Biochemical studies on a versatile esterase that is most catalytically active with polyaromatic esters. Issue 2 (13th January 2014)
- Record Type:
- Journal Article
- Title:
- Biochemical studies on a versatile esterase that is most catalytically active with polyaromatic esters. Issue 2 (13th January 2014)
- Main Title:
- Biochemical studies on a versatile esterase that is most catalytically active with polyaromatic esters
- Authors:
- Martínez‐Martínez, Mónica
Lores, Iván
Peña‐García, Carlina
Bargiela, Rafael
Reyes‐Duarte, Dolores
Guazzaroni, María‐Eugenia
Peláez, Ana Isabel
Sánchez, Jesús
Ferrer, Manuel - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>Herein, we applied a community genomic approach using a naphthalene‐enriched community (CN1) to isolate a versatile esterase (CN1E1) from the α/β‐hydrolase family. The protein shares low‐to‐medium identity (≤ 57%) with known esterase/lipase‐like proteins. The enzyme is most active at 25–30°C and pH 8.5; it retains approximately 55% of its activity at 4°C and less than 8% at ≥ 55°C, which indicates that it is a cold‐adapted enzyme. CN1E1 has a distinct substrate preference compared with other α/β‐hydrolases because it is catalytically most active for hydrolysing polyaromatic hydrocarbon (phenanthrene, anthracene, naphthalene, benzoyl, protocatechuate and phthalate) esters (7200–21 000 units g<sup>−1</sup> protein at 40°C and pH 8.0). The enzyme also accepts 44 structurally different common esters with different levels of enantio‐selectivity (1.0–55 000 units g<sup>−1</sup> protein), including (±)‐menthyl‐acetate, (±)‐neomenthyl acetate, (±)‐pantolactone, (±)‐methyl‐mandelate, (±)‐methyl‐lactate and (±)‐glycidyl 4‐nitrobenzoate (in that order). The results provide the first biochemical evidence suggesting that such broad‐spectrum esterases may be an ecological advantage for bacteria that mineralize recalcitrant pollutants (including oil refinery products, plasticizers and pesticides) as carbon sources under pollution pressure. They also offer a new tool for the stereo‐assembly (i.e. through ester bonds) of<abstract abstract-type="main"> <title>Summary</title> <p>Herein, we applied a community genomic approach using a naphthalene‐enriched community (CN1) to isolate a versatile esterase (CN1E1) from the α/β‐hydrolase family. The protein shares low‐to‐medium identity (≤ 57%) with known esterase/lipase‐like proteins. The enzyme is most active at 25–30°C and pH 8.5; it retains approximately 55% of its activity at 4°C and less than 8% at ≥ 55°C, which indicates that it is a cold‐adapted enzyme. CN1E1 has a distinct substrate preference compared with other α/β‐hydrolases because it is catalytically most active for hydrolysing polyaromatic hydrocarbon (phenanthrene, anthracene, naphthalene, benzoyl, protocatechuate and phthalate) esters (7200–21 000 units g<sup>−1</sup> protein at 40°C and pH 8.0). The enzyme also accepts 44 structurally different common esters with different levels of enantio‐selectivity (1.0–55 000 units g<sup>−1</sup> protein), including (±)‐menthyl‐acetate, (±)‐neomenthyl acetate, (±)‐pantolactone, (±)‐methyl‐mandelate, (±)‐methyl‐lactate and (±)‐glycidyl 4‐nitrobenzoate (in that order). The results provide the first biochemical evidence suggesting that such broad‐spectrum esterases may be an ecological advantage for bacteria that mineralize recalcitrant pollutants (including oil refinery products, plasticizers and pesticides) as carbon sources under pollution pressure. They also offer a new tool for the stereo‐assembly (i.e. through ester bonds) of multi‐aromatic molecules with benzene rings that are useful for biology, chemistry and materials sciences for cases in which enzyme methods are not yet available.</p> </abstract> … (more)
- Is Part Of:
- Microbial biotechnology. Volume 7:Issue 2(2014:Mar.)
- Journal:
- Microbial biotechnology
- Issue:
- Volume 7:Issue 2(2014:Mar.)
- Issue Display:
- Volume 7, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 7
- Issue:
- 2
- Issue Sort Value:
- 2014-0007-0002-0000
- Page Start:
- 184
- Page End:
- 191
- Publication Date:
- 2014-01-13
- Subjects:
- Microbial biotechnology -- Periodicals
Biotechnology
Microbiology
660.62 - Journal URLs:
- http://ejournals.ebsco.com/direct.asp?JournalID=714890 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1751-7915 ↗
http://www.blackwellpublishing.com/mbt_enhanced/aims.asp ↗
http://www3.interscience.wiley.com/journal/118902527/home ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1751-7915.12107 ↗
- Languages:
- English
- ISSNs:
- 1751-7915
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5756.911050
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4011.xml