Affinity purification and characterization of a yeast epoxide hydrolase
Purification of the membrane-associated epoxide hydrolase from the yeast Rhodosporidium toruloides CBS 0349 to electrophoretic homogeneity was achieved in a single chromatographic step employing the affinity ligand adsorbent Mimetic Green. More than 68% of the total epoxide hydrolase activity presen...
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| Vydáno v: | Biotechnology letters Ročník 21; číslo 6; s. 511 - 517 |
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| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
Dordrecht
Springer
01.06.1999
Springer Nature B.V |
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| ISSN: | 0141-5492, 1573-6776 |
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| Abstract | Purification of the membrane-associated epoxide hydrolase from the yeast Rhodosporidium toruloides CBS 0349 to electrophoretic homogeneity was achieved in a single chromatographic step employing the affinity ligand adsorbent Mimetic Green. More than 68% of the total epoxide hydrolase activity present in the whole cells was recovered from the membrane fraction. The enzyme was purified 26-fold with respect to the solubilized membrane proteins and was obtained in a 90% yield. The purified epoxide hydrolase has an apparent monomeric molecular weight of approximately 54 kDa, and a pI of 7.3. The enzyme was optimally active at 30-40 degrees C, and pH 7.3-8.5. The enzyme is highly glycosylated with a carbohydrate content >42%. The specific activity of the purified enzyme for (+/-)-1,2-epoxyoctane is 172 micromol min(-1) mg protein(-1). The amino acid composition of the protein was determined. This is the first report of a yeast epoxide hydrolase purified to homogeneity in milligram amounts. |
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| AbstractList | Purification of the membrane-associated epoxide hydrolase from the yeast Rhodosporidium toruloides CBS 0349 to electrophoretic homogeneity was achieved in a single chromatographic step employing the affinity ligand adsorbent Mimetic Green. More than 68% of the total epoxide hydrolase activity present in the whole cells was recovered from the membrane fraction. The enzyme was purified 26-fold with respect to the solubilized membrane proteins and was obtained in a 90% yield. The purified epoxide hydrolase has an apparent monomeric molecular weight of approximately 54 kDa, and a pI of 7.3. The enzyme was optimally active at 30-40 degrees C, and pH 7.3-8.5. The enzyme is highly glycosylated with a carbohydrate content >42%. The specific activity of the purified enzyme for (+/-)-1,2-epoxyoctane is 172 micromol min(-1) mg protein(-1). The amino acid composition of the protein was determined. This is the first report of a yeast epoxide hydrolase purified to homogeneity in milligram amounts. Purification of the membrane-associated epoxide hydrolase from the yeast Rhodosporidium toruloides CBS 0349 to electrophoretic homogeneity was achieved in a single chromatographic step employing the affinity ligand adsorbent Mimetic Green. More than 68% of the total epoxide hydrolase activity present in the whole cells was recovered from the membrane fraction. The enzyme was purified 26-fold with respect to the solubilized membrane proteins and was obtained in a 90% yield. The purified epoxide hydrolase has an apparent monomeric molecular weight of 54 kDa, and a pI of 7.3. The enzyme was optimally active at 30-40 °C, and pH 7.3-8.5. The enzyme is highly glycosylated with a carbohydrate content >42%. The specific activity of the purified enzyme for (±)-1,2-epoxyoctane is 172 μmol min^sup -1^ mg protein^sup -1^. The amino acid composition of the protein was determined. This is the first report of a yeast epoxide hydrolase purified to homogeneity in milligram amounts.[PUBLICATION ABSTRACT] Purification of the membrane-associated epoxide hydrolase from the yeast Rhodosporidium toruloides CBS 0349 to electrophoretic homogeneity was achieved in a single chromatographic step employing the affinity ligand adsorbent Mimetic Green. More than 68% of the total epoxide hydrolase activity present in the whole cells was recovered from the membrane fraction. The enzyme was purified 26-fold with respect to the solubilized membrane proteins and was obtained in a 90% yield. The purified epoxide hydrolase has an apparent monomeric molecular weight of similar to 54 kDa, and a pI of 7.3. The enzyme was optimally active at 30-40 degree C, and pH 7.3-8.5. The enzyme is highly glycosylated with a carbohydrate content >42%. The specific activity of the purified enzyme for ( plus or minus )-1,2-epoxyoctane is 172 mu mol min super(-1) mg protein super(-1). The amino acid composition of the protein was determined. This is the first report of a yeast epoxide hydrolase purified to homogeneity in milligram amounts. |
| Author | Botes, A.L |
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| CitedBy_id | crossref_primary_10_1023_A_1005630309102 crossref_primary_10_1016_j_molcatb_2005_09_003 crossref_primary_10_1016_S0141_0229_00_00306_9 crossref_primary_10_1016_j_jbiotec_2005_06_011 crossref_primary_10_1016_S0957_4166_99_00355_9 crossref_primary_10_1016_j_tibtech_2004_01_012 crossref_primary_10_1016_S0958_1669_01_00262_2 crossref_primary_10_1016_j_procbio_2022_12_029 crossref_primary_10_1016_S1381_1177_00_00229_0 crossref_primary_10_1016_j_bbagen_2005_11_002 crossref_primary_10_1007_s00253_007_1098_2 crossref_primary_10_1016_j_jbiosc_2010_03_007 crossref_primary_10_1016_S1367_5931_00_00179_4 crossref_primary_10_1007_BF02932009 crossref_primary_10_1002_yea_1437 crossref_primary_10_1038_ncomms2112 crossref_primary_10_1007_BF03026241 crossref_primary_10_1080_09168451_2020_1740581 crossref_primary_10_1007_BF02949324 crossref_primary_10_1007_s00253_006_0635_8 crossref_primary_10_1016_j_enzmictec_2006_04_004 crossref_primary_10_1023_A_1020613803342 crossref_primary_10_1016_j_procbio_2007_01_009 |
| Cites_doi | 10.1042/bj2050117 10.1016/S1381-1177(98)00011-3 10.1007/BF00127422 10.1074/jbc.272.23.14650 10.1016/S0168-1656(98)00025-X 10.1016/0003-2697(87)90166-7 10.1042/bj2820711 10.1016/S0021-9258(18)50495-6 10.1016/S0021-9673(01)81635-6 10.1046/j.1432-1327.1998.2530173.x 10.1111/j.1432-1033.1991.tb16493.x 10.1006/bbrc.1996.0404 10.1023/A:1005395817739 10.1016/0003-2697(82)90126-9 10.1016/0003-9861(86)90408-X 10.1016/S1381-1177(98)00123-4 10.1016/S0141-0229(97)00168-3 10.1016/0003-2697(88)90256-4 10.1016/S0957-4166(98)00180-3 10.1016/S0957-4166(97)00012-8 10.1016/S0167-7799(97)01161-X |
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| Keywords | Purification Enzyme Basidiomycetes Epoxide hydrolase Fungi Enzymatic activity Affinity chromatography Ether hydrolases Hydrolases Chemical composition Kinetic parameter Physicochemical properties Thallophyta Rhodosporidium toruloides |
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| SubjectTerms | adsorbents amino acid composition Amino acids Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology carbohydrate content chromatography electrophoresis epoxide hydrolase Fundamental and applied biological sciences. Psychology glycosylation Homogeneity membrane proteins Miscellaneous Mission oriented research Molecular weight Proteins Rhodosporidium toruloides solubilization Sporidiales Yeast Yeasts |
| Title | Affinity purification and characterization of a yeast epoxide hydrolase |
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