The value of microbial diversity.

In the past few years, due to the use of molecular methods, our knowledge of microbial diversity has increased dramatically, not only from a phylogenetic and taxonomic perspective but also from an ecological basis. We now know that microorganisms exist in every conceivable place on Earth, even in extreme environments. Temperature may be the only limitation as to where they can and cannot exist and/or function. As more small subunit rDNA sequence information becomes available there is a real need to start turning the information into knowledge that can be applied to better elucidate and understand structure-function relationships within ecosystems, develop new culturing methods, and discover new products and processes. It has been stated on numerous occasions that the 21(st) century is the century for biology. Within that context, we must address the real value of microbial diversity.

Isolation and characterization of a novel nonheme chloroperoxidase.

Chloroperoxidase, purified from the fermentation of Curvularia inaequalis, had a molecular weight of approximately 240,000 and was composed of 4 subunits of identical molecular weight (Mr 66,000). The enzyme was specific for I-, Br- and Cl-, and inactive toward F-. The optimum pH of the enzyme was centered around 5.0. X-ray fluorescence revealed that the enzyme contained 2.2 atoms of zinc and 0.7 atom of Fe per molecule of protein. The enzyme had no heme-like compound as a prosthetic group, making it the first nonheme chloroperoxidase to be reported. Under oxidative conditions that rapidly inactivated other haloperoxidases, this enzyme was remarkably stable.

Screening for a "new" enzyme in nature: Haloperoxidase production by Death Valley dematiaceous hyphomycetes.

Haloperoxidases are enzymes that have the ability to halogenate a broad range of substrates [10]. To find a biologically produced haloperoxidase that could function at a pH greater than 3.0 and at a temperature greater than 19°C, dematiaceous hyphomycetes were isolated from the Death Valley desert and screened for their ability to produce such an enzyme. A qualitative assay using bromophenol red was employed in situ over a 12-day fermentation period. Several dematiaceous hyphomycetes, such asDreschlera haloides andUlocladium chartarum, produced haloperoxidases that were active in broth culture at 19, 25, and 34°C at pH 7.0 and 8.0.