期刊
JOURNAL OF FUNCTIONAL FOODS
卷 9, 期 -, 页码 38-47出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2014.04.002
关键词
beta-lactoglobulin; Trypsin; Enzyme hydrolysis; Membrane processing; Bioactive peptides; Dipeptidyl peptidase IV; Antioxidant; Angiotensin converting enzyme
资金
- Enterprise Ireland under the Irish Research Council (IRC) [CC20080001]
- Severo Ochoa Programme (Principado de Asturias Government)
- Higher Education Authority under the Programme for Research in Third Level Institutions (cycle 4) as part of the National Development Plan
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 beta-lactoglobulin (beta-LgTH). UF processing selectively enhanced the biofunctional properties of beta-Lg TH with the permeate obtained using a 1 kDa polyethersulfone (HFP-1) membrane having highest in vitro multifunctional bioactivity. Compared to beta-Lg TH, the antioxidant activity was 1.7-fold higher (46,765 +/- 2504 vs. 77,251 +/- 5124 mu mol 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, beta-Lg f(15-20) was shown to have potent antioxidant activity (5.63 mu mol TE/mu mol peptide). Two new ACE inhibitory peptides, IIAEK and IPAVFK, having IC50 values of 63.7 +/- 7.22 and 144.+/- 8 25.3 mu M, respectively, were also identified in beta-Lg TH. This study demonstrates the multifunctional bioactive properties of a beta-Lg TH and its associated UF fractions. (C) 2014 Elsevier Ltd. All rights reserved.
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