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Titolo:
Role of cellulose-binding domain of exocellulase I from white rot basidiomycete Irpex lacteus
Autore:
Hamada, N; Kodaira, R; Nogawa, M; Shinji, K; Ito, R; Amano, Y; Shimosaka, M; Kanda, T; Okazaki, M;
Indirizzi:
Shinshu Univ, Fac Text Sci & Technol, Dept Appl Biol, Ueda, Nagano 3868567, Japan Shinshu Univ Ueda Nagano Japan 3868567 Biol, Ueda, Nagano 3868567, Japan Shinshu Univ, Ctr Gene Res, Ueda, Nagano 3868567, Japan Shinshu Univ UedaNagano Japan 3868567 e Res, Ueda, Nagano 3868567, Japan Shinshu Univ, Fac Engn, Dept Chem & Mat Engn, Nagano 3808553, Japan Shinshu Univ Nagano Japan 3808553 Chem & Mat Engn, Nagano 3808553, Japan
Titolo Testata:
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
fascicolo: 4, volume: 91, anno: 2001,
pagine: 359 - 362
SICI:
1389-1723(200104)91:4<359:ROCDOE>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
EXO-CELLULASE; POLYPORUS-TULIPIFERAE; 2 CELLOBIOHYDROLASES; TRICHODERMA-REESEI; PURIFICATION; GENE;
Keywords:
cellulose-binding domain; Irpex lacteus; O-linked sugar chains; limited proteolysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
14
Recensione:
Indirizzi per estratti:
Indirizzo: Okazaki, M Shinshu Univ, Fac Text Sci & Technol, Dept Appl Biol, 3-15-1 Tokida, Ueda,Nagano 3868567, Japan Shinshu Univ 3-15-1 Tokida Ueda Nagano Japan 3868567 567, Japan
Citazione:
N. Hamada et al., "Role of cellulose-binding domain of exocellulase I from white rot basidiomycete Irpex lacteus", J BIOSCI BI, 91(4), 2001, pp. 359-362

Abstract

The core fragment (designated P-42), devoid of the cellulose-binding domain (CBD) in the C-terminus and prepared from Irpex lacteus exocellulase I(Ex-l), was isolated by limited proteolysis using papain. Both the hydrolytic activity and binding ability of the isolated P-42 toward insoluble cellulose were lower than those of the native Ex-1, whereas Ex-1 and P-42 showed similar hydrolytic activities toward soluble substrates. These results indicate that the CBD of I. lacteus Ex-1 is the important domain which could enhance hydrolytic activity and binding ability of the enzyme toward insoluble cellulose. In addition, the isolated P-42 was different from the native Ex-1 in terms of enzymatic properties such as pH and temperature stabilities. These differences in stability, with regard to pH and temperature, between P-42 and the native Ex-1 are probably due to the O-linked sugar chains existing in the linker region.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 12:26:28