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dc.contributor.author Hashim, Suhaila O.
dc.contributor.author Delgado, Osvaldo Daniel
dc.contributor.author Martinez, Maria Alejandra
dc.contributor.author Kaul, Rajni-Hatti
dc.contributor.author Mulaa, Francis J.
dc.contributor.author Mattiasson, Bo
dc.date.available 2018-04-12T17:24:06Z
dc.date.issued 2005-12
dc.identifier.citation Hashim, Suhaila O.; Delgado, Osvaldo Daniel; Martinez, Maria Alejandra; Kaul, Rajni-Hatti; Mulaa, Francis J.; et al.; Alkaline active maltohexaose-forming α-amylase from Bacillus halodurans LBK 34; Elsevier Science Inc; Enzyme and Microbial Technology; 36; 1; 12-2005; 139-146
dc.identifier.issn 0141-0229
dc.identifier.uri http://hdl.handle.net/11336/41857
dc.description.abstract The gene encoding Amy 34, a maltohexaose-forming -amylase from Bacillus halodurans LBK 34 isolated from Lake Bogoria, Kenya, was cloned and sequenced. The mature peptide consists of 958 amino acids with a theoretical molecular weight of 107.2 kDa and pI 4.41, respectively. The gene was expressed in Escherichia coli and the recombinant enzyme purified to homogeneity by a combination of metal chelate affinity and size exclusion chromatography. The pure enzyme exhibited optimum activity at 60 ◦C and pH 10.5–11.5. The enzyme retained over 60% activity after incubation at 55 ◦C for 4 h and was most stable at pH 9.0. Complete inhibition of enzyme activity was observed in presence of 5 mM Cu2+, Fe2+, Fe3+, Mn2+ and 5 mM EDTA. The enzyme displayed 80% of its original activity in presence of 1% (w/v) SDS and was stable in presence of up to 5 mM DTT. Maltohexaose (G6) was the main initial product of starch hydrolysis while other products formed were G4 > G2 > G5 > G3 and G1. The main end product of the enzyme’s action on amylose, amylopectin and maltodextrin is maltotetraose. Amy 34 could not hydrolyse pullulan, and -cyclodextrin but could hydrolyse -cyclodextrin to produce glucose, maltose and maltotetraose. Maltotetraose was the smallest -(1–4) linked maltooligosaccharide that could be hydrolysed by the enzyme
dc.format application/pdf
dc.language.iso eng
dc.publisher Elsevier Science Inc
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject Alkaliphile
dc.subject Amylase
dc.subject B. halodurans
dc.subject Maltohexaose
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title Alkaline active maltohexaose-forming α-amylase from Bacillus halodurans LBK 34
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-04-10T13:55:35Z
dc.journal.volume 36
dc.journal.number 1
dc.journal.pagination 139-146
dc.journal.pais Países Bajos
dc.journal.ciudad Amsterdam
dc.description.fil Fil: Hashim, Suhaila O.. Lund University; Suecia
dc.description.fil Fil: Delgado, Osvaldo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
dc.description.fil Fil: Martinez, Maria Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
dc.description.fil Fil: Kaul, Rajni-Hatti. Lund University; Suecia
dc.description.fil Fil: Mulaa, Francis J.. University of Nairobi; Kenia
dc.description.fil Fil: Mattiasson, Bo. Lund University; Suecia
dc.journal.title Enzyme and Microbial Technology
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.enzmictec.2004.07.017
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022904002947
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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)