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Article: Proteolytic profiles of yogurt and probiotic bacteria

TitleProteolytic profiles of yogurt and probiotic bacteria
Authors
KeywordsOPA
Probiotic bacteria
Proteolytic activity
Yogurt bacteria
Issue Date2000
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/idairyj
Citation
International Dairy Journal, 2000, v. 10 n. 5-6, p. 401-408 How to Cite?
AbstractNine strains of Streptococcus thermophilus, 6 strains of Lactobacillus delbrueckii ssp. bulgaricus, 14 strains of Lactobacillus acidophilus and 13 strains of Bifidobacterium spp. were screened for proteolytic, amino-, di-, tri- and endopeptidase activity by using the o-pthaldialdehyde-based spectrophotometric assay. Strains showing the highest and lowest proteolytic activity were further studied for their peptidase activities at the extracellular and intracellular levels. The amounts of free amino groups released by S. thermophilus, L. delbrueckii ssp. bulgaricus and L. acidophilus strains were higher than by Bifidobacterium strains. Aminopeptidase activity was detected for all bacterial strains both at the extracellular and intracellular levels. The specific activity towards the six substrates studied was higher at the intracellular level for all strains. High dipeptidase activity was demonstrated by all bacterial strains for L. delbrueckii ssp. bulgaricus, L. acidophilus, and Bifidobacterium spp. whereas S. thermophilus had greater dipeptidase activity at the extracellular level. All bacterial cultures tested were able to hydrolyse large biologically active peptides, bradykinin, Ala-Ala-Ala-Ala-Ala and the tripeptide substrate Gly-Ala-Tyr at both the extracellular and intracellular levels. However, with the substrates ending with a C-terminal of phenylalanine, the hydrolysis only occurred at the intracellular level. (C) 2000 Elsevier Science Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/144343
ISSN
2015 Impact Factor: 1.938
2015 SCImago Journal Rankings: 0.991
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorShihata, Aen_HK
dc.contributor.authorShah, NPen_HK
dc.date.accessioned2012-01-20T09:01:32Z-
dc.date.available2012-01-20T09:01:32Z-
dc.date.issued2000en_HK
dc.identifier.citationInternational Dairy Journal, 2000, v. 10 n. 5-6, p. 401-408en_HK
dc.identifier.issn0958-6946en_HK
dc.identifier.urihttp://hdl.handle.net/10722/144343-
dc.description.abstractNine strains of Streptococcus thermophilus, 6 strains of Lactobacillus delbrueckii ssp. bulgaricus, 14 strains of Lactobacillus acidophilus and 13 strains of Bifidobacterium spp. were screened for proteolytic, amino-, di-, tri- and endopeptidase activity by using the o-pthaldialdehyde-based spectrophotometric assay. Strains showing the highest and lowest proteolytic activity were further studied for their peptidase activities at the extracellular and intracellular levels. The amounts of free amino groups released by S. thermophilus, L. delbrueckii ssp. bulgaricus and L. acidophilus strains were higher than by Bifidobacterium strains. Aminopeptidase activity was detected for all bacterial strains both at the extracellular and intracellular levels. The specific activity towards the six substrates studied was higher at the intracellular level for all strains. High dipeptidase activity was demonstrated by all bacterial strains for L. delbrueckii ssp. bulgaricus, L. acidophilus, and Bifidobacterium spp. whereas S. thermophilus had greater dipeptidase activity at the extracellular level. All bacterial cultures tested were able to hydrolyse large biologically active peptides, bradykinin, Ala-Ala-Ala-Ala-Ala and the tripeptide substrate Gly-Ala-Tyr at both the extracellular and intracellular levels. However, with the substrates ending with a C-terminal of phenylalanine, the hydrolysis only occurred at the intracellular level. (C) 2000 Elsevier Science Ltd.en_HK
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/idairyjen_HK
dc.relation.ispartofInternational Dairy Journalen_HK
dc.subjectOPAen_HK
dc.subjectProbiotic bacteriaen_HK
dc.subjectProteolytic activityen_HK
dc.subjectYogurt bacteriaen_HK
dc.titleProteolytic profiles of yogurt and probiotic 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.doi10.1016/S0958-6946(00)00072-8en_HK
dc.identifier.scopuseid_2-s2.0-0033816221en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033816221&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume10en_HK
dc.identifier.issue5-6en_HK
dc.identifier.spage401en_HK
dc.identifier.epage408en_HK
dc.identifier.isiWOS:000089707700012-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridShihata, A=6602968352en_HK
dc.identifier.scopusauthoridShah, NP=7401823907en_HK

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