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. 1992 Mar;58(3):1070–1072. doi: 10.1128/aem.58.3.1070-1072.1992

Comparison of extracellular peroxidase- and esterase-deficient mutants of Streptomyces viridosporus T7A.

T S Magnuson 1, D L Crawford 1
PMCID: PMC195385  PMID: 1315498

Abstract

Peroxidase-deficient mutants of the lignin-degrading bacterium Streptomyces viridosporus T7A were screened for their production of acid-precipitable polymeric lignin, extracellular peroxidases and esterases, and immunoreactivities against a polyclonal antibody produced against electrophoretically purified peroxidase isoform P3 of wild-type S. viridosporus. The mutants showed diminished abilities to solubilize lignin and produce acid-precipitable polymeric lignin. Their peroxidase activities were decreased, and their esterase production patterns were altered. Western immunoblots demonstrated that the mutants produced proteins immunologically reactive with the antibody, but with different mobilities from those of wild-type proteins. These findings confirm a direct role for peroxidases in lignin solubilization. They also indicate a possible role for esterases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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