Transformation of progesterone byCaldariella acidophila, an extreme thermophilic bacterium

Rosa, Mario De; Gambacorta, Agata; Sodano, G.; Trabucco, Armando E.

doi:10.1007/bf01990036

Cited by 11 publications

(3 citation statements)

References 3 publications

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“…For example, oxidoreductases from Caldariella acidophila have been studied using intact resting cells, acetonized cells or entrapped cells, for the transformation of progesterone resulting in a conversion efficiency between 4 and 24% at 85 "C. The product spectrum in this system depends on temperature and oxygen availability. The hydroxylative and oxydative system are both inactive below 70 "C, and the hydroxylative system is activated by oxygen [30]. Furthermore, thermostable and highly specific enzymes, e.g.…”

Section: More Stable Enzymes From Thermophilic Microorganismsmentioning

confidence: 99%

Enzymes from thermophiles

Zentgraf¹

1992

Acta Biotechnologica

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The most frequently used sources of more stable enzymes are thermophilic bacteria, e.g. Bacillus, Closrridium, and Therrnus strains, occurring in natural as well as man-made habitats. They grow from 55 to 88 "C with a specific growth rate of up to 2.6 h-' and a yield coefficient of up to 0.4 gram of dry cell weight per gram of carbohydrate consumed. Several thermophilic strains, e.g. Bacillus sp. TP32, rapidly and effectively produce enzymes having a higher thermal stability and resistance to chemical denaturants in comparison to their mesophilic counterparts. Therefore, thermostable enzymes are of importance for bioorganic syntheses. For the further optimization of enzyme production, genetic engineering is applied.

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Section: More Stable Enzymes From Thermophilic Microorganismsmentioning

confidence: 99%

Enzymes from thermophiles

Zentgraf¹

1992

Acta Biotechnologica

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“…1981. The enzyme of thermophiles may be immobilized and used for biotransformation (ROSA et al 1981). The use of purified enzymes could prevent formation of undesirable products which result from unwanted reactions.…”

Section: Immobilized Cells and Enzymesmentioning

confidence: 99%

“…Mycobacteria degrade the sterol (cholesterol) side chain by ,%oxidation as well as carry out 9a-hydroxylation which together with a 1,2 double bond leads to the un-264 V. S. RIALIK desirable fission of the steroid skeleton ( ROSA et al 1981, MAHATO et ul. 1981, BOHME and HORHOLU 1980.…”

Section: Microbial Degradation Of Side Chain Of Sterolsmentioning

confidence: 99%

Aspects of biotechnology in steriod biotransformation

Malik¹

1982

J of Basic Microbiology

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Bioconversion of steroids by Cochliobolus lunatus. I. Transformation of Reichstein's compound S with cell‐free preparations of Cochliobolus lunatus

Hörhold¹,

Undisz²,

Groh³

et al. 1986

J. Basic Microbiol.

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Steroid 11/3-hydroxylase activity and 20B-hydroxy-steroid dehydrogenase activity were found in the cell-free crude extract of Cochliobolus lunatus. It was possible to separate these two enzymatic activities by centrifugation at 100,000 x g. The 20B-hydroxy-steroid dehydrogenase activity remained in the supernatant while the ll/I-hydroxylase activity was present in the sediment. 11s-hydroxylation was clearly inhibited by CO.

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Transformation of progesterone byCaldariella acidophila, an extreme thermophilic bacterium

Cited by 11 publications

References 3 publications

Enzymes from thermophiles

Enzymes from thermophiles

Aspects of biotechnology in steriod biotransformation

Bioconversion of steroids by Cochliobolus lunatus. I. Transformation of Reichstein's compound S with cell‐free preparations of Cochliobolus lunatus

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