Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Stability and folding of endoglucanase I (Cel7b) from Humicola insolens
Autore:
Otzen, D; Schulein, M;
Indirizzi:
Univ Aalborg, Dept Life Sci, DK-9000 Aalborg, Denmark Univ Aalborg Aalborg Denmark DK-9000 Life Sci, DK-9000 Aalborg, Denmark Novozymes AS, DK-2880 Bagsvaerd, Denmark Novozymes AS Bagsvaerd Denmark DK-2880 es AS, DK-2880 Bagsvaerd, Denmark
Titolo Testata:
BIOCATALYSIS AND BIOTRANSFORMATION
fascicolo: 5-6, volume: 19, anno: 2001,
pagine: 469 - 487
SICI:
1024-2422(2001)19:5-6<469:SAFOEI>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSITION-STATE; RESIDUAL STRUCTURE; DENATURED STATE; PROTEIN; CELLULASES; PATHWAY; MECHANISM; LYSOZYME; KINETICS; BARNASE;
Keywords:
endoglucanase; Ce17B; stability; folding; intermediate; kinetics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Otzen, D Univ Aalborg, Dept Life Sci, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark Univ Aalborg Sohngaardsholmsvej 49 Aalborg Denmark DK-9000 nmark
Citazione:
D. Otzen e M. Schulein, "Stability and folding of endoglucanase I (Cel7b) from Humicola insolens", BIOCATAL B, 19(5-6), 2001, pp. 469-487

Abstract

Cellulases are of economic significance, particularly in the detergent andtextile industries, where they are subjected to a wide range of operating conditions affecting their stability. To increase our insight into the properties of this class of enzymes, we have carried out a study of the stability and folding behavior of the 413-residue endoglucanase I (Cel7B) from Humicola insolens. Data from chemical denaturation in guanidinium. chloride agree satisfactorily with calorimetric measurements, revealing an optimum stability of ca. 20 kcal mol(-1) around pH 7 and a peak half-width of 3-4 pH units. Stability and activity show very similar pH-profiles, but this is probably fortuitous. Judging from equilibrium m-values (the dependence of the log of the equilibrium unfolding constant on the denaturant concentration),the denatured state becomes significantly more compact outside pH 6-9. Folding and unfolding proceed very slowly with relaxation half times up to 6 h. Single- and double-jump kinetic data at pH 7 suggest a folding scheme involving two intermediates with native-like secondary structure but varying degrees of tertiary structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:57:09