Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/76914
Type: Artigo de periódico
Title: Adsorption of the inulinase from Kluyveromyces marxianus NRRL Y-7571 on Streamline((R)) DEAE resin
Author: Makino, Y
Lima, PSC
Filho, FM
Rodrigues, MI
Abstract: The enzyme inulinase is used to produce oligosaccharides and fructose, with up to 95% fructose in a single stage of inulina hydrolysis. With in the aim to purify the enzyme, studies on the conditions of enzyme adsorption in an expanded-bed column were conducted using phosphate and tris-HCl buffers. The inulinase used in this work was obtained from Kluyveromyces marxianus NRRL Y-7571 by fermentation in an industrial medium. Using the anionic resin Streamline DEAE, the adsorption equilibrium time was determined. It was observed that the adsorption isotherm follows the Langmuir model; the parameters for the maximum amount of adsorbed inulinase (Q(m)) and the dissociation constant (k(d)) were determined. With 0.05 M sodium phosphate buffer at pH 6.0, the parameter values 1428 UI/mL and 2 UI/mL with a correlation coefficient of 0.96 were obtained. For 0.02 M tris-HCl buffer at pH 7.5, the same parameters were 5000 UI/mL and 0.05 UI/mL with a correlation coefficient of 0.99. The best purification conditions for the fixed bed were shown to be a 0.4 M phosphate buffer with NaCl as eluter, a purification factor of 11.4, and a recovery yield of up to 79%.
Subject: enzyme
adsorption
oligosaccharides and fructose
Country: Brasil
Editor: Brazilian Soc Chemical Eng
Rights: aberto
Identifier DOI: 10.1590/S0104-66322005000400006
Date Issue: 2005
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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