Lignin peroxidase, Phanerochaete

Lignin peroxidase Phanerochaete 3.0 Veratryl alcohol oxidation [10-12]... 

Lignin peroxidase Phanerochaete NaN3, KCN, EDTA, Each at 1 mM [11,79]... 

Kersten PJ (1990) Glyoxal oxidase of Phanerochaete chrysosporium its characterization and activation by lignin peroxidase. Proc Natl Acad Sci USA 87 2936-2940. 

Expression of lignin peroxidases in Phanerochaete chtysosporium is induced by nitrogen-limitation, and by the concentration of Mn (11) in the medium (Perez and Jeffries 1990). 

The inclusion of nitrate may lead to various complications, which have been discussed in Chapter 2. In addition, the nitrogen status of the growth medium determines the levels of lignin peroxidases and manganese-dependent peroxidases that are synthesized in Phanerochaete chrysosporium. The role of Mn concentration is noted later and in Chapter 3, Part 5. 

Van der Woude MW, K Boominathan, CA Reddy (1993) Nitrogen regulation of lignin peroxidase and manganese-dependent peroxidase production is independent of carbon and manganese regulation in Phanerochaete chrysosporium. Arch Microbiol 160 1-4. 

Tatarko M, JA Bumpus (1993) Biodegradation of phenanthrene by Phanerochaete chrysporium on the role of lignin peroxidase. Lett Appl Microbiol 17 20-24. 

The degradation of chlorinated phenols has been examined with the white-rot basidiomy-cete Phanerochaete chrysosporium under conditions of nitrogen limitation, and apparently involves both lignin peroxidase and manganese-dependent peroxidase activities (Valli and Gold 1991). 

Pieper DH, R Winkler, H Sandermann (1992) Eormation of a toxic dimerization product of 3,4-dichloroani-line by lignin peroxidase from Phanerochaete chrysosporium. Angewandte Chemie 104 60-61. 

Bumpus JA, M Tatarko (1994) Biodegradation of 2,4,6-trinitrotoluene by Phanerochaete chrysosporium identification of initial degradation products and the discovery of a metabolite that inhibits lignin peroxidases. Curr Microbiol 28 185-190. 

Haapala A, Linko S (1993) Production of Phanerochaete chrysosporium lignin peroxidase under various culture conditions. Appl Microbiol Biotechnol 40 494-498... 

Nakamura Y, Sawada T, Sungusi MG, Kobayashi F, Kuwahara M, Ito H (1997) Lignin peroxidase production by Phanerochaete chrysosporium. J Chem Eng Jpn 30 1-6... 

Lignin peroxidase, secreted by the white-rot fungus Phanerochaete chrysosporium in response to nutrient deprivation, catalyzes the H202-dependent oxidation of non-phenolic aromatic substrates. The present report summarizes the kinetic and structural characteristics of lignin peroxidase isozymes. Our results indicate that the active site of lignin peroxidase is more electron deficient than other peroxidases. As a result, the redox potential of the heme active site is higher, the heme active site is more reactive and the oxycomplex is more stable than that of other peroxidases. Also discussed is the heme-linked ionization of lignin peroxidase. 

Production of Lignin Peroxidase. Medium for the inoculum was rich in yeast extract (25 g/1) and glucose (25 g/l) to promote maximal growth of the mycelia. The inoculum of Phanerochaete chrysosporium ATCC 24725 was first cultivated for 3 days at 30°C in five litres of medium divided in five shake flasks. The shake flask batches were transferred to a 100 litre bioreactor and cultivated again for 3 days at 30°C. The batches were stirred and aerated to obtain maximal growth of mycelia. 

Figure 1. 3-0-4 lignin substructure model compounds and products of their degradation by ligninolytic cultures of Phanerochaete chrysosporium and by lignin peroxidase. D H, and 0 of 3-ether bond and of H2 0, respectively. B and C show results of stable isotope experiments. 

Table L Correlation of Manganese Regulated Lignin Peroxidase and Mn -dependent Peroxidase Activities with Lignin Biodegradation for Phanerochaete chrysosporium and Lentinula edodes ...

Michel, F.C.J. Dass, S.B. Grulke, E.A. Reddy, C.A. Role of manganese peroxidases (MNP) and lignin peroxidases (LiP) of Phanerochaete chrysosporium in the decolorization of Kraft bleach plant effluent. Appl. Environ. Microbiol. 1991, 57, 2368-2375. 

Lignin peroxidase of Phanerochaete chrysosporium catalyzes the ring cleavage of /3-0-4 lignin substructure model compounds and synthetic lignin (DHP). A mechanism for the ring cleavage by the enzyme is described. 

Feijoo, G., Dosoretz, C., and Lerna, J.M., Production of lignin peroxidase from Phanerochaete chrysosporium in a packed bed bioreactor with recycling, Biotechnol.-Tech. 1994 vol. 8, no. 5, pp. 363-368. 

While the batch process is the dominant one in current use, researchers and companies have attempted to create continuous bioreactor systems. Lopez et al. immobilized Candida rugosa in polymethacrylamide hydrazide beads and polyurethane foam 3 with the intent to achieve the continuous production of lipase enzymes. Despite flow problems with the polyurethane foam, it showed high lipolytic activity. Biomass buildup was problematic. Feijoo et al. immobilized Phanerochaete chry-sosporium on polyurethane foam in packed bed bioreactors under near-plug flow conditions. Continuous lignin peroxidase production was accomplished, the rate of which was studied as a function of recycle ratio. 

Interestingly, phenanthrene, which is not a substrate for lignin peroxidase, is metabolized by Phanerochaete chrysosporium at the C-9 and C-10 positions to give... 

Michels, J. Gottschalk, G. (1994). Inhibition of the lignin peroxidase of Phanerochaete chrysosporium by the hydroxylaminodinitrotoluene intermediate in the degradation of... 

Because the three-dimensional structures of the peroxidase, its reductant cytochrome c, and the complex of the two (Fig. 16-9) are known, cytochrome c peroxidase is the subject of much experimental study. Other fungal peroxidases, some of which contain manganese rather than iron, act to degrade lignin (Chapter 25).218 A lignin peroxidase from the white wood-rot fungus Phanerochaete chrysosporium has a surface tryptophan with a specifically hydroxylated C(3 carbon atom which may have a functional role in catalysis.2183 0... 

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