We were investigating lignin degradation by the bacterium Lignumus decaderum in

Question

We were investigating lignin degradation by the bacterium Lignumus decaderum in the lab which was isolated from rotting piece oak. The genomic sequence of this bacterium has not yet been determined. The addition of a small quantity of hydrogen peroxide induces production of an enzyme that enables the organism to degrade lignin. Zymography has revealed that a single form of the enzyme is present in cultures grown under solid-state fermentation conditions. The enzyme was puried and was found to catalyzes C-C bond cleavage in the side chains of lignin but is unable to do so without added H2O2. When the enzyme preparation is added to pure cellulose under similar reaction conditions, hydrogen peroxide is consumed but to a lesser degree than when lignin is used as substrate. Interestingly, you find that bubbling pure oxygen into the cultures does not result in any enzyme activity against either lignin or cellulose.


What type of enzyme have you discovered? And what is the rationelle for it?

Explanation / Answer

There is a class of ligninolytic enzymes that are h2o2 dependent, called lignin peroxidase. These enzymes use hydrogen peroxide as an elecron donor to activate the catalyst of the C-C bond in lignin... These enzymes are normally found in fungi, but have been isolate as an extracellular product in some bacteria... there are several articals about it... http://www.ncbi.nlm.nih.gov/pmc/articles/PMC204427/ check it out!

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