نتایج جستجو برای: endoglucanase

تعداد نتایج: 1045  

2015
Marcoaurélio Almenara Rodrigues Ricardo Sposina Sobral Teixeira Viridiana Santana Ferreira-Leitão Elba Pinto da Silva Bon

BACKGROUND Chlorophyte microalgae have a cell wall containing a large quantity of cellulose Iα with a triclinic unit cell hydrogen-bonding pattern that is more susceptible to hydrolysis than that of the cellulose Iβ polymorphic form that is predominant in higher plants. This study addressed the enzymatic hydrolysis of untreated Chlorella homosphaera biomass using selected enzyme preparations, a...

Journal: :Applied and environmental microbiology 2007
Nathan A Ekborg Wendy Morrill Adam M Burgoyne Li Li Daniel L Distel

We characterized a multifunctional cellulase (CelAB) encoded by the endosymbiont Teredinibacter turnerae T7902(T). CelAB contains two catalytic and two carbohydrate-binding domains, each separated by polyserine linker regions. CelAB binds cellulose and chitin, degrades multiple complex polysaccharides, and displays two catalytic activities, cellobiohydrolase (EC 3.2.1.91) and beta-1,4(3) endogl...

Journal: :Applied and environmental microbiology 2008
Tomoko Shimokawa Hajime Shibuya Masanobu Nojiri Shigeki Yoshida Mitsuro Ishihara

A family 12 endoglucanase with a molecular mass of 23,926 Da (EG-II) from the brown-rot basidiomycete Fomitopsis palustris was purified and characterized. One of the roles of EG-II in wood degradation is thought to be to loosen the polysaccharide network in cell walls by disentangling hemicelluloses that are associated with cellulose.

Journal: :Applied and environmental microbiology 1994
S Wittmann F Shareck D Kluepfel R Morosoli

The endoglucanase CelB isolated from culture filtrates of Streptomyces lividans IAF9 has an M(r) of 36,000. With carboxymethyl cellulose as the substrate, the Vmax and Km values are 110 IU/mg of enzyme and 1.3 mg/ml, respectively. Comparison of primary amino acid sequences classifies CelB in the H family of cellulases.

Journal: :Bioscience, biotechnology, and biochemistry 2010
Tatsuya Fujii Katsuji Murakami Shigeki Sawayama

Cellulase hyperproducing mutants derived from the fungus Trichoderma reesei QM9414 were analyzed. They exhibited higher filter-paper degrading activity and a lower growth rate than the wild-type QM9414 strain. Transcription of the cellobiohydrolase I and endoglucanase I genes in the mutants was also greater than that of QM9414, suggesting that cellulase hyperproduction by these mutants was regu...

Journal: :Journal of bacteriology 2005
Sung Ok Han Hideaki Yukawa Masayuki Inui Roy H Doi

Clostridium cellulovorans produces a major noncellulosomal family 9 endoglucanase EngO. A genomic DNA fragment (40 kb) containing engO and neighboring genes was cloned. The nucleotide sequence contained reading frames for endoglucanase EngO, a putative response regulator, and a putative sensor histidine kinase protein. The engO gene consists of 2,172 bp and encodes a protein of 724 amino acids ...

2012
Olubusola A. Odeniyi Anthony A. Onilude Maria A. Ayodele

The characteristics of an endoglucanase produced by a Trichoderma virens strain T9 newly isolated from a palm-fruit husk dump site, its physiological characteristics and enzyme production were studied. Whole cells of the depolymerizing-enzyme producing T. virens were applied to palm-fruit husk and bird performance characteristics when employed as poultry diet additive were considered. Endogluca...

2014
André Luís Braghini Sá Armando Cavalcante Franco Dias Maria Carolina Quecine Simone Raposo Cotta Cristiane Cipola Fasanella Fernando Dini Andreote Itamar Soares de Melo

In screening the culturable endoglucanase-producing bacteria in the rhizosphere of Rhizophora mangle, we found a prevalence of genera Bacillus and Paenibacillus. These bacteria revealed different activities in endoglucolysis and biofilm formation when exposed to specific NaCl concentrations, indicating modulated growth under natural variations in mangrove salinity.

Journal: :Organic & biomolecular chemistry 2011
Solange Moréra Armelle Vigouroux Keith A Stubbs

Using structural insight, the binding mode of isofagomine-derived inhibitors with family GH9 glycosidases is achieved via the study of Alicyclobacillus acidocaldarius (AaCel9A) endoglucanase. In contrast to what was observed in the first report using these compounds with inverting glycosidases from family GH6, these inhibitors do not adopt a distorted conformation in the active site.

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