Molecular characterization of a beta-1,4-endoglucanase from an endophytic Bacillus pumilus strain

Appl Microbiol Biotechnol. 2005 Jul;68(1):57-65. doi: 10.1007/s00253-004-1740-1. Epub 2004 Nov 6.

Abstract

Endophytes comprise mainly microorganisms that colonize inner plant tissues, often living with the host in a symbiotic manner. Several ecological roles have been assigned to endophytic fungi and bacteria, such as antibiosis to phytopathogenic agents and plant growth promotion. Nowadays, endophytes are viewed as a new source of genes, proteins and biochemical compounds that may be used to improve industrial processes. In this study, the gene EglA was cloned from a citrus endophytic Bacillus strain. The EglA encodes a beta-1,4-endoglucanase capable of hydrolyzing cellulose under in vitro conditions. The predicted protein, EglA, has high homology to other bacterial cellulases and shows a modular structure containing a catalytic domain of the glycosyl hydrolase family 9 (GH9) and a cellulose-binding module type 3 (CBM3). The enzyme was expressed in Escherichia coli, purified to homogeneity, and characterized. EglA has an optimum pH range of 5-8, and remarkable heat stability, retaining more than 85% activity even after a 24-h incubation at pH 6-8.6. This characteristic is an important feature for further applications of this enzyme in biotechnological processes in which temperatures of 50-60 degrees C are required over long incubation periods.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus / enzymology*
  • Cellulase / chemistry*
  • Cellulase / metabolism*
  • Cloning, Molecular
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Protein Conformation
  • Temperature

Substances

  • Cellulase