Production and characterization of thermostable xylanase and pectinase from Streptomyces sp QG-11-3

Citation
Qk. Beg et al., Production and characterization of thermostable xylanase and pectinase from Streptomyces sp QG-11-3, J IND MIC B, 24(6), 2000, pp. 396-402
Citations number
36
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
ISSN journal
13675435 → ACNP
Volume
24
Issue
6
Year of publication
2000
Pages
396 - 402
Database
ISI
SICI code
1367-5435(200006)24:6<396:PACOTX>2.0.ZU;2-Q
Abstract
Streptomyces sp. QG-17-3, which produces a cellulase-free thermostable xyla nase (96 IU ml(-1)) and a pectinase (46 IU ml(-1)), was isolated on Horikos hi medium supplemented with 1% w/v wheat bran. Carbon sources that favored xylanase production were rice bran (82 IU ml(-1)) and birch-wood xylan (81 IU ml(-1)); pectinase production was also stimulated by pectin and cotton s eed cake (34 IU ml(-1) each). The partially purified xylanase and pectinase were optimally active at 60 degrees C. Both enzymes were 100% stable at 50 degrees C for more than 24 h. The half-lives of xylanase and pectinase at 70, 75 and 80 degrees C were 90, 75 and 9 min, and 90, 53 and 7 min, respec tively. The optimum pH values for xylanase and pectinase were 8.6 and 3.0, respectively, at 60 degrees C. Xylanase and pectinase were stable over a br oad pi-i range between 5.4 and 9.4 and 2.0 to 9.0, respectively retaining m ore than 85% of their activity. Ca2+ stimulated the activity of both enzyme s up to 7%, whereas Cd2+, Co2+ Cr3+, iodoacetic acid and iodoacetamide inhi bited xylanase up to 35% and pectinase up to 63%; at 1 mM, Hg2+ inhibited b oth enzymes completely.