Open Access Research

Hypocrea jecorina CEL6A protein engineering

Suzanne E Lantz1*, Frits Goedegebuur2, Ronald Hommes2, Thijs Kaper1, Bradley R Kelemen1, Colin Mitchinson1, Louise Wallace1, Jerry Ståhlberg3 and Edmundo A Larenas1

Author Affiliations

1 Genencor Division, Danisco USA Inc., 925 Page Mill Rd. Palo Alto, CA 94304, USA

2 Genencor, a Danisco Division, Archimedesweg 30, 2333CN, Leiden, The Netherlands

3 Department of Molecular Biology, Swedish University of Agricultural Sciences, POB 590, SE-751 24 Uppsala, Sweden

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Biotechnology for Biofuels 2010, 3:20  doi:10.1186/1754-6834-3-20

Published: 8 September 2010

Abstract

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 H. jecorina 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 H. jecorina 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.