Abstract
The zygomycete Rhizopus oryzae sb is a very efficient organism for retting of flax, the initial microbiological step in the process of making linen. An extracellular polygalacturonase, when isolated could perform retting, and therefore probably is the key component in the retting system of R. oryzae. This was purified and characterized. The purified enzyme has a molecular mass of 37,436 Da from mass spectrometric determination, an isoelectric point of 8.4, and has non-methylated polygalacturonic acid as its preferred substrate. Peptide sequences indicate that the enzyme belongs to family 28, in similarity with other polygalacturonases (EC. 3.2.1.15). It contains, however an N-terminal sequence absent in other fungal pectinases, but present in an enzyme from the phytopathogenic bacterium Ralstonia solanacearum. The biochemical background for the superior retting efficiency of R. oryzae sb is discussed.
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Acknowledgements
The Swedish Pulp and Paper Research Foundation supported this work. The Wallenberg Consortium North for Functional Genomics financed the mass spectrometer at AlbaNova University Centre/Royal Institute of Technology. We thank Dr. Evert Karlsson, Uppsala University, for important discussions about separation artifacts.
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Zhang, J., Henriksson, H., Szabo, I.J. et al. The active component in the flax-retting system of the zygomycete Rhizopus oryzae sb is a family 28 polygalacturonase. J IND MICROBIOL BIOTECHNOL 32, 431–438 (2005). https://doi.org/10.1007/s10295-005-0014-y
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DOI: https://doi.org/10.1007/s10295-005-0014-y