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Molecular cloning and characterization of a chitosanase from the chitosanolytic bacterium Burkholderia gladioli strain CHB101.
- Source :
-
Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2000 Sep; Vol. 54 (3), pp. 354-60. - Publication Year :
- 2000
-
Abstract
- A chitosanase was purified from the culture fluid of the chitino- and chitosanolytic bacterium Burkholderia gladioli strain CHB101. The purified enzyme (chitosanase A) had a molecular mass of 28 kDa, and catalyzed the endo-type cleavage of chitosans having a low degree of acetylation (0-30%). The enzyme hydrolyzed glucosamine oligomers larger than a pentamer, but did not exhibit any activity toward N-acetylglucosamine oligomers and colloidal chitin. The gene coding for chitosanase A (csnA) was isolated and its nucleotide sequence determined. B. gladioli csnA has an ORF encoding a polypeptide of 355 amino acid residues. Analysis of the N-terminal amino acid sequence of the purified chitosanase A and comparison with that deduced from the csnA ORF suggests post-translational processing of a putative signal peptide and a possible substrate-binding domain. The deduced amino acid sequence corresponding to the mature protein showed 80% similarity to the sequences reported from Bacillus circulans strain MH-K1 and Bacillus ehimensis strain EAG1, which belong to family 46 glycosyl hydrolases.
- Subjects :
- Amino Acid Sequence
Base Sequence
Burkholderia classification
Burkholderia genetics
Chitosan
Cloning, Molecular
Genes, Bacterial
Glycoside Hydrolases chemistry
Glycoside Hydrolases isolation & purification
Kinetics
Molecular Sequence Data
Open Reading Frames
Sequence Alignment
Substrate Specificity
Bacterial Proteins
Burkholderia enzymology
Chitin analogs & derivatives
Chitin metabolism
Glycoside Hydrolases genetics
Glycoside Hydrolases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0175-7598
- Volume :
- 54
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Applied microbiology and biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 11030572
- Full Text :
- https://doi.org/10.1007/s002530000388