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Article: Endogenous β-glucosidase and β-galactosidase activities from selected probiotic micro-organisms and their role in isoflavone biotransformation in soymilk

TitleEndogenous β-glucosidase and β-galactosidase activities from selected probiotic micro-organisms and their role in isoflavone biotransformation in soymilk
Authors
Keywordsβ-glucosidase and β-galactosidase activities
Aglycone increments
Otieno Shah (O-S) index
Issue Date2007
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JAM
Citation
Journal Of Applied Microbiology, 2007, v. 103 n. 4, p. 910-917 How to Cite?
AbstractAim: To compare endogenous β-glucosidases and β-galactosidases for hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk. Methods and Results: β-glucosidase and β-galactosidase activities of probiotic organisms including Lactobacillus acidophilus ATCC 4461, Lactobacillus casei 2607 and Bifidobacterium animalis ssp. lactis Bb12 in soymilk were evaluated and correlated with the increase in concentration of isoflavone aglycones during fermentation. The concentrations of isoflavone compounds in soymilk were monitored using a Varian model high-performance liquid chromatography (HPLC) with an amperometric electrochemical detector. In all micro-organisms, β-glucosidase activity was found greater than that of β-galactosidase. There was an increase in the aglycone concentration with incubation time because of the apparent hydrolytic action on isoflavone glycosides. Aglycone concentration in the soymilk with L. acidophilus 4461, L. casei 2607 and B. animalis ssp. lactis Bb12, increased by 5.37-, 5.52- and 6.10-fold, respectively, after 15 h of fermentation at 37°C. The maximum hydrolytic potential was also observed at 15 h of fermentation for the three micro-organims coinciding with peak activities of the two enzymes. Conclusions: β-glucosidase activity was more than 15 times higher than β-galactosidase activity in soymilk for each of the micro-organisms during fermentation. β-glucosidase played a greater role in isoflavone glycoside hydrolysis. Significance and Impact of the Study: Screening for β-glucosidase and β-galactosidase activities among probiotics in soymilk is important for the improvement of biological activity of soymilk and in the selection of micro-organisms for use in the growing industry of functional foods and beverages. © 2007 The Authors.
Persistent Identifierhttp://hdl.handle.net/10722/144411
ISSN
2015 Impact Factor: 2.156
2015 SCImago Journal Rankings: 0.921
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorOtieno, DOen_HK
dc.contributor.authorShah, NPen_HK
dc.date.accessioned2012-01-20T09:01:54Z-
dc.date.available2012-01-20T09:01:54Z-
dc.date.issued2007en_HK
dc.identifier.citationJournal Of Applied Microbiology, 2007, v. 103 n. 4, p. 910-917en_HK
dc.identifier.issn1364-5072en_HK
dc.identifier.urihttp://hdl.handle.net/10722/144411-
dc.description.abstractAim: To compare endogenous β-glucosidases and β-galactosidases for hydrolysis of the predominant isoflavone glycosides into isoflavone aglycones in order to improve biological activity of soymilk. Methods and Results: β-glucosidase and β-galactosidase activities of probiotic organisms including Lactobacillus acidophilus ATCC 4461, Lactobacillus casei 2607 and Bifidobacterium animalis ssp. lactis Bb12 in soymilk were evaluated and correlated with the increase in concentration of isoflavone aglycones during fermentation. The concentrations of isoflavone compounds in soymilk were monitored using a Varian model high-performance liquid chromatography (HPLC) with an amperometric electrochemical detector. In all micro-organisms, β-glucosidase activity was found greater than that of β-galactosidase. There was an increase in the aglycone concentration with incubation time because of the apparent hydrolytic action on isoflavone glycosides. Aglycone concentration in the soymilk with L. acidophilus 4461, L. casei 2607 and B. animalis ssp. lactis Bb12, increased by 5.37-, 5.52- and 6.10-fold, respectively, after 15 h of fermentation at 37°C. The maximum hydrolytic potential was also observed at 15 h of fermentation for the three micro-organims coinciding with peak activities of the two enzymes. Conclusions: β-glucosidase activity was more than 15 times higher than β-galactosidase activity in soymilk for each of the micro-organisms during fermentation. β-glucosidase played a greater role in isoflavone glycoside hydrolysis. Significance and Impact of the Study: Screening for β-glucosidase and β-galactosidase activities among probiotics in soymilk is important for the improvement of biological activity of soymilk and in the selection of micro-organisms for use in the growing industry of functional foods and beverages. © 2007 The Authors.en_HK
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JAMen_HK
dc.relation.ispartofJournal of Applied Microbiologyen_HK
dc.subjectβ-glucosidase and β-galactosidase activitiesen_HK
dc.subjectAglycone incrementsen_HK
dc.subjectOtieno Shah (O-S) indexen_HK
dc.titleEndogenous β-glucosidase and β-galactosidase activities from selected probiotic micro-organisms and their role in isoflavone biotransformation in soymilken_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.1365-2672.2007.03438.xen_HK
dc.identifier.pmid17897193-
dc.identifier.scopuseid_2-s2.0-34848818763en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34848818763&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume103en_HK
dc.identifier.issue4en_HK
dc.identifier.spage910en_HK
dc.identifier.epage917en_HK
dc.identifier.eissn1365-2672-
dc.identifier.isiWOS:000249825300018-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridOtieno, DO=12242657400en_HK
dc.identifier.scopusauthoridShah, NP=7401823907en_HK
dc.identifier.citeulike1798279-

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