Purification and properties of manganese peroxidase from Trametes versicolor
Two manganese peroxidase (MnP) active fractions D1 and D2 were got from the extracellular culture of Trametes versicolor by using ammonium sulfate precipitation, DEAE-cellulose DE52 chromatography. MnP1 was purified to electrophoretic homogeneity from the D2 by Phenyl Sepharose 6 Fast Flow chromatography and MnP2 was purified to electrophoretic homogeneity from the D1 by Sephacryl S-200HR chromatography and Phenyl Sepharose 6 Fast Flow chromatography. The specific activities of two MnP isozymes are 579.1U/mg and 425.0U/mg; purification folds are 17.51 and 12.85 and the yields are 6.17% and 2.47%, respectively. MnP1 and MnP2 have approximate molecular masses of 46.3kD and 43.0kD respectively, as determined by SDS-PAGE. The isoenzymes differed in optimum temperature (60degreesC and 65degreesC) and optimum pH(5.8 and 6.2) for oxidation of DMP (2,6-dimethoxyphenol). MnP1 and MnP2 are stable below 45degreesC and ranging from pH4.0 to pH7.0. DMP is the best substrate, the Km values of MnP1 and MnP2 for DMP are 13.43micromol/L and 12.45micromol/L respectively. Catalysis doesn't occur in the complete absence of Mn. EDTA inhibites the activities of MnP1 and MnP2 at the higher concentration and DTT inhibites the enzyme activities completely.
Medienart: |
Artikel |
---|
Erscheinungsjahr: |
2005 |
---|---|
Erschienen: |
2005 |
Enthalten in: |
Zur Gesamtaufnahme - volume:45 |
---|---|
Enthalten in: |
Wei sheng wu xue bao = Acta microbiologica Sinica - 45(2005), 5 vom: 01. Okt., Seite 711-5 |
Sprache: |
Chinesisch |
---|
Beteiligte Personen: |
Zhang, Lian-hui [VerfasserIn] |
---|
Themen: |
EC 1.11.1.- |
---|
Anmerkungen: |
Date Completed 23.04.2009 Date Revised 13.12.2005 published: Print Citation Status MEDLINE |
---|
Förderinstitution / Projekttitel: |
|
---|
PPN (Katalog-ID): |
NLM15944912X |
---|
LEADER | 01000naa a22002652 4500 | ||
---|---|---|---|
001 | NLM15944912X | ||
003 | DE-627 | ||
005 | 20231223084146.0 | ||
007 | tu | ||
008 | 231223s2005 xx ||||| 00| ||chi c | ||
028 | 5 | 2 | |a pubmed24n0532.xml |
035 | |a (DE-627)NLM15944912X | ||
035 | |a (NLM)16342761 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a chi | ||
100 | 1 | |a Zhang, Lian-hui |e verfasserin |4 aut | |
245 | 1 | 0 | |a Purification and properties of manganese peroxidase from Trametes versicolor |
264 | 1 | |c 2005 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
338 | |a Band |b nc |2 rdacarrier | ||
500 | |a Date Completed 23.04.2009 | ||
500 | |a Date Revised 13.12.2005 | ||
500 | |a published: Print | ||
500 | |a Citation Status MEDLINE | ||
520 | |a Two manganese peroxidase (MnP) active fractions D1 and D2 were got from the extracellular culture of Trametes versicolor by using ammonium sulfate precipitation, DEAE-cellulose DE52 chromatography. MnP1 was purified to electrophoretic homogeneity from the D2 by Phenyl Sepharose 6 Fast Flow chromatography and MnP2 was purified to electrophoretic homogeneity from the D1 by Sephacryl S-200HR chromatography and Phenyl Sepharose 6 Fast Flow chromatography. The specific activities of two MnP isozymes are 579.1U/mg and 425.0U/mg; purification folds are 17.51 and 12.85 and the yields are 6.17% and 2.47%, respectively. MnP1 and MnP2 have approximate molecular masses of 46.3kD and 43.0kD respectively, as determined by SDS-PAGE. The isoenzymes differed in optimum temperature (60degreesC and 65degreesC) and optimum pH(5.8 and 6.2) for oxidation of DMP (2,6-dimethoxyphenol). MnP1 and MnP2 are stable below 45degreesC and ranging from pH4.0 to pH7.0. DMP is the best substrate, the Km values of MnP1 and MnP2 for DMP are 13.43micromol/L and 12.45micromol/L respectively. Catalysis doesn't occur in the complete absence of Mn. EDTA inhibites the activities of MnP1 and MnP2 at the higher concentration and DTT inhibites the enzyme activities completely | ||
650 | 4 | |a English Abstract | |
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 7 | |a Peroxidases |2 NLM | |
650 | 7 | |a EC 1.11.1.- |2 NLM | |
650 | 7 | |a manganese peroxidase |2 NLM | |
650 | 7 | |a EC 1.11.1.13 |2 NLM | |
700 | 1 | |a Yang, Xiu-qing |e verfasserin |4 aut | |
700 | 1 | |a Ge, Ke-shan |e verfasserin |4 aut | |
700 | 1 | |a Qian, Shi-jun |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Wei sheng wu xue bao = Acta microbiologica Sinica |d 1985 |g 45(2005), 5 vom: 01. Okt., Seite 711-5 |w (DE-627)NLM012631655 |x 0001-6209 |7 nnns |
773 | 1 | 8 | |g volume:45 |g year:2005 |g number:5 |g day:01 |g month:10 |g pages:711-5 |
912 | |a GBV_USEFLAG_A | ||
912 | |a GBV_NLM | ||
951 | |a AR | ||
952 | |d 45 |j 2005 |e 5 |b 01 |c 10 |h 711-5 |