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Journal : HAYATI Journal of Biosciences

Characterization of Xylanase Streptomyces spp. SKK1-8 ANJA MERYANDINI; TRIO HENDARWIN; DEDEN SAPRUDIN; YULIN LESTARI
HAYATI Journal of Biosciences Vol. 13 No. 4 (2006): December 2006
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (134.007 KB) | DOI: 10.4308/hjb.13.4.151

Abstract

Streptomyces spp. SKK1-8 producing xylanase was isolated from soil sample from Sukabumi West Java. The xylanase have an optimum condition at pH 6 and 50 0C. Addition of 5 mM Cu2+ decreased the xylanase activity up to about 77%, whereas not by other cations. The xylanase was stable at 3 0C for 48 hours, and the enzyme half lifetime was 1 hour 45 minute at 50 0C. This xylanase showed the highest activity on oatspelt xylan, and their molecular masses were estimated approximately 16.80, 15.21, and 13.86 kDa. HPLC analysis showed that xylosa and arabinosa were the main hydrolytic product of birchwood xylan. Key words: xilanase, Streptomyces spp., characterization, zymogram and SDS-PAGE, stability
Characterization of Xylanase from Streptomyces spp. Strain C1-3 ANJA MERYANDINI
HAYATI Journal of Biosciences Vol. 14 No. 3 (2007): September 2007
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (52.565 KB) | DOI: 10.4308/hjb.14.3.115

Abstract

Xylan is the major constituent of hemi cellulose. Several enzymes are needed to hydrolyse xylan completely, including xylanase. Currently, there is an increasing use of this enzyme. This study was carried out to characterize the xylanase from Streptomyces spp. strain C1-3. Results showed that the xylanase displayed its highest activity at pH 3 and 90 0C and was stable up to 10 hours at this conditions. Its activity increased after the addition of Cu2+, Fe2+, and Co2+ under concentration of 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 of Streptomyces spp. C1-3 showed its preferences to Birchwood- and Arabino-xylan. The results showed that the xylanase of Streptomyces spp. C1-3 was characterized as a thermostable acid xylanase. Key words: xylanase, Streptomyces, stability, CMCase