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Titolo:
THE ENZYMATIC PRODUCTION OF ADIPIC ACID
Autore:
MOREAU JL; BIGEY F; AZZA S; ARNAUD A; GALZY P;
Indirizzi:
ECOLE NATL SUPER AGRON MONTIPELLIER,CHAIR MICROBIOL IND & GENET MICOORGANISMES,PL VIALA F-34060 MONTPELLIER FRANCE
Titolo Testata:
Biocatalysis
fascicolo: 1-4, volume: 10, anno: 1994,
pagine: 325 - 340
SICI:
0886-4454(1994)10:1-4<325:TEPOAA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
BREVIBACTERIUM-SP; NITRILE-HYDRATASE; ACYLAMIDE AMIDOHYDROLASE; LIQUID-CHROMATOGRAPHY; AMIDASE; SPECTRUM; INTERMEDIATE; DINITRILE; BACTERIA;
Keywords:
BREVIBACTERIUM SP; 1,4-DICYANOBUTANE (ADIPONITRILE); 5-CYANOVALERIC ACID; ADIPAMIDE; 5-CYANOVALERAMIDE; ADIPIC ACID; MUTANT; NITRILE HYDRATASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
J.L. Moreau et al., "THE ENZYMATIC PRODUCTION OF ADIPIC ACID", Biocatalysis, 10(1-4), 1994, pp. 325-340

Abstract

Mutants of Brevibacterium sp. R312 were isolated for the production of adipic acid from 1,4-dicyanobutane (adiponitrile). One mutant (Ad), with a modified cell wall showed activity against adipamide three times greater than the wild type. Another mutant (ACV2) derived from the Ad strain had 30 times more activity on 5-cyanovaleric acid, and 7 times more on adipamide than the wild type. The nitrile hydratase from themutant strain ACV2 was purified and compared to that from the wild type R312. The nitrile hydratase of the mutant strain is different from that of the wild type by its pHi, optimum activity pH, and its fates of hydrolysis of 5-cyanovaleramide and 5-cyanovaleric acid which were 30 and 15 folds greater. The presence of a new amidase named ''adipamidase'' acting on amide intermediates in the hydrolysis of dinitriles toorganic acids was demonstrated in this mutant ACV2.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 08:56:43