Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58034
Type: Artigo de periódico
Title: THERMAL STABILITY OF THE IMMOBILIZED FRUCTOSYLTRANSFERASE FROM Rhodotorula sp.
Author: Aguiar-Oliveira, E
Maugeri, F
Abstract: The thermal stability of the extracellular fructosyltransferase (FTase) from Rhodotorula sp., recovered from cultivation medium by ethanol precipitation and immobilized onto niobium ore, was studied by Arrhenius plot, half-life profile, half-inactivation temperature (T-50) and thermodynamic parameters. The Arrhenius plot showed two different behaviors with different deactivation energies (E-ad) only after immobilization, the transition occurring in the temperature interval between 51 and 52 degrees C. T-50 for the free enzyme was estimated to be around 62 degrees C and, after immobilization, 66 degrees C. After 15 minutes at 52 degrees C, it was also possible to observe enzymatic activation for both the free and immobilized forms, but greater activation was achieved at pH 4.5 with the immobilized enzyme. Between 47-51 degrees C the immobilized enzyme was more stable than the free enzyme, with pH 6.0 being the more stable condition for the immobilized enzyme. However, above 52 degrees C the free form was more stable.
Subject: Niobium
Adsorption
Half-life
Thermal activation
Arrhenius plot
Dimer
Country: Brasil
Editor: Brazilian Soc Chemical Eng
Rights: aberto
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000294795300002.pdf585.18 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.