV half maximal inhibitory concentration (IC50) decreased threefold (1.6 ± 0.31 vs. 0.53 ± 0.05 mg/mL; P < 0.05) and there was a twofold reduction in ACE IC50 (0.131 ± 0.005 vs. 0.068 ± 0.018 mg/mL; P < 0.05). The multifunctional peptide VAGTWY, β-Lg f(15-20) was shown to have potent antioxidant activity (5.63 μmol TE/μmol peptide). Two new ACE inhibitory peptides, IIAEK and IPAVFK, having IC50 values of 63.7 ± 7.22 and 144.8 ± 25.3 μM, respectively, were also identified in β-Lg TH. This study demonstrates the multifunctional bioactive properties of a β-Lg TH and its associated UF fractions.
AB - Whey proteins are rich sources of bioactive peptides which may play a role in the dietary management of chronic diseases. Fractionation via ultrafiltration (UF) was investigated for the enrichment of antioxidant, dipeptidyl peptidase IV (DPP-IV) and angiotensin converting enzyme (ACE) inhibitory activity in a tryptic hydrolysate of β-lactoglobulin (β-Lg TH). UF processing selectively enhanced the biofunctional properties of β-Lg TH with the permeate obtained using a 1 kDa polyethersulfone (HFP-1) membrane having highest in vitro multifunctional bioactivity. Compared to β-Lg TH, the antioxidant activity was 1.7-fold higher (46,765 ± 2504 vs. 77,251 ± 5124 μmol Trolox equivalent/100 g dw; P < 0.05), DPP-IV half maximal inhibitory concentration (IC50) decreased threefold (1.6 ± 0.31 vs. 0.53 ± 0.05 mg/mL; P < 0.05) and there was a twofold reduction in ACE IC50 (0.131 ± 0.005 vs. 0.068 ± 0.018 mg/mL; P < 0.05). The multifunctional peptide VAGTWY, β-Lg f(15-20) was shown to have potent antioxidant activity (5.63 μmol TE/μmol peptide). Two new ACE inhibitory peptides, IIAEK and IPAVFK, having IC50 values of 63.7 ± 7.22 and 144.8 ± 25.3 μM, respectively, were also identified in β-Lg TH. This study demonstrates the multifunctional bioactive properties of a β-Lg TH and its associated UF fractions.
KW - Angiotensin converting enzyme
KW - Antioxidant
KW - Bioactive peptides
KW - Dipeptidyl peptidase IV
KW - Enzyme hydrolysis
KW - Membrane processing
KW - Trypsin
KW - β-lactoglobulin
UR - http://www.scopus.com/inward/record.url?scp=84902689746&partnerID=8YFLogxK
U2 - 10.1016/j.jff.2014.04.002
DO - 10.1016/j.jff.2014.04.002
M3 - Article
AN - SCOPUS:84902689746
SN - 1756-4646
VL - 9
SP - 38
EP - 47
JO - Journal of Functional Foods
JF - Journal of Functional Foods
IS - 1
ER -