<it>Hypocrea jecorina </it>CEL6A protein engineering

<p>Abstract</p> <p>The complex technology of converting lignocellulose to fuels such as ethanol has advanced rapidly over the past few years, and enzymes are a critical component of this technology. The production of effective enzyme systems at cost structures that facilitate comme...

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Main Authors: Lantz Suzanne E, Goedegebuur Frits, Hommes Ronald, Kaper Thijs, Kelemen Bradley R, Mitchinson Colin, Wallace Louise, Ståhlberg Jerry, Larenas Edmundo A
Format: Article
Language:English
Published: BMC 2010-09-01
Series:Biotechnology for Biofuels
Online Access:http://www.biotechnologyforbiofuels.com/content/3/1/20
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spelling doaj-f02d4dfeb530456db1122af00f2cf2f62020-11-25T00:04:25ZengBMCBiotechnology for Biofuels1754-68342010-09-01312010.1186/1754-6834-3-20<it>Hypocrea jecorina </it>CEL6A protein engineeringLantz Suzanne EGoedegebuur FritsHommes RonaldKaper ThijsKelemen Bradley RMitchinson ColinWallace LouiseStåhlberg JerryLarenas Edmundo A<p>Abstract</p> <p>The complex technology of converting lignocellulose to fuels such as ethanol has advanced rapidly over the past few years, and enzymes are a critical component of this technology. The production of effective enzyme systems at cost structures that facilitate commercial processes has been the focus of research for many years. Towards this end, the <it>H. jecorina </it>cellobiohydrolases, CEL7A and CEL6A, have been the subject of protein engineering at Genencor. Our first rounds of cellobiohydrolase engineering were directed towards improving the thermostability of both of these enzymes and produced variants of CEL7A and CEL6A with apparent melting temperatures above 70°C, placing their stability on par with that of <it>H. jecorina </it>CEL5A (EG2) and CEL3A (BGL1). We have now moved towards improving CEL6A- and CEL7A-specific performance in the context of a complete enzyme system under industrially relevant conditions. Achievement of these goals required development of new screening strategies and tools. We discuss these advances along with some results, focusing mainly on engineering of CEL6A.</p> http://www.biotechnologyforbiofuels.com/content/3/1/20
collection DOAJ
language English
format Article
sources DOAJ
author Lantz Suzanne E
Goedegebuur Frits
Hommes Ronald
Kaper Thijs
Kelemen Bradley R
Mitchinson Colin
Wallace Louise
Ståhlberg Jerry
Larenas Edmundo A
spellingShingle Lantz Suzanne E
Goedegebuur Frits
Hommes Ronald
Kaper Thijs
Kelemen Bradley R
Mitchinson Colin
Wallace Louise
Ståhlberg Jerry
Larenas Edmundo A
<it>Hypocrea jecorina </it>CEL6A protein engineering
Biotechnology for Biofuels
author_facet Lantz Suzanne E
Goedegebuur Frits
Hommes Ronald
Kaper Thijs
Kelemen Bradley R
Mitchinson Colin
Wallace Louise
Ståhlberg Jerry
Larenas Edmundo A
author_sort Lantz Suzanne E
title <it>Hypocrea jecorina </it>CEL6A protein engineering
title_short <it>Hypocrea jecorina </it>CEL6A protein engineering
title_full <it>Hypocrea jecorina </it>CEL6A protein engineering
title_fullStr <it>Hypocrea jecorina </it>CEL6A protein engineering
title_full_unstemmed <it>Hypocrea jecorina </it>CEL6A protein engineering
title_sort <it>hypocrea jecorina </it>cel6a protein engineering
publisher BMC
series Biotechnology for Biofuels
issn 1754-6834
publishDate 2010-09-01
description <p>Abstract</p> <p>The complex technology of converting lignocellulose to fuels such as ethanol has advanced rapidly over the past few years, and enzymes are a critical component of this technology. The production of effective enzyme systems at cost structures that facilitate commercial processes has been the focus of research for many years. Towards this end, the <it>H. jecorina </it>cellobiohydrolases, CEL7A and CEL6A, have been the subject of protein engineering at Genencor. Our first rounds of cellobiohydrolase engineering were directed towards improving the thermostability of both of these enzymes and produced variants of CEL7A and CEL6A with apparent melting temperatures above 70°C, placing their stability on par with that of <it>H. jecorina </it>CEL5A (EG2) and CEL3A (BGL1). We have now moved towards improving CEL6A- and CEL7A-specific performance in the context of a complete enzyme system under industrially relevant conditions. Achievement of these goals required development of new screening strategies and tools. We discuss these advances along with some results, focusing mainly on engineering of CEL6A.</p>
url http://www.biotechnologyforbiofuels.com/content/3/1/20
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