Two possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation
Epiphytic bacteria from marine macroalgae synthesize enzymes of industrial and biotechnological interest. In this study, we obtained two DNA candidate fragments for lipid-degrading enzymes from the total DNA of Ulva lactuca-associated epiphytic bacteria. First, we evaluated a method for total ba...
Guardado en:
Autor principal: | |
---|---|
Formato: | article |
Lenguaje: | EN ES |
Publicado: |
Pontificia Universidad Javeriana
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/1b4b40d9736a4faca8c63bb122e99d55 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:1b4b40d9736a4faca8c63bb122e99d55 |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:1b4b40d9736a4faca8c63bb122e99d552021-11-16T20:16:09ZTwo possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation10.11144/Javeriana.SC25-2.tpce0122-74832027-1352https://doaj.org/article/1b4b40d9736a4faca8c63bb122e99d552020-07-01T00:00:00Zhttps://revistas.javeriana.edu.co/index.php/scientarium/article/view/25583https://doaj.org/toc/0122-7483https://doaj.org/toc/2027-1352Epiphytic bacteria from marine macroalgae synthesize enzymes of industrial and biotechnological interest. In this study, we obtained two DNA candidate fragments for lipid-degrading enzymes from the total DNA of Ulva lactuca-associated epiphytic bacteria. First, we evaluated a method for total bacterial DNA isolation from the surface of U. lactuca thalli. Then, we designed sets of primers and used them directly for PCR amplification. The resulting PCR products were sequence-analyzed and used for expression and functional evaluation with the Escherichia coli pBAD-TOPO system. We obtained high molecular weight and good quality total bacterial DNA that served as a template to identify a fragment corresponding to an Acetyl-CoA C-Acetyltransferase (or Thiolase), and a candidate fragment for a versatile “true” lipase. We expressed the possible “true” lipase gene fragment heterologously in Escherichia coli and obtained proof of hydrolytic activity on Tributyrin, Tween-20, and Olive-oil media. This study resulted in new knowledge on U. lactuca-associated epiphytic bacteria as possible brand-new sources of enzymes such as thiolases and “true” lipases. However, future studies are required to describe the characteristics and important applications of these candidate enzymes.Ruiz-Toquica Jordan Steven, Comba-González Natalia Beatriz, Montoya-Castaño DollyPontificia Universidad Javerianaarticleepiphytic bacteria; lipases; pcr; thiolases; ulva lactuca.Science (General)Q1-390ENESUniversitas Scientiarum, Vol 25, Iss 2, Pp 247-275 (2020) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN ES |
topic |
epiphytic bacteria; lipases; pcr; thiolases; ulva lactuca. Science (General) Q1-390 |
spellingShingle |
epiphytic bacteria; lipases; pcr; thiolases; ulva lactuca. Science (General) Q1-390 Ruiz-Toquica Jordan Steven, Comba-González Natalia Beatriz, Montoya-Castaño Dolly Two possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation |
description |
Epiphytic bacteria from marine macroalgae synthesize enzymes of
industrial and biotechnological interest. In this study, we obtained two
DNA candidate fragments for lipid-degrading enzymes from the total
DNA of Ulva lactuca-associated epiphytic bacteria. First, we evaluated a
method for total bacterial DNA isolation from the surface of U. lactuca
thalli. Then, we designed sets of primers and used them directly for
PCR amplification. The resulting PCR products were sequence-analyzed
and used for expression and functional evaluation with the Escherichia
coli pBAD-TOPO system. We obtained high molecular weight and
good quality total bacterial DNA that served as a template to identify
a fragment corresponding to an Acetyl-CoA C-Acetyltransferase (or
Thiolase), and a candidate fragment for a versatile “true” lipase. We
expressed the possible “true” lipase gene fragment heterologously in
Escherichia coli and obtained proof of hydrolytic activity on Tributyrin,
Tween-20, and Olive-oil media. This study resulted in new knowledge
on U. lactuca-associated epiphytic bacteria as possible brand-new sources
of enzymes such as thiolases and “true” lipases. However, future studies
are required to describe the characteristics and important applications of
these candidate enzymes. |
format |
article |
author |
Ruiz-Toquica Jordan Steven, Comba-González Natalia Beatriz, Montoya-Castaño Dolly |
author_facet |
Ruiz-Toquica Jordan Steven, Comba-González Natalia Beatriz, Montoya-Castaño Dolly |
author_sort |
Ruiz-Toquica Jordan Steven, Comba-González Natalia Beatriz, Montoya-Castaño Dolly |
title |
Two possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation |
title_short |
Two possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation |
title_full |
Two possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation |
title_fullStr |
Two possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation |
title_full_unstemmed |
Two possible candidate enzymes from Ulva lactuca-associated epiphytic bacteria obtained through PCR and functional evaluation |
title_sort |
two possible candidate enzymes from ulva lactuca-associated epiphytic bacteria obtained through pcr and functional evaluation |
publisher |
Pontificia Universidad Javeriana |
publishDate |
2020 |
url |
https://doaj.org/article/1b4b40d9736a4faca8c63bb122e99d55 |
work_keys_str_mv |
AT ruiztoquicajordanstevencombagonzaleznataliabeatrizmontoyacastanodolly twopossiblecandidateenzymesfromulvalactucaassociatedepiphyticbacteriaobtainedthroughpcrandfunctionalevaluation |
_version_ |
1718426033674256384 |