Open AccessCharacterization of a chitinase gene ( chiA ) from Serratia marcescens BJL200 and one‐step purification of the gene product
Author(s) -
Brurberg May B.,
Eijsink Vincent G.H.,
Nes Ingolf F.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb07315.x
Subject(s) - serratia marcescens , chitinase , gene , gene product , escherichia coli , biology , biochemistry , nucleic acid sequence , amino acid , peptide sequence , microbiology and biotechnology , chemistry , gene expression
Abstract The nucleotide sequence of the chiA gene from Serratia marcescens strain BJL200 was determined. The gene was found to encode a protein of 563 amino acid residues, with a typical N‐terminal signal peptide of 23 residues, that is cleaved off during export. The gene exhibited striking differences with two previously characterized chiA genes of S. marcescens in the region corresponding to amino acid residues 410–467 of the gene product. Periplasmic fractions of an Escherichia coli strain harbouring the cloned gene were used as starting material for the development of a fast, one‐step purification protocol for the chitinase that is based on hydrophobic interaction chromatography.