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dc.contributor.authordeSouza, E. L.
dc.contributor.authorHoffmann, EHE
dc.contributor.authorCastilho, V. M.
dc.contributor.authordeLima, V. A.
dc.contributor.authorBellini, M. Z.
dc.contributor.authorCruz, V. D.
dc.contributor.authorCruz, R.
dc.date.accessioned2014-05-20T15:23:51Z
dc.date.available2014-05-20T15:23:51Z
dc.date.issued1996-01-01
dc.identifierhttp://www.scielo.br/scielo.php?script=sci_issues&pid=1516-8913&lng=en&nrm=iso
dc.identifier.citationArquivos de Biologia E Tecnologia. Curitiba-Paraná: Inst Tecnologia Parana, v. 39, n. 4, p. 831-839, 1996.
dc.identifier.issn0365-0979
dc.identifier.urihttp://hdl.handle.net/11449/34545
dc.description.abstractA strain of Rhizopus sp. screened among more than 800 filamentous fungi showed great ability to produce a thermostable alpha-amylase by solid state fermentation. The best production was obtained with a bran moisture content of 40% when the enzyme activity reached 60 EU/g. of medium. During the purification procedures, a column of DEAE-Sephadex A-50 separated the enzyme in two fractions and the larger (85% of the total activity) showed optimum pH in a range from 4.0 to 5.6. Optimum temperature was found at 60-65 degrees C and in this range no loss of activity was observed after 60 min. of treatment in pH 5,0. Its K-m and V-m are, respectively, of 5.0 mg/ml of starch and 10,01 uMol of reducing sugar/min./mg. of protein. Its molecular weight was calculated in 64.000 by gel filtration in Sephadex G-200. The dextrinization power of the enzyme was observed preferentialy on substrates compound by chains with higher ramifications, that is: amylopectin > starch > amylose. Other aspects of the enzyme pattern action are also discussed.en
dc.format.extent831-839
dc.language.isopor
dc.publisherInst Tecnologia Parana
dc.relation.ispartofArquivos de Biologia E Tecnologia
dc.sourceWeb of Science
dc.titleProduction and characterization of alpha-amylase from Rhizopus spen
dc.typeArtigo
dcterms.licensehttp://www.scielo.br/revistas/babt/iaboutj.htm
dcterms.rightsHolderInst Tecnologia Parana
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.description.affiliationUNESP,DEPT CIENCIAS BIOL,FAC CIENCIAS & LETRAS,AV DOM ANTONIO 2100,CAMPUS UNIV,BR-19800000 SAO PAULO,BRAZIL
dc.description.affiliationUnespUNESP,DEPT CIENCIAS BIOL,FAC CIENCIAS & LETRAS,AV DOM ANTONIO 2100,CAMPUS UNIV,BR-19800000 SAO PAULO,BRAZIL
dc.identifier.wosWOS:A1996WV57900010
dc.rights.accessRightsAcesso restrito
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