Manganese peroxidase from Phanerochaete crassa WD1694
Manganese peroxidase from Phanerochaete crassa WD1694
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来自粗糙原毛平革菌的锰过氧化物酶 WD1694
DOI：
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Ishihara Mitsuro
中科院分区：
文献类型：
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作者：
Takano Mariko;Nakamura Masaya;Nishida Atsumi;Ishihara Mitsuro
从白腐菌Phanerochaete crassa WD1694中分离得到一种对未漂白硫酸盐浆具有很高漂白能力的锰过氧化物酶，并对其进行了纯化和鉴定。采用DEAE-Sepahrose CL-6B吸附-脱附和DEAE-Toyota opearl FPLC吸附-脱附的方法纯化MNP。纯化后的MNP在48.3 kDa处出现一条单一条带，经等电聚焦可在极近等电点上分离出4条同工酶(pI4.61、4.59、4.52、4.50)。四种同工酶的N-末端序列与黄孢原毛霉mNPs高度同源。该酶能氧化2，6-二甲氧基苯酚，但不能氧化藜芦醇。粗毛假单胞菌WD1694MNP的最适pH为3.0~4.0，低于黄孢原毛霉和索氏假单胞菌的最适pH(4.5~5.0)。氧化锰(Ⅱ)的表观Km值为35.8×10-3 mm，不加锰(Ⅱ)的表观Km值为30.7 mm。这些结果表明，粗毛假单胞菌WD1694产生的MNP在催化性质和N端序列方面与黄孢原毛假单胞菌的MNP非常相似。
A manganese peroxidase from the white-rot fungus Phanerochaete crassa WD1694, that had exhibited very high ability to bleach unbleached kraft pulp, was purified and characterized. The MnP was purified by adsorption-desorption on DEAE-Sepahrose CL-6B and FPLC on DEAE-Toyopearl. The purified MnP gave a single band at 48.3 kDa on SDS-PAGE and could be separated into four isozymes at extremely close pIs (pI4.61, 4.59, 4.52, 4.50) by isoelectric focusing. The N-terminal sequences of the four isozymes were highly homologous and similar to those of the MnPs from P. chrysosporium. The enzyme oxidized 2,6-dimethoxyphenol (DMP) with and without Mn(Ⅱ) but did not oxidize veratryl alcohol. The optimal pH of P. crassa WD1694 MnP was 3.0-4.0 and lower than that (4.5-5.0) of P. chrysosporium and P. sordida MnPs. Apparent Km values for oxidation of Mn(Ⅱ) and DMP without Mn(Ⅱ) were 35.8×10 -3 mM and 30.7 mM, respectively. These results showed that the MnP from P. crassa WD1694 was very similar to the MnPs from P. chrysosporium in terms of catalytic properties and N-terminal sequences.
来自 Phanerochaete chrysosporium 的锰依赖性过氧化物酶。
DOI：
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发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Pease,EA;Andrawis,A;Tien,M
通讯作者：
Tien,M