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Article: Enzyme Stability of Microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after Freeze Drying and during Storage in Low Water Activity at Room Temperature

TitleEnzyme Stability of Microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after Freeze Drying and during Storage in Low Water Activity at Room Temperature
Authors
KeywordsLong-term storage
Low a w
Mannitol
Sodium alginate-based system
Stability of enzymes activities
Issue Date2011
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, 2011, v. 76 n. 6, p. M463-M471 How to Cite?
AbstractStability of enzymes such as β-galactosidase (β-gal), β-glucosidase (β-glu), lactate dehydrogenase (LDH), pyruvate kinase (PK), hexokinase (HK), and ATPase of microencapsulatedBifidobacterium animalisssp.lactisBb12 after freeze-drying and after 10 wk of storage at low water activity (a w) at room temperature was studied. Bacteria were microencapsulated using alginate formulation with or without mannitol fortification (sodium alginate and mannitol [SAM] and sodium alginate [SA], respectively) by creating gel beads followed by freeze drying. Two types of dried gel beads were then stored at low a w, such as 0.07, 0.1, and 0.2; storage in an aluminum foil was used as control. All storage was carried out at room temperature of 25 °C for 10 wk. Measurement of β-gal, β-glu, LDH, PK, HK, and ATPase (with or without exposure to pH 2.0 for 2 h) activities was carried out before freeze drying, after freeze drying, and after 10 wk of storage. There was a significant decrease in almost all enzyme activities, except that of PK. SAM and SA showed no different effect on maintaining enzyme activities during freeze drying. Storage for 10 wk at room temperature at various low a w using SAM and SA system had a significant effect on retention of most enzymes studied, except that of PK and LDH. Storage at a w of 0.07 and 0.1 was more effective in maintaining enzyme activities than storage at a w of 0.2 and in an aluminum foil. However, mannitol fortification into alginate system did not significantly improve retention of enzymes during 10 wk of storage. © 2011 Institute of Food Technologists ®.
Persistent Identifierhttp://hdl.handle.net/10722/179246
ISSN
2021 Impact Factor: 3.693
2020 SCImago Journal Rankings: 0.772
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDianawati, Den_US
dc.contributor.authorShah, NPen_US
dc.date.accessioned2012-12-19T09:53:21Z-
dc.date.available2012-12-19T09:53:21Z-
dc.date.issued2011en_US
dc.identifier.citationJournal Of Food Science, 2011, v. 76 n. 6, p. M463-M471en_US
dc.identifier.issn0022-1147en_US
dc.identifier.urihttp://hdl.handle.net/10722/179246-
dc.description.abstractStability of enzymes such as β-galactosidase (β-gal), β-glucosidase (β-glu), lactate dehydrogenase (LDH), pyruvate kinase (PK), hexokinase (HK), and ATPase of microencapsulatedBifidobacterium animalisssp.lactisBb12 after freeze-drying and after 10 wk of storage at low water activity (a w) at room temperature was studied. Bacteria were microencapsulated using alginate formulation with or without mannitol fortification (sodium alginate and mannitol [SAM] and sodium alginate [SA], respectively) by creating gel beads followed by freeze drying. Two types of dried gel beads were then stored at low a w, such as 0.07, 0.1, and 0.2; storage in an aluminum foil was used as control. All storage was carried out at room temperature of 25 °C for 10 wk. Measurement of β-gal, β-glu, LDH, PK, HK, and ATPase (with or without exposure to pH 2.0 for 2 h) activities was carried out before freeze drying, after freeze drying, and after 10 wk of storage. There was a significant decrease in almost all enzyme activities, except that of PK. SAM and SA showed no different effect on maintaining enzyme activities during freeze drying. Storage for 10 wk at room temperature at various low a w using SAM and SA system had a significant effect on retention of most enzymes studied, except that of PK and LDH. Storage at a w of 0.07 and 0.1 was more effective in maintaining enzyme activities than storage at a w of 0.2 and in an aluminum foil. However, mannitol fortification into alginate system did not significantly improve retention of enzymes during 10 wk of storage. © 2011 Institute of Food Technologists ®.en_US
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_US
dc.relation.ispartofJournal of Food Scienceen_US
dc.rightsThe definitive version is available at www3.interscience.wiley.com-
dc.subjectLong-term storage-
dc.subjectLow a w-
dc.subjectMannitol-
dc.subjectSodium alginate-based system-
dc.subjectStability of enzymes activities-
dc.subject.meshAdenosine Triphosphatases - Chemistry - Metabolismen_US
dc.subject.meshAlginates - Chemistryen_US
dc.subject.meshBacterial Proteins - Chemistry - Metabolismen_US
dc.subject.meshBifidobacterium - Enzymologyen_US
dc.subject.meshEmulsionsen_US
dc.subject.meshEnzyme Stabilityen_US
dc.subject.meshFood Technologyen_US
dc.subject.meshFreeze Dryingen_US
dc.subject.meshGelsen_US
dc.subject.meshGlucuronic Acid - Chemistryen_US
dc.subject.meshGlycoside Hydrolases - Chemistry - Metabolismen_US
dc.subject.meshHexuronic Acids - Chemistryen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMannitol - Chemistryen_US
dc.subject.meshMicrospheresen_US
dc.subject.meshPhosphotransferases (Alcohol Group Acceptor) - Chemistry - Metabolismen_US
dc.subject.meshProbiotics - Chemistry - Metabolismen_US
dc.subject.meshTemperatureen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshWater - Analysisen_US
dc.titleEnzyme Stability of Microencapsulated Bifidobacterium animalis ssp. lactis Bb12 after Freeze Drying and during Storage in Low Water Activity at Room Temperatureen_US
dc.typeArticleen_US
dc.identifier.emailShah, NP: npshah@hku.hken_US
dc.identifier.authorityShah, NP=rp01571en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1111/j.1750-3841.2011.02246.xen_US
dc.identifier.pmid21696390-
dc.identifier.scopuseid_2-s2.0-79961128183en_US
dc.identifier.hkuros205694-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79961128183&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume76en_US
dc.identifier.issue6en_US
dc.identifier.spageM463en_US
dc.identifier.epageM471en_US
dc.identifier.isiWOS:000293633100062-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridDianawati, D=40761270000en_US
dc.identifier.scopusauthoridShah, NP=7401823907en_US
dc.identifier.issnl0022-1147-

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