Cloning, expression and characterization of a beta-agarase gene from a marine bacterium, Pseudomonas sp. SK38

Biotechnol Lett. 2003 Jul;25(14):1165-70. doi: 10.1023/a:1024586207392.

Abstract

A gene (pagA) encoding beta-agarase from Pseudomonas sp. SK38 was cloned and expressed in Escherichia coli. The structural gene consists of 1011 bp encoding 337 amino acids with a predicted molecular weight of 37326 and has a signal peptide of 18 amino acids. The deduced amino acid sequence showed 57% and 58% homology to beta-agarase from Pseudoalteromonas atalntica and Aeromonas sp., respectively. The recombinant enzyme was purified and biochemically characterized. The enzyme had maximum activity at pH 9 and 30 degrees C. It was stable at pHs from 8 to 9 and below 37 degrees C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA, Bacterial / genetics
  • Escherichia coli / genetics
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial*
  • Glycoside Hydrolases / biosynthesis*
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / genetics*
  • Glycoside Hydrolases / metabolism
  • Molecular Sequence Data
  • Pseudomonas / enzymology
  • Pseudomonas / genetics*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Sequence Homology, Amino Acid

Substances

  • DNA, Bacterial
  • Recombinant Proteins
  • Glycoside Hydrolases
  • agarase