 BackResearch Article ScienceAsia 22 (1996): 275-284 |doi: 10.2306/scienceasia1513-1874.1996.22.275 PURIFICATION AND PROPERTIES OF XYLANASE FROM PICHIA STIPITISAMORNRAT PHONGDARA AND PONGSATHORN TUMSUWANABSTRACT: A xylanase was purified from the culture medium of Pichia stipitis by chromatography on sephacyl S-300. The purified enzyme showed a pH optimum of 5 and was stable at pH 3-6. A temperature optimum for the activity was 40 oC and was stable up to 40 oC for 30 min. The apparent molecular mass was 43 kDa from SDS-PAGE. The enzyme had a Km of 1.43 mg/ml and Vmax value of 1.54 Department of Biochemistry, Faculty of Science, Prince of songkla University, Hat- Yai, songkla 90112, Thailand. Received June 8, 1996
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mol/min. Activity was inhibited by 10 mM CuH, EDTA and 1% SDS. The hydrolysis pattern on xylan demonstrated that the enzyme is an exo-xylanase which produces xylobiose as a final product.
