Metals and linear alkylbenzene sulphonate as inhibitors of the algae Pseudokirchneriella subcapitata acid phosphatase activity.

dc.contributorCLAUDIO MARTIN JONSSON, CNPMA; LOURIVAL COSTA PARAIBA, CNPMA; HIROSHI AOYAMA, UNICAMP - Instituto de Biologia.
dc.creatorJONSSON, C. M.
dc.creatorPARAIBA, L. C.
dc.creatorAOYAMA, H.
dc.date2016-06-03T12:40:10Z
dc.date2016-06-03T12:40:10Z
dc.date2009-08-20
dc.date2009
dc.date2016-06-03T12:40:10Z
dc.date.accessioned2026-07-07T05:00:42Z
dc.descriptionSewage sludge applied to soils as a fertilizer often contains metals and linear alkylbenzene sulphonate (LAS) as contaminants. These pollutants can be transported to the aquatic environment where they can alter the phosphatase activity in living organisms. The acid phosphatase of algae plays important roles in metabolism such as decomposing organic phosphate into free phosphate and autophagic digestive processes. The order of in vitro inhi- bition of Pseudokirchneriella subcapitata acid phosphatase at the highest concentration tested was LAS[Hg2? = Al 3?[Se4? = Pb2?[Cd2?. A non-competitive inhibi- tion mechanism was obtained for Hg2? (Ki = 0.040 mM) and a competitive inhibition for LAS (Ki = 0.007 mM). In vivo studies with treated algae cultures showed that the inhibition of specific activity was observed in algae exposed during 7 days, in contrast to short term (24 h) treatments with both these chemicals. Our results suggest that the inhibition parameters in vitro did not markedly differ between the two chemicals. On the other hand, in vivo evaluations showed strong differences between both pollu- tants regarding the concentration values and the degree of response.
dc.identifierEcotoxicology, v.18, n.5, p.610-619, 2009.
dc.identifierhttp://www.alice.cnptia.embrapa.br/alice/handle/doc/257015
dc.identifier.urihttp://hdl.handle.net/123456789/477178
dc.languageeng
dc.rightsopenAccess
dc.subjectAlga
dc.subjectFosfatase Ácida
dc.titleMetals and linear alkylbenzene sulphonate as inhibitors of the algae Pseudokirchneriella subcapitata acid phosphatase activity.
dc.typeArtigo de periódico

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