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KMID : 0364819930310010063
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Korean Journal of Microbiology
1993 Volume.31 No. 1 p.63 ~ p.71
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Purification and Characterization of Xylanase I from Trichoderma koningii ATCC 26113
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Kim Hyun-Ju
Kang Sa-Ouk
Hah Yung-Chil
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Abstract
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A xylanase (xylanase 1) was purified 11.9-fold from the culture filtrate of Trichoderma koningii ATCC 26113 by the column chromatography on Sephadex G-75, SP-Sephadex C-50, DEAESephadex A-50 and Sephadex G-50 with an overall yield of 8.2%. The molecular mass determined by gel filtration and sodium dodecyl sulfate polyacrylamide gel electrophoresis was found to be a monomeric polypeptide of ca. 35 kDa. The isoelectric point of the enzyme was estimated to be 93. The optimal reaction pH and temperature are 5.8 and 55°C, respectively. The enzyme is stable up to 60°C, while 78% of its activity is lost after the incubation for 10 min at 70°C. The enzyme hydrolyzes xylan with relatively high activity, as well as carboxymethyl cellulose and Avicel. The K. values of the enzyme for oat-spelt xylan, larchwood xylan and Avicel were 3.5, 1.6 and 10.1 mg/ml, respectively. The enzyme hydrolyzed oat-spelt xylan to xylose, xylobiose, xylotriose and arabinoxylobiose, while it degraded larchwood xylan to xylose, xylobiose and xylotriose as the major products. The hydrolysis patterns indicate that xylanase I is endo-enzyme.
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KEYWORD
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Trichoderma koningii, xylanase I, endo-xylanase
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