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Titolo:
Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase and its application
Autore:
Wieser, M; Yoshida, T; Nagasawa, T;
Indirizzi:
Gifu Univ, Fac Engn, Dept Biomol Sci, Gifu 5011193, Japan Gifu Univ GifuJapan 5011193 Engn, Dept Biomol Sci, Gifu 5011193, Japan
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 4-6, volume: 11, anno: 2001,
pagine: 179 - 184
SICI:
1381-1177(20010122)11:4-6<179:CDFBRP>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACILLUS-MEGATERIUM PYR2910; 2,3-DIHYDROXYBENZOIC ACID DECARBOXYLASE; CELL-FREE-EXTRACTS; CLOSTRIDIUM-HYDROXYBENZOICUM; 4-HYDROXYBENZOATE DECARBOXYLASE; EUBACTERIUM-OXIDOREDUCENS; PELOBACTER-ACIDIGALLICI; ANAEROBIC DEGRADATION; INITIAL STEPS; PURIFICATION;
Keywords:
non-oxidative decarboxylation; pyrrole-2-carboxylate; reaction equilibrium; reversibility; organic acid; carbon dioxide fixation; Bacillus megaterium;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Nagasawa, T Gifu Univ, Fac Engn, Dept Biomol Sci, Gifu 5011193, Japan GifuUniv Gifu Japan 5011193 Biomol Sci, Gifu 5011193, Japan
Citazione:
M. Wieser et al., "Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase and its application", J MOL CAT B, 11(4-6), 2001, pp. 179-184

Abstract

Inducible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR3910 catalyzes the decarboxylation of pyrrole-2-carboxylate to stoichiometric amounts of pyrrole and CO2. A unique feature of the homodimeric enzyme is its requirement for an organic acid such as acetate, propionate, butyrateor pimelate. A catalytic mechanism including a cofactor function of the organic acid was proposed. Due to an equilibrium constant of 0.3-0.4 M, the enzyme also catalyzes the reverse carboxylation of pyrrole after the addition of bicarbonate. For the synthesis of pyrrole-2-carboxylate, the reverse reaction was optimized and the equilibrium shifted towards the carboxylate. The product yield was 230 mM (25.5 g/l) pyrrole-2-carboxylate from 300 mM pyrrole in a batch reaction and 325 mM (36.1 g/l) from 400 mM pyrrole in a fed batch reaction, using both whole cells and the purified enzyme in a pH 8.0 reaction mixture with bicarbonate saturation of 1.9 M. (C) 2001 ElsevierScience B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 20:04:08