Preparation of ingredients containing an ACE-inhibitory peptide by tryptic hydrolysis of whey protein concentrates

被引：64

作者：

Ferreira, I. M. P. L. V. O.

Pinho, O.

Mota, M. V.

Tavares, P.

Pereira, A.

Goncalves, M. P.

Torres, D.

Rocha, C.

Teixeira, J. A.

机构：

[1] Univ Porto, Fac Farm, Serv Bromatol, REQUIMTE, P-4050047 Oporto, Portugal

[2] Univ Porto, Fac Ciencias Nutr & Alimentacao, P-4200465 Oporto, Portugal

[3] Univ Nova Lisboa, Dept Quim, REQUIMTE, Fac Ciencias & Tecnol, P-2825 Monte De Caparica, Portugal

[4] Univ Porto, Fac Engn, Dept Engn Quim, REQUIMTE, P-4200465 Oporto, Portugal

[5] Univ Minho, IBQF, Ctr Engn Biol, P-4710057 Braga, Portugal

来源：

INTERNATIONAL DAIRY JOURNAL | 2007年 / 17卷 / 05期

关键词：

whey protein concentrates; trypsin hydrolysis; ACE-inhibitory peptides; gelation;

D O I：

10.1016/j.idairyj.2006.06.023

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

This study describes the characterisation of whey protein hydrolysates obtained from tryptic hydrolysis to assess their application as ingredients with angiotensin-converting-enzyme (ACE) inhibitory action. The levels of a-lactalbumin (alpha-la) and P-lactoglobulin (beta-lg) remaining after hydrolysis were quantified. Peptides were separated by RP-HPLC, and Ala-Leu-Pro-Met-His-Ile-Arg (ALPMHIR), the most potent beta-lg-derived ACE-inhibitory peptide was monitored. A correlation curve was established for the production of this peptide as a function of hydrolysis time. Heat-induced gelation of hydrolysates was studied by small-deformation rheology. The gelation times and the strength of the final gels were highly dependent on the degree of hydrolysis. Smaller peptides liberated by hydrolysis contributed to the inability of whey protein hydrolysates to gel. (c) 2006 Elsevier Ltd. All rights reserved.

引用

页码：481 / 487

页数：7

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