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KMID : 0366119740020030133
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Korean Journal of Applied Microbiology & Bioengineering
1974 Volume.2 No. 3 p.133 ~ p.140
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Studies on Enzyme of the Thermophilic Mold (PartⅤ.)
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Abstract
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1) Two xylanase (designed as A and B) of Myriococcus albomyces were purified from an extract of wheat koji culture. Purification steps included first ammonium sulfate fractionation followed successively by SE-Sephadex column chromatgraphy, DEAE-Sephadex column chromatography and gel filtration on Sephiadex G-100 repectively.
2) The optimum pH and pH stability for crude xylanse were found to be pH 5.0 and pH 4.0―7.0 respectively.
3) The optimium temperature wasfound to be 50℃ and for the thermal statbility of xylanase, the e incubated at 65℃ for 60 min did not affect their stability.
4) The purified xylanase A and B were considered as liquefying xylanase and saccharogenic xylanase ctively.
5) The xylanase A was most active at pH 4.0 and range of pH 3.0―8.0 at 30℃ for six hrs. The B was most active at pH 5.0 showing stability range of pH 4.0 to 8.5 at 30℃ for 6 hrt. incubation respectively. The Optimum temperature of xylanase A and B were found to be 70℃ and 65℃ for 60 min repectively.
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