Characterization of thermostable ?-amylase isozymes from Lactobacillus fermentum

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dc.authoridAkkaya, Birnur/0000-0001-9139-1884
dc.authoridYenidunya, Ali Fazil/0000-0002-9886-977X
dc.authorwosidkocabay, samet/HZI-2537-2023
dc.authorwosidAkkaya, Birnur/AAZ-2285-2021
dc.authorwosidkocabay, samet/AAA-6158-2021
dc.authorwosidÇetinkaya, Serap/AAB-7018-2021
dc.authorwosidÇetinkaya, Serap/AAE-7285-2021
dc.contributor.authorKocabay, Samet
dc.contributor.authorCetinkaya, Serap
dc.contributor.authorAkkaya, Birnur
dc.contributor.authorYenidunya, Ali Fazil
dc.date.accessioned2024-08-04T20:42:37Z
dc.date.available2024-08-04T20:42:37Z
dc.date.issued2016
dc.departmentİnönü Üniversitesien_US
dc.description.abstractA strain of Lactobacillus fermentum producing two isozymes of a 20 kDa beta-amylase was isolated from the faecal sample of a newborn. The starin was identified by sequencing its 16S rRNA gene. The two beta-amylase isozymes were resolved and visualized by two dimensional protein gel electrophoresis (2-D gel electrophoresis). Some of the physical and biochemical properties of the enzymes were characterized. The beta-amylase displayed two optimum pH s, 5.0 and 10.0 and two optimum temperatures, 45 degrees C and 37 degrees C, respectively. The isozymes hydrolyzed different substrates: glycogen at pH 5.0, and corn starch at pH 10.0. The activity did not require Ca2+, though the activity at pH 10.0 was enhanced in the presence of 5.0 mM and 10.0 mM CaCl2, 110% and 130%, respectively. (C) 2016 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorshipCumhuriyet University, Turkey/Sivas (CUBAP) [F-408]en_US
dc.description.sponsorshipThis work was supported by The Research Fund of Cumhuriyet University, Turkey/Sivas (CUBAP, project number F-408).en_US
dc.identifier.doi10.1016/j.ijbiomac.2016.08.078
dc.identifier.endpage202en_US
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.pmid27581558en_US
dc.identifier.scopus2-s2.0-84984686671en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage195en_US
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2016.08.078
dc.identifier.urihttps://hdl.handle.net/11616/97489
dc.identifier.volume93en_US
dc.identifier.wosWOS:000389090900024en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherElsevier Science Bven_US
dc.relation.ispartofInternational Journal of Biological Macromoleculesen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBeta-amylaseen_US
dc.subjectIsozymeen_US
dc.subjectLactobacillus fermentumen_US
dc.subjectPurificationen_US
dc.subjectTwo dimentional protein electrophoresisen_US
dc.titleCharacterization of thermostable ?-amylase isozymes from Lactobacillus fermentumen_US
dc.typeArticleen_US

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