Acremonium alcalophilum JCM7366の生産する低温でセルロースキシランを分解する酵素の精製と性質

概要

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A low-temperature-active CMCase from Acremonium alcalophilum JCM 7366 was purified by ammonium sulfate fractionation, QAE-Toyopearl 650c column chromatography, TSKgel ether-5PW high performance liquid column chromatography, and TSKgel G3000SWxl high performance liquid column chromatography. The molecular weight of the purified enzyme was estimated to be 46,000 and 48,000 by SDS-PAGE and TSKgel G3000SWxl gel filtration, respectively. The isoeletric point was 4.4. The purified enzyme hydrolyzed CMC, Avicel, and xylan. The main product after 24-h digestion of CMC or xylan was cellobiose or xylobiose. The maximal CMCase and xylanase activities of the purified low-temperature-active enzyme were obtained at 40℃ and pH7.0. CMCase and xylanase activities at 0℃ were retained at more than 25.0 and 48.8% of the activities at 40℃, respectively. Both these enzyme activities were stable at pHs from 5.5 to 10.0 and at 50℃ for 10 min.
社団法人日本生物工学会の論文
1997-01-25