Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/486
Type: Artigo de periódico
Title: Effect of Polyethylene Glycol on the Thermal Stability of Green Fluorescent Protein
Author: NOVAES, Leticia C. de Lencastre
MAZZOLA, Priscila G.
PESSOA JR., Adalberto
PENNA, Thereza C. Vessoni
Abstract: Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. Some polymers, such as polyethylene glycol, are often used as modifiers of characteristics of biological macromolecules, to improve the biochemical activity and stability of proteins or drug bioavailability. The aim of this study was to evaluate the thermal stability of GFP in the presence of different PEG molar weights at several concentrations and exposed to constant temperatures, in a range of 70-95 degrees C. Thermal stability was expressed in decimal reduction time. It was observed that the D-values obtained were almost constant for temperatures of 85, 90, and 95 degrees C, despite the PEG concentration or molar weight studied. Even though PEG can stabilize proteins, only at 75 degrees C, PEG 600 and 4,000 g/mol stabilized GFP. (C) 2009 American Institute of Chemical Engineers Biotechnol. Prog., 26: 252-256, 2010
Subject: green fluorescent protein
polyethylene glycol
protein stability
thermal stability
Country: Inglaterra
Editor: JOHN WILEY & SONS LTD
Citation: BIOTECHNOLOGY PROGRESS, v.26, n.1, p.252-256, 2010
Rights: fechado
Identifier DOI: 10.1002/btpr.296
Address: http://apps.isiknowledge.com/InboundService.do?Func=Frame&product=WOS&action=retrieve&SrcApp=EndNote&UT=000274973400032&Init=Yes&SrcAuth=ResearchSoft&mode=FullRecord
http://dx.doi.org/10.1002/btpr.296
Date Issue: 2010
Appears in Collections:IQ - Artigos e Outros Documentos

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