| Summary: | Purification and characterization mercuric reductase four isolates Streptomyces
(Streptomyces sp. AS1, Streptomyces sp. AS2, Streptomyces sp. AS6, and
Streptomyces sp. BR28) have been investigated. Cell free extract was obtained by
disrupting cells using sea sand at 4 °C and followed by centrifugation. Mercuric
reductase was purified by ammonium sulfat precipitation, dialysis, and
chromatography column (DEAE Sepharose anion column chromatography).
Determination pH and temperature optimum of mercuric reductase activity based
on the number of NADPH2 oxidized to NADP per mg protein per minute by using
a spectrophotometer. Molecular weight mercuric reductase determined using
SDS-PAGE. The result showed spesific activity of mercuric reductase
Streptomyces sp. BR28 was the highest. The optimum pH and temperature cellfree
extract enzyme mercuric reductase were 7,5 and 80 °C, respectively. The
enzyme was purified to 431,87-fold with spesific activity 21918,95 U/mg protein.
SDS PAGE showed that Streptomyces sp. BR 28 has mercuric reductase. It can be
concluded that Streptomyces isolates have mercuric reductase and be potential as a
bioremediation agent.
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