title: Differential scanning calorimetry of the irreversible thermal denaturation of cellulase from Streptomyces halstedii JM8.
abstract: High-sensitivity differential scanning calorimetry has been applied to characterize the irreversible thermal denaturation of a cellulase, assuming that thermal denaturation takes place according to the kinetic scheme N-k-->D, where k is a first-order kinetic constant that changes with temperature, as given by the Arrhenius equation; N the native state, and D the denatured one. On the basis of this model, the values of the rate constant as a function of temperature and the activation energy were calculated. The analytical data obtained with the fluorescence method as well by measurement of the enzymatic activity temperature dependence support this two-state kinetic model.
authors.affiliation: Instituto de Microbiologia Bioquimica, Consejo Superior de Investigaciones Cientificas - Universidad de Salamanca, Spain.
authors.forename: A L
authors.initials: AL
authors.lastname: Garda-Salas
authors.forename: R I
authors.initials: RI
authors.lastname: Santamaria
authors.forename: M J
authors.initials: MJ
authors.lastname: Marcos
authors.forename: G G
authors.initials: GG
authors.lastname: Zhadan
authors.forename: E
authors.initials: E
authors.lastname: Villar
authors.forename: V L
authors.initials: VL
authors.lastname: Shnyrov
mesh_terms: D002152:Calorimetry, Differential Scanning; D002266:Carboxymethylcellulose Sodium / Q000378:metabolism; D002480:Cellulase / Q000737:chemistry* / Q000378:metabolism; D005453:Fluorescence; D005947:Glucose / Q000032:analysis / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011489:Protein Denaturation; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature; D013816:Thermodynamics
chemical_list: D002480:Cellulase; D005947:Glucose; D002266:Carboxymethylcellulose Sodium