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Titolo:
Purification and characterization of a cellulase from the ruminal fungus Orpinomyces joyonii cloned in Escherichia coli
Autore:
Ye, XY; Ng, TB; Cheng, KJ;
Indirizzi:
Chinese Univ Hong Kong, Dept Biochem, Shatin, Hong Kong, Peoples R China Chinese Univ Hong Kong Shatin Hong Kong Peoples R China Peoples R China Agr & Agri Food Canada, Lethbridge Res Stn, Lethbridge, AB, Canada Agr & Agri Food Canada Lethbridge AB Canada Stn, Lethbridge, AB, Canada Inst Acad Sinica, Taipei, Taiwan Inst Acad Sinica Taipei TaiwanInst Acad Sinica, Taipei, Taiwan
Titolo Testata:
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
fascicolo: 1, volume: 33, anno: 2001,
pagine: 87 - 94
SICI:
1357-2725(200101)33:1<87:PACOAC>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID-SEQUENCE SIMILARITIES; GLYCOSYL HYDROLASES; MOLECULAR-CLONING; 1,3-1,4-BETA-D-GLUCANASE LICHENASE; NEOCALLIMASTIX-PATRICIARUM; TRICHODERMA-REESEI; ANAEROBIC FUNGI; RUMEN; GENE; CLASSIFICATION;
Keywords:
cellulase; purification; ruminal fungus; Orpinomyces joyonii;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Ng, TB Chinese Univ Hong Kong, Dept Biochem, Shatin, Hong Kong, Peoples R China Chinese Univ Hong Kong Shatin Hong Kong Peoples R China s R China
Citazione:
X.Y. Ye et al., "Purification and characterization of a cellulase from the ruminal fungus Orpinomyces joyonii cloned in Escherichia coli", INT J BIO C, 33(1), 2001, pp. 87-94

Abstract

A cellulase from the luminal fungus Orpinomyces joyonii cloned in Escherichia coli was purified 88-fold by chromatography on High Q and hydroxyapatite. N-terminal amino acid sequence analyses confirmed that the cellulase represented the product of the cellulase gene Cel B2. The purified enzyme possessed high activity toward barley beta -glucan, lichenan, carboxymethyl cellulose (CMC), xylan, but not toward laminarin and pachyman. In addition, the cloned enzyme was able to hydrolyze p-nitrophenyl (PNP)-cellobioside, PNP-cellotrioside, PNP-cellotetraoside, PNP-cellopentaoside, but not PNP-glucopyranoside. The specific activity of the cloned enzyme on barley beta -glucan was 297 units/mg protein. The purified enzyme appeared as a single band in SDS-polyacrylamide gel electrophoresis and the molecular mass of this enzyme (58 000) was consistent with the value (56 463) calculated from the DNA sequence. The optimal pH of the enzyme was 5.5, and the enzyme was stablebetween pH 5.0 and pH 7.5. The enzyme had a temperature optimum at 40 degreesC. The K-m values estimated for barley B-glucan and CMC were 0.32 and 0.50 mg/ml, respectively. (C) 2001 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 19:00:18