Cargando…
Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110
BACKGROUND AND OBJECTIVES: Lipases are particularly important due to the fact that they specifically hydrolyze acyl glycerol, oils and greases, which is of great interest for different industrial applications. MATERIALST AND METHODS: In this study, several lipase-producing bacteria were isolated fro...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Tehran University of Medical Sciences
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279805/ https://www.ncbi.nlm.nih.gov/pubmed/22347589 |
_version_ | 1782223739905114112 |
---|---|
author | Mobarak-Qamsari, E Kasra-Kermanshahi, R Moosavi-nejad, Z |
author_facet | Mobarak-Qamsari, E Kasra-Kermanshahi, R Moosavi-nejad, Z |
author_sort | Mobarak-Qamsari, E |
collection | PubMed |
description | BACKGROUND AND OBJECTIVES: Lipases are particularly important due to the fact that they specifically hydrolyze acyl glycerol, oils and greases, which is of great interest for different industrial applications. MATERIALST AND METHODS: In this study, several lipase-producing bacteria were isolated from wastewater of an oil processing plant. The strain possessing the highest lipase activity was identified both biochemically and sequencing of 16S rRNA gene. Then we increase lipase activity by improving conditions of production medium. Also, lipase from this strain was preliminarily characterized for use in industrial application. RESULTS: The 16S rRNA sequensing revealed it as a new strain of Pseudomonas aeruginosa and the type strain was KM110. An overall 3-fold enhanced lipase production (0.76 U mL(−1)) was achieved after improving conditions of production medium. The olive oil and peptone was found to be the most suitable substrate for maximum enzyme production. Also the enzyme exhibited maximum lipolytic activity at 45°C where it was also stably maintained. At pH 8.0, the lipase had the highest stability but no activity. It was active over a pH range of 7.0–10.0. The lipase activity was inhibited by Zn(2+) & Cu(2+) (32 and 27%, respectively) at 1mM. The enzyme lost 29% of its initial activity in 1.0% SDS concentration, whereas, Triton X-100, Tween-80 & DMSO did not significantly inhibit lipase activity. CONCLUSIONS: Based on the findings of present study, lipase of P. aeruginosa KM110 is a potential alkaline lipase and a candidate for industrial applications such as detergent, leather and fine chemical industries. |
format | Online Article Text |
id | pubmed-3279805 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Tehran University of Medical Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-32798052012-02-16 Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110 Mobarak-Qamsari, E Kasra-Kermanshahi, R Moosavi-nejad, Z Iran J Microbiol Original Artical BACKGROUND AND OBJECTIVES: Lipases are particularly important due to the fact that they specifically hydrolyze acyl glycerol, oils and greases, which is of great interest for different industrial applications. MATERIALST AND METHODS: In this study, several lipase-producing bacteria were isolated from wastewater of an oil processing plant. The strain possessing the highest lipase activity was identified both biochemically and sequencing of 16S rRNA gene. Then we increase lipase activity by improving conditions of production medium. Also, lipase from this strain was preliminarily characterized for use in industrial application. RESULTS: The 16S rRNA sequensing revealed it as a new strain of Pseudomonas aeruginosa and the type strain was KM110. An overall 3-fold enhanced lipase production (0.76 U mL(−1)) was achieved after improving conditions of production medium. The olive oil and peptone was found to be the most suitable substrate for maximum enzyme production. Also the enzyme exhibited maximum lipolytic activity at 45°C where it was also stably maintained. At pH 8.0, the lipase had the highest stability but no activity. It was active over a pH range of 7.0–10.0. The lipase activity was inhibited by Zn(2+) & Cu(2+) (32 and 27%, respectively) at 1mM. The enzyme lost 29% of its initial activity in 1.0% SDS concentration, whereas, Triton X-100, Tween-80 & DMSO did not significantly inhibit lipase activity. CONCLUSIONS: Based on the findings of present study, lipase of P. aeruginosa KM110 is a potential alkaline lipase and a candidate for industrial applications such as detergent, leather and fine chemical industries. Tehran University of Medical Sciences 2011-06 /pmc/articles/PMC3279805/ /pubmed/22347589 Text en © 2011 Iranian Society of Microbiology & Tehran University of Medical Sciences http://creativecommons.org/licenses/by/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License which allows users to read, copy, distribute and make derivative works for non-commercial purposes from the material, as long as the author of the original work is cited properly. |
spellingShingle | Original Artical Mobarak-Qamsari, E Kasra-Kermanshahi, R Moosavi-nejad, Z Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110 |
title | Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110 |
title_full | Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110 |
title_fullStr | Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110 |
title_full_unstemmed | Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110 |
title_short | Isolation and identification of a novel, lipase-producing bacterium, Pseudomnas aeruginosa KM110 |
title_sort | isolation and identification of a novel, lipase-producing bacterium, pseudomnas aeruginosa km110 |
topic | Original Artical |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3279805/ https://www.ncbi.nlm.nih.gov/pubmed/22347589 |
work_keys_str_mv | AT mobarakqamsarie isolationandidentificationofanovellipaseproducingbacteriumpseudomnasaeruginosakm110 AT kasrakermanshahir isolationandidentificationofanovellipaseproducingbacteriumpseudomnasaeruginosakm110 AT moosavinejadz isolationandidentificationofanovellipaseproducingbacteriumpseudomnasaeruginosakm110 |