Purification and characterization of thermostable and detergent-stable α-amylase from Anoxybacillus sp. AH1

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dc.contributor.authorAcer, Ömer
dc.contributor.authorBekler, Fatma Matpan
dc.contributor.authorPirinççioğlu, Hemşe
dc.contributor.authorGüven, Reyhan Gül
dc.contributor.authorGüven, Kemal
dc.date.accessioned2024-04-24T17:56:48Z
dc.date.available2024-04-24T17:56:48Z
dc.date.issued2016
dc.departmentDicle Üniversitesien_US
dc.description.abstractA thermostable and detergent-stable ?-amylase from a newly isolated Anoxybacillus sp. AH1 was purified and characterized. Maximum enzyme production (1874.8 U/mL) was obtained at 24 h of incubation. The amylase was purified by using Sephadex G-75 gel filtration, after which an 18-fold increase in specific activity and a yield of 9 % were achieved. The molecular mass of the purified enzyme was estimated at 85 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH and temperature values of the enzyme were 7.0 and 60 °C, respectively. The enzyme was highly stable in the presence of 30 % glycerol, retaining 85 % of its original activity at 60 °C within 120 min. Km and vmax values were 0.102 ?mol and 0.929 ?mol/min, respectively, using Lineweaver- Burk plot. The enzyme activity was increased by various detergents, but it was significantly inhibited in the presence of urea. Mg2+ and Ca2+ also significantly activated ?-amylase, while Zn2+, Cu2+ and metal ion chelators ethylenediaminetetraacetic acid (EDTA) and 1,10-phenanthroline (phen) greatly inhibited the enzyme activity. ?-Amylase activity was enhanced by ?-mercaptoethanol (?-ME) and dithiothreitol (DTT) to a great extent, but inhibited by p-chloromercuribenzoic acid (PCMB). Iodoacetamide (IAA) and N-ethylmaleimide (NEM) had a slight, whereas phenylmethylsulfonyl fluoride (PMSF) had a strong inhibitory effect on the amylase activity.en_US
dc.identifier.citationAcer, Ö., Bekler, F. M., Pirinççioğlu, H., Güven, R. G. ve Güven, K. (2016). Purification and characterization of thermostable and detergent-stable α-amylase from Anoxybacillus sp. AH1. Food Technology and Biotechnology, 54(1), 70-77.
dc.identifier.doi10.17113/ftb.54.01.16.4122
dc.identifier.endpage77en_US
dc.identifier.issn1330-9862
dc.identifier.issue1en_US
dc.identifier.scopus2-s2.0-84964888680
dc.identifier.scopusqualityQ2
dc.identifier.startpage70en_US
dc.identifier.urihttps://doi.org/10.17113/ftb.54.01.16.4122
dc.identifier.urihttps://hdl.handle.net/11468/23671
dc.identifier.volume54en_US
dc.identifier.wosWoSIDEksik
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoenen_US
dc.publisherUniversity of Zagreben_US
dc.relation.ispartofFood Technology and Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAnoxybacillus Sp. Ah1en_US
dc.subjectDetergent-Stable ?-Amylaseen_US
dc.subjectEnzyme activity inhibitionen_US
dc.subjectEnzyme purificationen_US
dc.titlePurification and characterization of thermostable and detergent-stable α-amylase from Anoxybacillus sp. AH1en_US
dc.titlePurification and characterization of thermostable and detergent-stable ?-amylase from Anoxybacillus sp. AH1
dc.typeArticleen_US

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