The paper reports the partial purification and characterization of the 7_- and 7_-hydroxysteroid dehydrogenases (HSDH) and cholylglycine hydrolase (CGH), isolated from Xanthomonas maltophilia CBS 897.97. The activity of 7_-HSDH and 7_-HSDH in the reduction of the 7-keto bile acids is determined. The affinity of 7_-HSDH for bile acids is confirmed by the reduction, on analytical scale, to the corresponding 7_-OH derivatives. A crude mixture of 7_- and 7_-HSDH, in soluble or immobilized form, is employed in the synthesis, on preparative scale, of ursocholic and ursodeoxycholic acids starting from the corresponding 7_-derivatives. On the other hand, a partially purified 7_-HSDH in a double enzyme system, where the couple formate/formate dehydrogenase allows the cofactor recycle, affords 6_- fluoro-3_, 7_-dihydroxy-5_-cholan-24-oic acid (6-FUDCA) by reduction of the corresponding 7-keto derivative. This compound is not obtainable by microbiological route. The efficient and mild hydrolysis of glycinates and taurinates of bile acids with CGH is also reported. Very promising results are also obtained with bile acid containing raw materials.

Xanthomonas maltophilia CBS 897.97 as a source of new 7β- and 7α-hydroxysteroid dehydrogenases and cholylglycine hydrolase: Improved biotransformations of bile acids / Pedrini, P; Andreotti, Elisa; Guerrini, A; Dean, M; Fantin, G; Giovannini, P. P.. - In: STEROIDS. - ISSN 0039-128X. - STAMPA. - 71:3(2006), pp. 189-198. [10.1016/j.steroids.2005.10.002]

Xanthomonas maltophilia CBS 897.97 as a source of new 7β- and 7α-hydroxysteroid dehydrogenases and cholylglycine hydrolase: Improved biotransformations of bile acids

ANDREOTTI, Elisa;
2006

Abstract

The paper reports the partial purification and characterization of the 7_- and 7_-hydroxysteroid dehydrogenases (HSDH) and cholylglycine hydrolase (CGH), isolated from Xanthomonas maltophilia CBS 897.97. The activity of 7_-HSDH and 7_-HSDH in the reduction of the 7-keto bile acids is determined. The affinity of 7_-HSDH for bile acids is confirmed by the reduction, on analytical scale, to the corresponding 7_-OH derivatives. A crude mixture of 7_- and 7_-HSDH, in soluble or immobilized form, is employed in the synthesis, on preparative scale, of ursocholic and ursodeoxycholic acids starting from the corresponding 7_-derivatives. On the other hand, a partially purified 7_-HSDH in a double enzyme system, where the couple formate/formate dehydrogenase allows the cofactor recycle, affords 6_- fluoro-3_, 7_-dihydroxy-5_-cholan-24-oic acid (6-FUDCA) by reduction of the corresponding 7-keto derivative. This compound is not obtainable by microbiological route. The efficient and mild hydrolysis of glycinates and taurinates of bile acids with CGH is also reported. Very promising results are also obtained with bile acid containing raw materials.
2006
71
3
189
198
Xanthomonas maltophilia CBS 897.97 as a source of new 7β- and 7α-hydroxysteroid dehydrogenases and cholylglycine hydrolase: Improved biotransformations of bile acids / Pedrini, P; Andreotti, Elisa; Guerrini, A; Dean, M; Fantin, G; Giovannini, P. P.. - In: STEROIDS. - ISSN 0039-128X. - STAMPA. - 71:3(2006), pp. 189-198. [10.1016/j.steroids.2005.10.002]
Pedrini, P; Andreotti, Elisa; Guerrini, A; Dean, M; Fantin, G; Giovannini, P. P.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/585104
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