Manganese Peroxidase Catalyzed Bleaching of Kraft Pulps, 1997 Biological Sciences Symposium Proceedings

In 1993, we found that manganese peroxidase (MnP) was produced by Trametes versicolor cultures during pulp bleaching, and that isolated enzyme supplied with sufficient hydrogen peroxide and chelator could delignify kraft pulp. Subsequently, we applied the enzyme to oxygen-delignified pulps, and found that totally chlorine tree pulp could be produced with a lo-point brightness gain when MnP was included prior to conventional chemical chelation and peroxide brightening. Chelated Mn(II1) is a versatile oxidant and many of the variables associated with delignification, such as chelator type and concentration, have now been optimized. We conclude that MnP-catalyzed bleaching shows potential, although enzyme costs are still unknown.

Author: Paice, M.G., Archibald, F.S., Bourbonnais, R., Reid, I.D., Renaud, S.
Manganese Peroxidase Catalyzed Bleaching of Kraft Pulps, 199
Manganese Peroxidase Catalyzed Bleaching of Kraft Pulps, 1997 Biological Sciences Symposium Proceedings
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