Purification and Characterization of Xylanase from Bacillus sp. A-6
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A xylanase was purified from the culture supernatant of Bacillus sp. A-6 by using ultrafiltration and ion exchange chromatography on the column of SP-Sepharose using 5 mM acetate buffer, pH 5.0. The xylanase was eluted from the column at the concentration less than 0.05 M NaCl. The eluted xylanase was shown to be a single protein band in SDS-PAGE. Zymogram analysis indicated that the protein band in SDS-PAGE had the enzyme activity to hydrolyze oat spelt xylan. The molecular weights of the xylanase were 15,000 based on SDS-PAGE and 14,100 based on gel filtration chromatography. Thin layer chromatography showed that the xylanase hydrolyzed oat spelt xylan into xylobiose and high-molecular-weight xylooligosaccharides. The relative activities of the heated xylanase decreased to 80% at 40℃ after 7 hr and less than 40% at 60℃ after 1 hr.
Abstract
A xylanase was purified from the culture supernatant of Bacillus sp. A-6 by using ultrafiltration and ion exchange chromatography on the column of SP-Sepharose using 5 mM acetate buffer, pH 5.0. The xylanase was eluted from the column at the concentration less than 0.05 M NaCl. The eluted xylanase was shown to be a single protein band in SDS-PAGE. Zymogram analysis indicated that the protein band in SDS-PAGE had the enzyme activity to hydrolyze oat spelt xylan. The molecular weights of the xylanase were 15,000 based on SDS-PAGE and 14,100 based on gel filtration chromatography. Thin layer chromatography showed that the xylanase hydrolyzed oat spelt xylan into xylobiose and high-molecular-weight xylooligosaccharides. The relative activities of the heated xylanase decreased to 80% at 40℃ after 7 hr and less than 40% at 60℃ after 1 hr.
참고문헌 (21)
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