Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase.

Journal Article (Journal Article)

Bacillus subtilis lipase loses activity above pH 10.5 and below pH 6.0. However, at low pH, i.e. below pH 5.0, the lipase acquires remarkable thermostability. Activity was unaltered for 2 h at 323 K at pH 4.0-5.0, although at pH values above 7.0 the activity was lost rapidly within minutes. Circular-dichroism studies indicate significant changes in the tertiary structure of the lipase, whereas the secondary-structural content remained unaltered. To elucidate the structural basis of the enhanced thermostability, three different forms have been crystallized at low pH along with three crystal forms of two thermostable mutants obtained using a directed-evolution approach.

Full Text

Duke Authors

Cited Authors

  • Rajakumara, E; Acharya, P; Ahmad, S; Shanmugam, VM; Rao, NM; Sankaranarayanan, R

Published Date

  • January 2004

Published In

Volume / Issue

  • 60 / Pt 1

Start / End Page

  • 160 - 162

PubMed ID

  • 14684916

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/s0907444903024478


  • eng

Conference Location

  • United States