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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| Vydané v: | Biotechnology letters Ročník 21; číslo 6; s. 511 - 517 |
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| Médium: | Journal Article |
| Jazyk: | English |
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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 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. 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] |
| Author | Botes, A.L |
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| 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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