Yeasts from Colombian Kumis as source of peptides with Angiotensin I converting enzyme (ACE) inhibitory activity in milk

被引:75
作者
Chaves-Lopez, Clemencia [1 ]
Tofalo, Rosanna [1 ]
Serio, Annalisa [1 ]
Paparella, Antonello [1 ]
Sacchetti, Giampiero [1 ]
Suzzi, Giovanna [1 ]
机构
[1] Univ Teramo, Dipartimento Sci Alimenti, I-64023 Mosciano Sant Angelo, TE, Italy
关键词
Yeast; Angiotensin converting enzyme; Proteolysis; Fermented milk; Kumis; LACTIC-ACID BACTERIA; NATURALLY FERMENTED MILK; ANTIHYPERTENSIVE ACTIVITY; GEOTRICHUM-CANDIDUM; GOAT WHEY; RAW-MILK; IDENTIFICATION; PROTEOLYSIS; STRAINS; PRODUCTS;
D O I
10.1016/j.ijfoodmicro.2012.07.028
中图分类号
TS2 [食品工业];
学科分类号
100403 [营养与食品卫生学];
摘要
This study investigated the possibility of using yeast strains in fermented milks to obtain products with high Angiotensin I-converting enzyme (ACE) inhibitory activity and low bitter taste. Ninety-three yeast strains isolated from Colombian Kumis in different geographic regions were molecularly identified, and their milk fermentation performances were determined. Molecular identification evidenced that Galactomyces geotrichum, Pichia kudriavzevii, Clavispora lusitaniae and Candida tropicalis, were the dominant species. Eighteen out of 93 strains produced fermented milk with ACE-inhibitory (ACEI) activity values ranging from 8.69 to 88.19%. Digestion of fermented milk samples by pepsin and pancreatin demonstrated an increase in ACEI activity, with C. lusitaniae KL4A as the best producer of ACEI peptides. Moreover, sensory analysis of the products containing the major ACE-inhibitory activity pointed out that P. kudriavzevii KL84A and Kluyveromyces marxianus KL26A could be selected as potential adjunct starter cultures in Kumis, since they made a considerable contribution to the ACE inhibitory activity and produced fermented milk without bitter taste. In this study we observed that Colombian Kumis can be an excellent vehicle for the isolation of yeasts With a potential to enhance bioactive peptides produced during milk fermentation. (C) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:39 / 46
页数:8
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