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

Publication ,  Journal Article
Rajakumara, E; Acharya, P; Ahmad, S; Shanmugam, VM; Rao, NM; Sankaranarayanan, R
Published in: Acta Crystallogr D Biol Crystallogr
January 2004

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.

Duke Scholars

Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

January 2004

Volume

60

Issue

Pt 1

Start / End Page

160 / 162

Location

United States

Related Subject Headings

  • Point Mutation
  • Lipase
  • Hydrogen-Ion Concentration
  • Hot Temperature
  • Enzyme Stability
  • Directed Molecular Evolution
  • Crystallography, X-Ray
  • Crystallization
  • Biophysics
  • Bacterial Proteins
 

Citation

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ICMJE
MLA
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Rajakumara, E., Acharya, P., Ahmad, S., Shanmugam, V. M., Rao, N. M., & Sankaranarayanan, R. (2004). Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase. Acta Crystallogr D Biol Crystallogr, 60(Pt 1), 160–162. https://doi.org/10.1107/s0907444903024478
Rajakumara, Eerappa, Priyamvada Acharya, Shoeb Ahmad, Vellaiah M. Shanmugam, Nalam M. Rao, and Rajan Sankaranarayanan. “Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase.Acta Crystallogr D Biol Crystallogr 60, no. Pt 1 (January 2004): 160–62. https://doi.org/10.1107/s0907444903024478.
Rajakumara E, Acharya P, Ahmad S, Shanmugam VM, Rao NM, Sankaranarayanan R. Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):160–2.
Rajakumara, Eerappa, et al. “Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase.Acta Crystallogr D Biol Crystallogr, vol. 60, no. Pt 1, Jan. 2004, pp. 160–62. Pubmed, doi:10.1107/s0907444903024478.
Rajakumara E, Acharya P, Ahmad S, Shanmugam VM, Rao NM, Sankaranarayanan R. Crystallization and preliminary X-ray crystallographic investigations on several thermostable forms of a Bacillus subtilis lipase. Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):160–162.
Journal cover image

Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

January 2004

Volume

60

Issue

Pt 1

Start / End Page

160 / 162

Location

United States

Related Subject Headings

  • Point Mutation
  • Lipase
  • Hydrogen-Ion Concentration
  • Hot Temperature
  • Enzyme Stability
  • Directed Molecular Evolution
  • Crystallography, X-Ray
  • Crystallization
  • Biophysics
  • Bacterial Proteins