Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58470
Type: Artigo de periódico
Title: Purification by expanded bed adsorption and characterization of an alpha-amylases FORILASE NTL (R) from A-niger
Author: Toledo, AL
Severo, JB
Souza, RR
Campos, ES
Santana, JCC
Tambourgi, EB
Abstract: In this work the purification and biochemistry characterization of alpha-amylases from Aspergillns niger (FORILASE NTL (R)) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies were done to achieve the optimal conditions of the amylases recovery on ion-exchange resin, and glucose solution was used as a new tracer. Results showed that height equivalent of the theoretical plates (HETP), axial dispersion and the Prandt number increased with bed height, bed voidage and linear velocity. The adsorption capacity of a-amylases, on the resin, increased with bed height and the best condition was at four-expansion degree. (x-Amylase characterization showed that this enzyme has high affinity with soluble starch, good hydrolysis potential and molecular weight of 116 kDa. (c) 2006 Elsevier B.V. All rights reserved.
Subject: Aspergillus niger
alpha-amylase
expanded bed adsorption
expansion degree
purification
biochemistry characterization
Country: Holanda
Editor: Elsevier Science Bv
Rights: fechado
Identifier DOI: 10.1016/j.jchromb.2006.08.011
Date Issue: 2007
Appears in Collections:Unicamp - Artigos e Outros Documentos

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