期刊
FOOD CHEMISTRY
卷 134, 期 4, 页码 1947-1958出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2012.03.113
关键词
ACE inhibitory peptides; beta-Lactoglobulin; Casein derived peptides; Ion exchange resin; Protease N 'Amano'; Bitterness
资金
- Kerry Group
- BBSRC
The overall aim of this work was to characterise the major angiotensin-converting enzyme (ACE) inhibitory peptides produced by enzymatic hydrolysis of whey proteins, through the application of a novel integrative process. This process consisted of the combination of adsorption and microfiltration within a stirred cell unit for the selective immobilisation of beta-lactoglobulin and casein-derived peptides (CDP) from whey. The adsorbed proteins were hydrolysed in situ, which resulted in the separation of peptide products from the substrate and fractionation of peptides. Two different hydrolysates were produced: (i) from CDP (IC50 = 287 mu g/mL) and (ii) from beta-lactoglobulin (IC50 = 128 mu g/mL). The well-known antihypertensive peptide IPP and several novel peptides that have structural similarities with reported ACE inhibitory peptides were identified and characterised in both hydrolysates. Furthermore, the hydrolysates were assessed for bitterness. No significant difference was found between the bitterness of the control (milk with no hydrolysate) and hydrolysate samples at different concentrations (at, below and above the IC50). (C) 2012 Elsevier Ltd. All rights reserved.
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