| Description |
Xylan is the major constituent of hemi cellulose. Several enzymes are needed to hydrolyse xylan completely, includingxylanase. Currently, there is an increasing use of this enzyme. This study was carried out to characterize the xylanasefrom Streptomyces spp. strain C1-3. Results showed that the xylanase displayed its highest activity at pH 3 and 90 oC and wasstable up to 10 hours at this conditions. Its activity increased after the addition of Cu2+, Fe2+, and Co2+ under concentrationof 1 and 5 mM, respectively. The activity however, decreased after the addition of Mg2+, Ca2+ at 1 mM and Zn2+ at 5 mM.After a test with five kinds of xylan (i.e. from Birchwood, Beechwood, Arabinoxylan, Oat spelt and CMC), the xylanase ofStreptomyces spp. C1-3 showed its preferences to Birchwood- and Arabino-xylan. The results showed that the xylanase ofStreptomyces spp. C1-3 was characterized as a thermostable acid xylanase.
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