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Stability of xylanases in the presence of methanol and its evaluation on the bleaching capacity
Authors:J Ruiz  R Angelo  J Freer  J Baeza  C Aguirre  E Curotto  N Durán
Institution:(1) Renewable Resources Laboratory, Department of Chemistry, Universidad de Concepcion-Chile, Chile;(2) Department of Biochemistry, Universidad Catolica de Valparaiso, Chile;(3) Instituto de Química, Biological Chemistry Laboratory, Universidade Estadual de Campinas, C.P.
Abstract:A commercial (Cartazyme) and non-commercial (Asperzyme) xylanases were studied. Cartazyme stability in a 0–70% (v/v) methanol at 50thinsp°C and 65thinsp°C was carried out. No deactivation was found for Cartazyme in the presence of 15% methanol at 50thinsp°C. Half-life activity decay (t1/2) of Cartazyme at 50thinsp°C in 30%, 50% and 70% methanol solutions were 4.0 h, 2.3 h and 1.2 h, respectively. At 65thinsp°C, which is the ozone-alkali-peroxide (ZEP) bleaching temperature, only significant results on Kappa number reduction and selectivity were only observed in 15% methanol (t1/2 30 min) at the Z stage. For the Asperzyme, a t1/2 of 36.5 min at 50thinsp°C was found. In the Z stage with Asperzyme in the presence of 25% of methanol, a 20% Kappa number reduction and an improvement of the ZEP sequence of the brightness of 3.1 points were obtained. These results were correlated with the xylanase stability.
Keywords:bleaching (of paper)  enzyme stability  Kappa number  xylanase
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