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Article: Release and identification of angiotensin-converting enzyme-inhibitory peptides as influenced by ripening temperatures and probiotic adjuncts in Cheddar cheeses

TitleRelease and identification of angiotensin-converting enzyme-inhibitory peptides as influenced by ripening temperatures and probiotic adjuncts in Cheddar cheeses
Authors
KeywordsAngiotensin-converting enzyme
Cheddar cheese
Probiotic bacteria
Proteolysis
Issue Date2008
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/lwt
Citation
Lwt - Food Science And Technology, 2008, v. 41 n. 9, p. 1555-1566 How to Cite?
AbstractThe aim of the study was to examine the release of angiotensin-converting enzyme (ACE)-inhibitory peptides in Cheddar cheeses made with starter lactococci and Bifidobacterium longum 1941, B. animalis subsp. lactis LAFTI® B94, Lactobacillus casei 279, Lb. casei LAFTI® L26, Lb. acidophilus 4962 or Lb. acidophilus LAFTI® L10 during ripening at 4 and 8 °C for 24 weeks. ACE-inhibitory activity of the cheeses was maximum at 24 weeks. Cheeses made with the addition of Lb. casei 279, Lb. casei LAFTI® L26 or Lb. acidophilus LAFTI® L10 had significantly higher (P < 0.05) ACE-inhibitory activity than those without any probiotic adjunct after 24 weeks at 4 and 8 °C. The IC50 of cheeses ripened at 4 °C was not significantly different (P > 0.05) to that ripened at 8 °C. The lowest value of the IC50 (0.13 mg mL-1) and therefore the highest ACE-inhibitory activity corresponded to the cheese with the addition of Lb. acidophilus LAFTI® L10. Several ACE-inhibitory peptides were identified as κ-CN (f 96-102), αs1-CN (f 1-9), αs1-CN (f 1-7), αs1-CN (f 1-6), αs1-CN (f 24-32) and β-CN (f 193-209). Most of the ACE-inhibitory peptides accumulated at the early stage of ripening, and as proteolysis proceeded, some of the peptides were hydrolyzed into smaller peptides. © 2007 Swiss Society of Food Science and Technology.
Persistent Identifierhttp://hdl.handle.net/10722/144387
ISSN
2015 Impact Factor: 2.711
2015 SCImago Journal Rankings: 1.300
ISI Accession Number ID
Funding AgencyGrant Number
Australian Research Council (ARC)
Funding Information:

This study was made possible through a grant from Australian Research Council (ARC) under a strategic partnership with industry for research and training (SPIRT) scheme in collaboration with DSM Food Specialties Pty. Ltd. (NSW, Australia).

References

 

DC FieldValueLanguage
dc.contributor.authorOng, Len_HK
dc.contributor.authorShah, NPen_HK
dc.date.accessioned2012-01-20T09:01:46Z-
dc.date.available2012-01-20T09:01:46Z-
dc.date.issued2008en_HK
dc.identifier.citationLwt - Food Science And Technology, 2008, v. 41 n. 9, p. 1555-1566en_HK
dc.identifier.issn0023-6438en_HK
dc.identifier.urihttp://hdl.handle.net/10722/144387-
dc.description.abstractThe aim of the study was to examine the release of angiotensin-converting enzyme (ACE)-inhibitory peptides in Cheddar cheeses made with starter lactococci and Bifidobacterium longum 1941, B. animalis subsp. lactis LAFTI® B94, Lactobacillus casei 279, Lb. casei LAFTI® L26, Lb. acidophilus 4962 or Lb. acidophilus LAFTI® L10 during ripening at 4 and 8 °C for 24 weeks. ACE-inhibitory activity of the cheeses was maximum at 24 weeks. Cheeses made with the addition of Lb. casei 279, Lb. casei LAFTI® L26 or Lb. acidophilus LAFTI® L10 had significantly higher (P < 0.05) ACE-inhibitory activity than those without any probiotic adjunct after 24 weeks at 4 and 8 °C. The IC50 of cheeses ripened at 4 °C was not significantly different (P > 0.05) to that ripened at 8 °C. The lowest value of the IC50 (0.13 mg mL-1) and therefore the highest ACE-inhibitory activity corresponded to the cheese with the addition of Lb. acidophilus LAFTI® L10. Several ACE-inhibitory peptides were identified as κ-CN (f 96-102), αs1-CN (f 1-9), αs1-CN (f 1-7), αs1-CN (f 1-6), αs1-CN (f 24-32) and β-CN (f 193-209). Most of the ACE-inhibitory peptides accumulated at the early stage of ripening, and as proteolysis proceeded, some of the peptides were hydrolyzed into smaller peptides. © 2007 Swiss Society of Food Science and Technology.en_HK
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/lwten_HK
dc.relation.ispartofLWT - Food Science and Technologyen_HK
dc.subjectAngiotensin-converting enzymeen_HK
dc.subjectCheddar cheeseen_HK
dc.subjectProbiotic bacteriaen_HK
dc.subjectProteolysisen_HK
dc.titleRelease and identification of angiotensin-converting enzyme-inhibitory peptides as influenced by ripening temperatures and probiotic adjuncts in Cheddar cheesesen_HK
dc.typeArticleen_HK
dc.identifier.emailShah, NP: npshah@hku.hken_HK
dc.identifier.authorityShah, NP=rp01571en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.lwt.2007.11.026en_HK
dc.identifier.scopuseid_2-s2.0-47649096199en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-47649096199&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume41en_HK
dc.identifier.issue9en_HK
dc.identifier.spage1555en_HK
dc.identifier.epage1566en_HK
dc.identifier.isiWOS:000258500600004-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridOng, L=16200369500en_HK
dc.identifier.scopusauthoridShah, NP=7401823907en_HK

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