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KMID : 0545120090190080818
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Journal of Microbiology and Biotechnology
2009 Volume.19 No. 8 p.818 ~ p.822
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Purification and Characterization of a Thermostable ￥a-1,3-1,4-Glucanase from Laetiporus sulphureus var. miniatus
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Hong Mi-Ri
Kim Yeong-Su
Joo Ah-Reum
Lee Jung-Kul
Kim Yeong-Suk
Oh Deok-Kun
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Abstract
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￥a-1,3-1,4-glucanase from the fungus Laetiporus sulphureus var. miniatus was purified as a single 26 kDa band by ammonium sulfate precipitation, HiTrap Q HP, and UNO Q ion-exchange chromatography, with a specific activity of 29U/mg. The molecular mass of the native enzyme was 52 kDa as a dimer by gel filtration. ￥a-1,3-1,4-Glucanase showed optimum activity at pH 4.0 and 75oC. The half-lives of the enzyme at 70oC and 75oC were 152 h and 22 h, respectively. The enzyme showed the highest activity for barley ￥a- glucan as ￥a-1,3-1,4-glucan among the tested polysaccharides and p-nitrophenyl-￥a-D-glycosides with a Km of 0.67 mg/ml, a kcat of 13.5 s-1 and a kcat/Km of 20 mg/ml/s.
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KEYWORD
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Characterization, β-1, 3-1, 4-glucanase, Laetiporus sulphureus var. miniatus, purification, thermostable enzyme
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