title: Crystallization, solubility and thermodynamics of the highly thermostable glucose isomerase from Streptomyces sp. strain.
abstract: The crystallization behaviour of the highly thermostable glucose isomerase from the Streptomyces sp. strain isolated from Tunisian soil was investigated using ammonium sulfate as a precipitating agent. We established phase diagrams at different temperatures and protein concentrations. It was found that the solubility increased with increasing temperature and decreased with increasing salt concentration. The temperature-dependent solubility was used to characterize the thermodynamic parameters of crystallization such as enthalpy, entropy and free energy.
authors.affiliation: Laboratory of Enzymes and Metabolites of Prokaryotes, CBS, B.P 1177, Sfax, Tunisia. borgima@yahoo.com.
authors.forename: Mohamed A
authors.initials: MA
authors.lastname: Borgi
authors.forename: Moez
authors.initials: M
authors.lastname: Rhimi
authors.forename: Adel
authors.initials: A
authors.lastname: Kadri
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000737:chemistry* / Q000378:metabolism; D055162:Biocatalysis; D003460:Crystallization; D019277:Entropy; D004795:Enzyme Stability; D057927:Hydrophobic and Hydrophilic Interactions; D012988:Soil Microbiology; D012995:Solubility; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature
chemical_list: D019747:Aldose-Ketose Isomerases; C023298:xylose isomerase