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1.
Rev. argent. microbiol ; Rev. argent. microbiol;51(1): 39-46, mar. 2019. ilus
Artigo em Inglês | LILACS | ID: biblio-1003279

RESUMO

Tributyltin (TBT) is recognized as a major environmental problem at a global scale. Haloalkaliphilic tributyltin (TBT)-degrading bacteria may be a key factor in the remediation of TBT polluted sites. In this work, three haloalkaliphilic bacteria strains were isolated from a TBT-contaminated site in the Mediterranean Sea. After analysis of the 16S rRNA gene sequences the isolates were identified as Sphingobium sp. HS1, Stenotrophomonas chelatiphaga HS2 and Rhizobium borbori HS5. The optimal growth conditions for biodegradation of TBT by the three strains were pH 9 and 7% (w/v) salt concentration. S. chelatiphaga HS2 was the most effective TBT degrader and has the ability to transform most TBT into dibutyltin and monobutyltin (DBT and MBT). A gene was amplified from strain HS2 and identified as TBTB-permease-like, that encodes an ArsB-permease. A reverse transcription polymerase chain reaction analysis in the HS2 strain confirmed that the TBTB-permease-like gene contributes to TBT resistance. The three novel haloalkaliphilic TBT degraders have never been reported previously.


Se considera a la tributiltina (TBT) como un problema medioambiental serio a escala global. Las bacterias haloalcalifílicas degradadoras de TBT pueden constituir un factor clave para remediar áreas contaminadas con dicho xenobiótico. En este estudio se aislaron 3 cepas de bacterias haloalcalifílicas procedentes de un sitio contaminado con TBT en el mar Mediterráneo. Tras analizar las secuencias del gen de 16S del ARNr, se identificaron los aislados como Sphingo-bium sp. HS1, Stenotrophomonas chelatiphaga HS2 y Rhizobium borbori HS5. Las condiciones de crecimiento óptimas para la biodegradación de TBT por parte de las 3 cepas fueron pH 9 y 7% (p/v) de concentración de sal. S. chelatiphaga HS2 fue el degradador de TBT más efectivo, con capacidad de transformar la mayor parte de ese compuesto en dibutiltina y monobutiltina (DBT y MBT). Se amplificó un gen de la cepa HS2, que fue identificado como tipo TBTB-permeasa, que codifica para una ArsB permeasa. Un análisis de la cepa HS2 por reacción en cadena de la polimerasa con transcriptasa inversa (RT PCR) confirmó que el gen TBTB-permeasa contribuye a la resistencia al TBT. Estos 3 nuevos degradadores haloalcalifílicos de TBT no habían sido reportados previamente.


Assuntos
Bactérias/isolamento & purificação , Recuperação e Remediação Ambiental/métodos , Biodegradação Ambiental , Mar Mediterrâneo/epidemiologia , Reação em Cadeia da Polimerase/métodos , Transcrição Reversa/genética , /análise
2.
Rev Argent Microbiol ; 51(1): 39-46, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-29605458

RESUMO

Tributyltin (TBT) is recognized as a major environmental problem at a global scale. Haloalkaliphilic tributyltin (TBT)-degrading bacteria may be a key factor in the remediation of TBT polluted sites. In this work, three haloalkaliphilic bacteria strains were isolated from a TBT-contaminated site in the Mediterranean Sea. After analysis of the 16S rRNA gene sequences the isolates were identified as Sphingobium sp. HS1, Stenotrophomonas chelatiphaga HS2 and Rhizobium borbori HS5. The optimal growth conditions for biodegradation of TBT by the three strains were pH 9 and 7% (w/v) salt concentration. S. chelatiphaga HS2 was the most effective TBT degrader and has the ability to transform most TBT into dibutyltin and monobutyltin (DBT and MBT). A gene was amplified from strain HS2 and identified as TBTB-permease-like, that encodes an ArsB-permease. A reverse transcription polymerase chain reaction analysis in the HS2 strain confirmed that the TBTB-permease-like gene contributes to TBT resistance. The three novel haloalkaliphilic TBT degraders have never been reported previously.


Assuntos
Bactérias/metabolismo , Compostos de Trialquitina/metabolismo , Poluentes Químicos da Água/metabolismo , Biodegradação Ambiental , Egito , Concentração de Íons de Hidrogênio , Mar Mediterrâneo , Tolerância ao Sal
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