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Article: Proteolytic profiles and angiotensin-I converting enzyme and α-glucosidase inhibitory activities of selected lactic acid bacteria

TitleProteolytic profiles and angiotensin-I converting enzyme and α-glucosidase inhibitory activities of selected lactic acid bacteria
Authors
Keywordsα-glucosidase
Angiotensin-I converting enzyme
Lactic acid bacteria
Peptidase
Proteolysis
Issue Date2008
PublisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-1147
Citation
Journal Of Food Science, 2008, v. 73 n. 2, p. M75-M81 How to Cite?
AbstractThis study was conducted to examine the growth, proteolytic profiles as well as angiotensin-I converting enzyme (ACE) and α-glucosidase (α-glu) inhibitory potentials of selected strains of lactic acid bacteria (LAB). Two strains each of yogurt bacteria (Streptococcus thermophilus - 1275 and 285, and Lactobacillus delbrueckii ssp. bulgaricus - 1092 and 1368), and probiotics (L. acidophilus - 4461 and 33200, and L. casei - 2607 and 15286, and 1 strain of Bifidobacterium longum 5022), were cultivated in reconstituted skim milk (RSM) at 37°C and their proteolytic profiles and ACE as well as α-glu inhibitory activities were determined. Among all the strains of lactic acid bacteria studied, yogurt bacteria grew very well, with the exception of L. delbrueckii ssp. bulgaricus 1368 which showed a slower growth during the initial 3 h of incubation. The growth pattern corresponded well with the decrease in pH for the organisms. All the organisms showed an increase in proteolysis with time. The variations in proteolytic capabilities translated into corresponding variations in ACE inhibitory potential of these organisms. Bifidobacterium longum 5022 showed the highest ACE inhibitory potential followed by L. delbrueckii ssp. bulgaricus 1368, L. casei 15286, S. thermophilus 1275, and L. acidophilus 4461. Organisms with high intracellular enzymatic activities grew well. Also, aminopeptidases of strains of L. acidophilus 4461 and S. thermophilus 1275 that could better utilize proline containing substrates showed enhanced ACE inhibitory potential. Lactic acid bacteria possessed the ability to inhibit α-glu activity, which endowed them an antidiabetic property as well. © 2008 Institute of Food Technologists.
Persistent Identifierhttp://hdl.handle.net/10722/144396
ISSN
2015 Impact Factor: 1.649
2015 SCImago Journal Rankings: 0.839
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorRamchandran, Len_HK
dc.contributor.authorShah, NPen_HK
dc.date.accessioned2012-01-20T09:01:49Z-
dc.date.available2012-01-20T09:01:49Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal Of Food Science, 2008, v. 73 n. 2, p. M75-M81en_HK
dc.identifier.issn0022-1147en_HK
dc.identifier.urihttp://hdl.handle.net/10722/144396-
dc.description.abstractThis study was conducted to examine the growth, proteolytic profiles as well as angiotensin-I converting enzyme (ACE) and α-glucosidase (α-glu) inhibitory potentials of selected strains of lactic acid bacteria (LAB). Two strains each of yogurt bacteria (Streptococcus thermophilus - 1275 and 285, and Lactobacillus delbrueckii ssp. bulgaricus - 1092 and 1368), and probiotics (L. acidophilus - 4461 and 33200, and L. casei - 2607 and 15286, and 1 strain of Bifidobacterium longum 5022), were cultivated in reconstituted skim milk (RSM) at 37°C and their proteolytic profiles and ACE as well as α-glu inhibitory activities were determined. Among all the strains of lactic acid bacteria studied, yogurt bacteria grew very well, with the exception of L. delbrueckii ssp. bulgaricus 1368 which showed a slower growth during the initial 3 h of incubation. The growth pattern corresponded well with the decrease in pH for the organisms. All the organisms showed an increase in proteolysis with time. The variations in proteolytic capabilities translated into corresponding variations in ACE inhibitory potential of these organisms. Bifidobacterium longum 5022 showed the highest ACE inhibitory potential followed by L. delbrueckii ssp. bulgaricus 1368, L. casei 15286, S. thermophilus 1275, and L. acidophilus 4461. Organisms with high intracellular enzymatic activities grew well. Also, aminopeptidases of strains of L. acidophilus 4461 and S. thermophilus 1275 that could better utilize proline containing substrates showed enhanced ACE inhibitory potential. Lactic acid bacteria possessed the ability to inhibit α-glu activity, which endowed them an antidiabetic property as well. © 2008 Institute of Food Technologists.en_HK
dc.languageengen_US
dc.publisherWiley-Blackwell Publishing, Inc. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-1147en_HK
dc.relation.ispartofJournal of Food Scienceen_HK
dc.subjectα-glucosidaseen_HK
dc.subjectAngiotensin-I converting enzymeen_HK
dc.subjectLactic acid bacteriaen_HK
dc.subjectPeptidaseen_HK
dc.subjectProteolysisen_HK
dc.titleProteolytic profiles and angiotensin-I converting enzyme and α-glucosidase inhibitory activities of selected lactic acid bacteriaen_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.doi10.1111/j.1750-3841.2007.00643.xen_HK
dc.identifier.pmid18298740-
dc.identifier.scopuseid_2-s2.0-39749127715en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-39749127715&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume73en_HK
dc.identifier.issue2en_HK
dc.identifier.spageM75en_HK
dc.identifier.epageM81en_HK
dc.identifier.isiWOS:000253313600029-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridRamchandran, L=23467601800en_HK
dc.identifier.scopusauthoridShah, NP=7401823907en_HK

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