Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Enzymatic properties of the highly thermophilic and alkaline pectate lyasePel-4B from alkaliphilic Bacillus sp strain P-4-N and the entire nucleotide and amino acid sequences
Autore:
Hatada, Y; Kobayashi, T; Ito, S;
Indirizzi:
Kao Corp, Tochigi Res Labs, Haga, Tochigi 3213497, Japan Kao Corp Haga Tochigi Japan 3213497 es Labs, Haga, Tochigi 3213497, Japan
Titolo Testata:
EXTREMOPHILES
fascicolo: 2, volume: 5, anno: 2001,
pagine: 127 - 133
SICI:
1431-0651(200104)5:2<127:EPOTHT>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ERWINIA-CHRYSANTHEMI EC16; PLANT VIRULENCE FACTOR; MOLECULAR-WEIGHT; PECTIC ENZYMES; GENE; CLONING; ISOLATE; SUPERFAMILY; EXPRESSION; SUBTILIS;
Keywords:
pectin; pectate lyase; cloning; alkaliphile; Bacillus;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Ito, S Kao Corp, Tochigi Res Labs, 2606 Akabane, Haga, Tochigi 3213497, Japan Kao Corp 2606 Akabane Haga Tochigi Japan 3213497 igi 3213497, Japan
Citazione:
Y. Hatada et al., "Enzymatic properties of the highly thermophilic and alkaline pectate lyasePel-4B from alkaliphilic Bacillus sp strain P-4-N and the entire nucleotide and amino acid sequences", EXTREMOPHIL, 5(2), 2001, pp. 127-133

Abstract

We cloned two genes for alkaline pectate lyase, pel-4A and pel-4B, from alkaline pectinase-producing alkaliphilic Bacillus sp. strain P-4-N. The pel-4B gene product Pel-4B was purified to homogeneity and characterized. The purified enzyme had an isoelectric point of pH 9.6 and a molecular mass of 35 kDa, values dose to those of the pel-4A gene product Pel-4A. The pH and temperature optima for activity were as high as 11.5 and 70 degreesC, respectively, which are the highest among the pectate lyases reported to date. The mature Pel-4B (304 amino acids; 33,868 Da) was structurally related to the enzymes in the polysaccharide lyase family I and showed 35.6% identity with Pel-4A on the amino acid level. It showed significant homology to other pectate lyases in the same family, such as the enzymes from alkaliphilic Bacillus sp. strains KSM-P7 and KSM-P103 and the fungi Aspergillus nidulans and Colletotrichum gloeosporioides f. sp. malvae.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 13:05:26