Expression and characteristics of a Ca2+-dependent endoglucanase from Cytophaga hutchinsonii

Verfasser / Beitragende:
[Cong Zhang, Weican Zhang, Xuemei Lu]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/22(2015-11-01), 9617-9623
Format:
Artikel (online)
ID: 605500851
LEADER caa a22 4500
001 605500851
003 CHVBK
005 20210128100558.0
007 cr unu---uuuuu
008 210128e20151101xx s 000 0 eng
024 7 0 |a 10.1007/s00253-015-6746-3  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-015-6746-3 
245 0 0 |a Expression and characteristics of a Ca2+-dependent endoglucanase from Cytophaga hutchinsonii  |h [Elektronische Daten]  |c [Cong Zhang, Weican Zhang, Xuemei Lu] 
520 3 |a Cytophaga hutchinsonii is a Gram-negative bacterium that can degrade crystalline cellulose efficiently with an unknown strategy. Genomic analysis suggested it lacks exoglucanases which are found in many cellulolytic organisms and most of the cellulases in C. hutchinsonii lack recognizable carbohydrate-binding modules (CBMs). CHU_1280, speculated to be an endoglucanase belonging to glycoside hydrolase family 9 (GH9) in C. hutchinsonii, was functionally expressed in Escherichia coli, and evidence was presented suggesting that it may be a processive endoglucanase. In the absence of Ca2+, CHU_1280 was inactive. But in the presence of Ca2+, it had a specific activity of 600U/μmol with carboxymethyl cellulose (CMC) as the substrate. With Ca2+, CHU_1280 hydrolyzed regenerated amorphous cellulose (RAC) with nearly 80% of the reducing ends appearing in the soluble fraction, suggesting it degraded cellulose in a processive way. CHU_1280 could bind to cellulose without recognizable CBMs and its binding ability was also Ca2+-dependent. Ca2+ could stabilize the catalytic domain at high temperature, but the denaturation temperature of the whole protein was decreased. C. hutchinsonii might have an exoglucanase-independent cellulases system which included endoglucanases, processive endoglucanases, and β-glucosidases. 
540 |a Springer-Verlag Berlin Heidelberg, 2015 
690 7 |a Cytophaga hutchinsonii  |2 nationallicence 
690 7 |a Family 9 glycoside hydrolase  |2 nationallicence 
690 7 |a Endoglucanase  |2 nationallicence 
690 7 |a Calcium-dependent  |2 nationallicence 
700 1 |a Zhang  |D Cong  |u State Key Laboratory of Microbial Technology, College of Life Science, Shandong University, 250100, Jinan, China  |4 aut 
700 1 |a Zhang  |D Weican  |u State Key Laboratory of Microbial Technology, College of Life Science, Shandong University, 250100, Jinan, China  |4 aut 
700 1 |a Lu  |D Xuemei  |u State Key Laboratory of Microbial Technology, College of Life Science, Shandong University, 250100, Jinan, China  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/22(2015-11-01), 9617-9623  |x 0175-7598  |q 99:22<9617  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-015-6746-3  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-015-6746-3  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Zhang  |D Cong  |u State Key Laboratory of Microbial Technology, College of Life Science, Shandong University, 250100, Jinan, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Zhang  |D Weican  |u State Key Laboratory of Microbial Technology, College of Life Science, Shandong University, 250100, Jinan, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Lu  |D Xuemei  |u State Key Laboratory of Microbial Technology, College of Life Science, Shandong University, 250100, Jinan, China  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/22(2015-11-01), 9617-9623  |x 0175-7598  |q 99:22<9617  |1 2015  |2 99  |o 253