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  • 1.
    Cassland, Pierre
    et al.
    Applied Microbiology, Lund University/Lund Institute of Technology.
    Sjöde, Anders
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Winestrand, Sandra
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Jönsson, Leif J.
    Karlstad University, Faculty of Technology and Science.
    Nilvebrant, Nils-Olof
    STFI-Packforsk AB, Swedish Pulp and Paper Research Institute, Stockholm.
    Comparison between oxalate decarboxylase and oxalate oxidase in the degradation of oxalic acid in filtrates from the pulp and paper industryManuscript (Other academic)
  • 2.
    Cassland, Pierre
    et al.
    Applied Microbiology, Lund University.
    Sjöde, Anders
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Winestrand, Sandra
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Jönsson, Leif J.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Nilvebrant, Nils-Olof
    Karlstad University, Faculty of Technology and Science, Department of Chemical Engineering.
    Evaluation of Oxalate Decarboxylase and Oxalate Oxidase for Industrial Applications2010In: Applied Biochemistry and Biotechnology, ISSN 0273-2289, E-ISSN 1559-0291, Vol. 161, p. 255-263Article in journal (Refereed)
  • 3.
    Sjöde, Anders
    et al.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Winestrand, Sandra
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Nilvebrant, Nils-Olof
    STFI-Packforsk AB, Swedish Pulp and Paper Research Institute, Stockholm.
    Jönsson, Leif J.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Enzyme-based control of oxalic acid in the pulp and paper industry2008In: Enzyme and microbial technology, ISSN 0141-0229, E-ISSN 1879-0909, Vol. 43, p. 78-83Article in journal (Refereed)
  • 4.
    Winestrand, Sandra
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Industrial applications and properties of oxalate-degrading enzymes2010Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    Oxalate-degrading enzymes were investigated with focus on potential applications in the pulp and paper industry and in active packaging. Changes introduced to make the pulp and paper industry more environmentally friendly, such as recirculation of process-water streams and elementary chlorine free bleaching of pulp, have led to increasing problems with precipitation of calcium oxalate. The potential of using enzymes for degradation of oxalic acid in industrial bleaching filtrates was explored to find a way to decrease the problem.

    The studies included chemical characterization and enzymatic treatments of 34 filtrates from kraft, mechanical, and sulfite pulping. Eight oxalate-degrading enzymes were included in the experiments. The treatments of the filtrates were affected by substances that inhibit oxalate-degrading enzymes. Multivariate data analysis, analytical treatment of filtrates with ion-exchange resins, and analysis of the effects of separate compounds on the enzyme activity were employed as tools to investigate inhibiting substances and groups of inhibitors. The experiments with ion-exchangers indicated that the inhibitors included anions, cations, as well as uncharged substances. Sulfite (≥1 mM) caused complete or almost complete inhibition of all oxalate-degrading enzymes so far examined, while the effects of chlorine oxyanions differed for the various enzymes investigated. A newly discovered oxalate decarboxylase was chosen for experiments performed directly in a mill producing mechanical pulp. The new enzyme degraded 70% of the oxalic acid in one hour, while the well-characterized oxalate decarboxylase from Aspergillus niger degraded <5% of the oxalic acid during the same period of time.

    Oxalate decarboxylase from the white-rot basidiomycete fungus Trametes versicolor was purified by using chromatographic methods and characterized with gel electrophoresis and tandem mass spectrometry. Results indicate that it is a 69-kDa heavily glycosylated enzyme with optimal activity at pH 2.5.

    Experiments designed to investigate the potential of using oxalate oxidase from barley in active packaging showed that it could be entrapped with retained catalytic activity in a latex-polymer matrix. Furthermore, the experiments indicate that oxalate oxidase can be used in active packaging either as an oxalic acid scavenger or as an oxygen scavenger.

  • 5.
    Winestrand, Sandra
    et al.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Larsson, Simona
    Riga Technical University, Faculty of Civil Engineering, Latvia.
    Cassland, Pierre
    Applied Microbiology, Lund University/Lund Institute of Technology.
    Nilvebrant, Nils-Olof
    Karlstad University, Faculty of Technology and Science.
    Jönsson, Leif J.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Effects of ionic substances in bleaching filtrates and of lignosulfonates on the activity of oxalate oxidase from barley2011In: Engineering in Life Sciences, ISSN 1618-0240, E-ISSN 1618-2863, Vol. 11, no 3, p. 245-252Article in journal (Refereed)
    Abstract [en]

    The effects of ionic substances in seven industrial filtrates from kraft pulping, mechanical pulping, and sulfite pulping on the activity of oxalate oxidase from barley were investigated by pre-treatment of the filtrates with ion-exchange resins prior to enzymatic degradation of the oxalic acid in the filtrates. The pre-treatment resulted in increased oxalic acid degradation rates in all filtrates, except for one that was obtained from sulfite pulping. The possibility that lignosulfonates, which were present in the filtrate from sulfite pulping, could affect oxalate oxidase was investigated in a separate set of experiments involving four different preparations of lignosulfonates. At a lignosulfonate concentration of 50 mg/mL and a pH of 3.8, only 2-16% of the activity of oxalate oxidase remained. The results show the effects of anionic and cationic substances in bleaching filtrates on oxalate oxidase and indicate that there is an interaction between the enzyme, which has a positive net charge at pH 3.8, and the polymeric anionic lignosulfonates.

  • 6.
    Winestrand, Sandra
    et al.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Latha Gandla, Madhavi
    Department of Chemistry, Umeå University.
    Hong, Feng
    College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, China.
    Chen, Qi Zhi
    College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, China.
    Jönsson, Leif J.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Oxalate decarboxylase of Trametes versicolor: biochemical characterization and performance in bleaching filtrates from the pulp and paper industry2012In: Journal of chemical technology and biotechnology (1986), ISSN 0268-2575, E-ISSN 1097-4660, Vol. 87, no 11, p. 1600-1606Article in journal (Refereed)
    Abstract [en]

    BACKGROUND: Oxalate decarboxylase (ODC) from acid-induced cultures of the white-rot fungus Trametes versicolor was purified and characterized with respect to its biochemical properties and the possibility to utilize the enzyme for treatment of process water with the intention to prevent problems with calcium-oxalate scaling in the pulp and paper industry. RESULTS: Purified T. versicolor ODC was identified by tandem mass spectrometry. As estimated by using SDS-PAGE, the molecular mass was 69 kDa, and 60 kDa after deglycosylation with N-glycosidase F. The pH optimum was 2.5 and the temperature optimum was 4045 degrees C. The effects of ten potential inhibitors in industrial filtrates were examined. The enzyme was sensitive to low concentrations (0.1 mmol L-1) of chlorite and sulfite. T. versicolor ODC exhibited activity in 16 filtrates collected from mechanical pulping and kraft pulping. It had higher activity than ODC from Aspergillus niger in all of the filtrates and higher activity than oxalate oxidase from barley in all filtrates except two. CONCLUSIONS: The investigation shows basic biochemical properties of T. versicolor ODC and indicates that the enzyme may be useful for treatment of industrial filtrates under acidic conditions. Copyright (c) 2012 Society of Chemical Industry

  • 7.
    Winestrand, Sandra
    et al.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Nilvebrant, Nils-Olof
    Karlstad University, Faculty of Technology and Science.
    The Effects of Oxyanions on the Activity of Oxalate Oxidase2009In: The Open Enzyme Inhibition Journal, ISSN 1874-9402, Vol. 2, p. 36-40Article in journal (Refereed)
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