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Evaluation of Oxalate Decarboxylase and Oxalate Oxidase for Industrial Applications.

Cassland, Pierre LU ; Sjöde, Anders; Winestrand, Sandra; Jönsson, Leif and Nilvebrant, Nils-Olof (2010) In Applied Biochemistry and Biotechnology 161. p.255-263
Abstract
Increased recirculation of process water has given rise to problems with formation of calcium oxalate incrusts (scaling) in the pulp and paper industry and in forest biorefineries. The potential in using oxalate decarboxylase from Aspergillus niger for oxalic acid removal in industrial bleaching plant filtrates containing oxalic acid was examined and compared with barley oxalate oxidase. Ten different filtrates from chemical pulping were selected for the evaluation. Oxalate decarboxylase degraded oxalic acid faster than oxalate oxidase in eight of the filtrates, while oxalate oxidase performed better in one filtrate. One of the filtrates inhibited both enzymes. The potential inhibitory effect of selected compounds on the enzymatic activity... (More)
Increased recirculation of process water has given rise to problems with formation of calcium oxalate incrusts (scaling) in the pulp and paper industry and in forest biorefineries. The potential in using oxalate decarboxylase from Aspergillus niger for oxalic acid removal in industrial bleaching plant filtrates containing oxalic acid was examined and compared with barley oxalate oxidase. Ten different filtrates from chemical pulping were selected for the evaluation. Oxalate decarboxylase degraded oxalic acid faster than oxalate oxidase in eight of the filtrates, while oxalate oxidase performed better in one filtrate. One of the filtrates inhibited both enzymes. The potential inhibitory effect of selected compounds on the enzymatic activity was tested. Oxalate decarboxylase was more sensitive than oxalate oxidase to hydrogen peroxide. Oxalate decarboxylase was not as sensitive to chlorate and chlorite as oxalate oxidase. Up to 4 mM chlorate ions, the highest concentration tested, had no inhibitory effect on oxalate decarboxylase. Analysis of the filtrates suggests that high concentrations of chlorate present in some of the filtrates were responsible for the higher sensitivity of oxalate oxidase in these filtrates. Oxalate decarboxylase was thus a better choice than oxalate oxidase for treatment of filtrates from chlorine dioxide bleaching. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Applied Biochemistry and Biotechnology
volume
161
pages
255 - 263
publisher
Humana Press
external identifiers
  • wos:000275455000024
  • pmid:19763895
  • scopus:77952998413
ISSN
1559-0291
DOI
10.1007/s12010-009-8769-7
language
English
LU publication?
yes
id
900539e9-7b8f-4956-8a76-d8f76f09e317 (old id 1483358)
date added to LUP
2009-10-13 08:51:37
date last changed
2018-05-29 10:29:15
@article{900539e9-7b8f-4956-8a76-d8f76f09e317,
  abstract     = {Increased recirculation of process water has given rise to problems with formation of calcium oxalate incrusts (scaling) in the pulp and paper industry and in forest biorefineries. The potential in using oxalate decarboxylase from Aspergillus niger for oxalic acid removal in industrial bleaching plant filtrates containing oxalic acid was examined and compared with barley oxalate oxidase. Ten different filtrates from chemical pulping were selected for the evaluation. Oxalate decarboxylase degraded oxalic acid faster than oxalate oxidase in eight of the filtrates, while oxalate oxidase performed better in one filtrate. One of the filtrates inhibited both enzymes. The potential inhibitory effect of selected compounds on the enzymatic activity was tested. Oxalate decarboxylase was more sensitive than oxalate oxidase to hydrogen peroxide. Oxalate decarboxylase was not as sensitive to chlorate and chlorite as oxalate oxidase. Up to 4 mM chlorate ions, the highest concentration tested, had no inhibitory effect on oxalate decarboxylase. Analysis of the filtrates suggests that high concentrations of chlorate present in some of the filtrates were responsible for the higher sensitivity of oxalate oxidase in these filtrates. Oxalate decarboxylase was thus a better choice than oxalate oxidase for treatment of filtrates from chlorine dioxide bleaching.},
  author       = {Cassland, Pierre and Sjöde, Anders and Winestrand, Sandra and Jönsson, Leif and Nilvebrant, Nils-Olof},
  issn         = {1559-0291},
  language     = {eng},
  pages        = {255--263},
  publisher    = {Humana Press},
  series       = {Applied Biochemistry and Biotechnology},
  title        = {Evaluation of Oxalate Decarboxylase and Oxalate Oxidase for Industrial Applications.},
  url          = {http://dx.doi.org/10.1007/s12010-009-8769-7},
  volume       = {161},
  year         = {2010},
}