Purification and some properties of a chitinase from Xanthomonas sp strainAK

Citation
H. Yamaoka et al., Purification and some properties of a chitinase from Xanthomonas sp strainAK, J BIOSCI BI, 88(3), 1999, pp. 328-330
Citations number
14
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
ISSN journal
13891723 → ACNP
Volume
88
Issue
3
Year of publication
1999
Pages
328 - 330
Database
ISI
SICI code
1389-1723(199909)88:3<328:PASPOA>2.0.ZU;2-G
Abstract
Chitinase B (ChiB) was purified from the culture supernatant of Xanthomonas sp. strain AIC by Phenyl-Togopearl 650M and DEAE-Toyopearl 650M column chr omatographies. The purified enzyme preparation gave a single band on SDS-po lyacrylamide gel electrophoresis and the molecular weight of ChiB was estim ated to be 48,000. The enzyme was optimally active at pH 6.0 and 60 degrees C. N-Terminal amino acid sequence analysis suggested that ChiB is a member of glycosyl hydrolase family 18 and that it is genetically different from ChiA recently reported (Sakka et al., J. Ferment. Bioeng., 86, 527-533, 199 8). Immunological analysis suggested that ChiB was the major chitinase spec ies in the culture supernatant of Xanthomonas sp. strain Ag and that produc tion of the enzyme was induced by the presence of chitin.