Effect of Phanerochaete chrysosporium Produced Protease on Peroxidases
Lu Shi
Abstract
Lu Shi
Abstract
Extracellular protease produced by cells of Phanerochaete chrysosporium has been studied in terms of the decay of lignin peroxidase (LiP) and manganese peroxidase (MnP). The activity of this protease was high when pH was about 7.0, and it mainly accelerated the deactivation of the peroxidases rather than inhibited their production. HgCl2 was showed to be an effective inhibitor of the protease and the inhibition mechanism was similar to that of Protease K inhibition by HgCl2. The activity and stability of ligninase system were improved by addition of HgCl2. The optimal addition amount was 1 μmol/L, and the best adding time was the 5th day after the inoculation.
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Extracellular protease produced by cells of Phanerochaete chrysosporium has been studied in terms of the decay of lignin peroxidase (LiP) and manganese peroxidase (MnP). The activity of this protease was high when pH was about 7.0, and it mainly accelerated the deactivation of the peroxidases rather than inhibited their production. HgCl2 was showed to be an effective inhibitor of the protease and the inhibition mechanism was similar to that of Protease K inhibition by HgCl2. The activity and stability of ligninase system were improved by addition of HgCl2. The optimal addition amount was 1 μmol/L, and the best adding time was the 5th day after the inoculation.
Key concepts: Phanerochaete, Peroxidase, Chrysosporium, Protease, Manganese peroxidase, Chemistry, Extracellular, Biochemistry