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Thermostabilization of an esterase by alignment-guided focussed directed evolution

Helge Jochens, Dirk Aerts UGent and Uwe Bornscheuer (2010) PROTEIN ENGINEERING DESIGN & SELECTION. 23(12). p.903-909
abstract
Site-saturation libraries of the Pseudomonas fluorescens esterase were created targeting three surface positions to increase its thermostability on the basis of the B-factor iterative test principle. All three positions were saturated simultaneously using our recently developed protocol for the design of 'small, but smart' mutant libraries bearing only consensus-like mutations. Hence, the library size could be significantly reduced while ensuring a high hit rate. Variants could be identified that showed significantly improved stability (8 degrees C higher compared with the wild type) without compromising specific activity. Subsequent iterative saturation mutagenesis gave an esterase mutant with a 9 degrees C increased melting point, but unchanged catalytic properties.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
site-saturation mutagenesis, thermostability, Pseudomonas fluorescens esterase, directed evolution, B-FIT, DESIGN, RESIDUES, HYDROLASE, DEHYDROGENASE, STABILIZATION, ENANTIOSELECTIVITY, ENZYME STABILITY, PSEUDOMONAS-FLUORESCENS, PROTEIN STABILITY
journal title
PROTEIN ENGINEERING DESIGN & SELECTION
Protein Eng. Des. Sel.
volume
23
issue
12
pages
903 - 909
Web of Science type
Article
Web of Science id
000284167400002
JCR category
BIOTECHNOLOGY & APPLIED MICROBIOLOGY
JCR impact factor
3.023 (2010)
JCR rank
47/158 (2010)
JCR quartile
2 (2010)
ISSN
1741-0126
DOI
10.1093/protein/gzq071
language
English
UGent publication?
yes
classification
A1
copyright statement
I have retained and own the full copyright for this publication
id
1891142
handle
http://hdl.handle.net/1854/LU-1891142
date created
2011-08-21 17:01:08
date last changed
2016-12-19 15:46:39
@article{1891142,
  abstract     = {Site-saturation libraries of the Pseudomonas fluorescens esterase were created targeting three surface positions to increase its thermostability on the basis of the B-factor iterative test principle. All three positions were saturated simultaneously using our recently developed protocol for the design of 'small, but smart' mutant libraries bearing only consensus-like mutations. Hence, the library size could be significantly reduced while ensuring a high hit rate. Variants could be identified that showed significantly improved stability (8 degrees C higher compared with the wild type) without compromising specific activity. Subsequent iterative saturation mutagenesis gave an esterase mutant with a 9 degrees C increased melting point, but unchanged catalytic properties.},
  author       = {Jochens, Helge and Aerts, Dirk and Bornscheuer, Uwe},
  issn         = {1741-0126},
  journal      = {PROTEIN ENGINEERING DESIGN \& SELECTION},
  keyword      = {site-saturation mutagenesis,thermostability,Pseudomonas fluorescens esterase,directed evolution,B-FIT,DESIGN,RESIDUES,HYDROLASE,DEHYDROGENASE,STABILIZATION,ENANTIOSELECTIVITY,ENZYME STABILITY,PSEUDOMONAS-FLUORESCENS,PROTEIN STABILITY},
  language     = {eng},
  number       = {12},
  pages        = {903--909},
  title        = {Thermostabilization of an esterase by alignment-guided focussed directed evolution},
  url          = {http://dx.doi.org/10.1093/protein/gzq071},
  volume       = {23},
  year         = {2010},
}

Chicago
Jochens, Helge, Dirk Aerts, and Uwe Bornscheuer. 2010. “Thermostabilization of an Esterase by Alignment-guided Focussed Directed Evolution.” Protein Engineering Design & Selection 23 (12): 903–909.
APA
Jochens, H., Aerts, D., & Bornscheuer, U. (2010). Thermostabilization of an esterase by alignment-guided focussed directed evolution. PROTEIN ENGINEERING DESIGN & SELECTION, 23(12), 903–909.
Vancouver
1.
Jochens H, Aerts D, Bornscheuer U. Thermostabilization of an esterase by alignment-guided focussed directed evolution. PROTEIN ENGINEERING DESIGN & SELECTION. 2010;23(12):903–9.
MLA
Jochens, Helge, Dirk Aerts, and Uwe Bornscheuer. “Thermostabilization of an Esterase by Alignment-guided Focussed Directed Evolution.” PROTEIN ENGINEERING DESIGN & SELECTION 23.12 (2010): 903–909. Print.