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Identification of peptides in traditional and probiotic sheep milk yoghurt with angiotensin I-converting enzyme (ACE)-inhibitory activity

Title
Identification of peptides in traditional and probiotic sheep milk yoghurt with angiotensin I-converting enzyme (ACE)-inhibitory activity
Type
Article in International Scientific Journal
Year
2007
Authors
Papadimitriou, CG
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Vafopoulou Mastrojiannaki, A
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Silva, SV
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Gomes, AM
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F. Xavier Malcata
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Alichanidis, E
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Journal
Title: Food ChemistryImported from Authenticus Search for Journal Publications
Vol. 105 No. 3
Pages: 647-656
ISSN: 0308-8146
Publisher: Elsevier
Other information
Authenticus ID: P-004-D5V
Abstract (EN): Two sets of traditional Greek sheep milk yoghurt were produced: the first one (YC) using normal yoghurt culture (Lactobacillus delbrueckii subsp. bulgaricus gamma 10.13 and Streptococcus thermophilus gamma 10.7) and the second (PR) with the same normal culture mixed with Lactobacillus paracasei subsp. paracasei DC412. YC and PR had similar physicochemical properties and proteolysis patterns throughout storage. Both products showed similar peptide profiles by RP-HPLC but quantitative differences were observed in respect to storage time. Single-strain cultures of the microorganisms used showed similar peptide profiles for both lactobacilli, yet L. delbrueckii subsp. bulgaricus was the most proteolytic of all three microorganisms. The peptide content and the ACE-inhibitory activity of the water-soluble extracts of yoghurts, YC and PR, increased throughout storage. Major peptides were identified from yoghurt PR and from the separate cultures of L. delbrueckii subsp. bulgaricus and L. paracasei subsp. paracasei. Most of these peptides were derived from beta-casein. A peptide, beta-CN f114-121, with well-established ACE-inhibitory and opiate-like activity was identified in yoghurt PR. Further identified peptides were regarded as potential ACE-inhibitors according to their sequence. @ 2007 Elsevier Ltd. All rights reserved.
Language: English
Type (Professor's evaluation): Scientific
No. of pages: 10
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