Characterization of a jasmonate-regulated wheat protein related to a beta-glucosidase-aggregating factor

2005 ◽  
Vol 43 (2) ◽  
pp. 185-192 ◽  
Author(s):  
Xing-Mei Wang ◽  
Qing-Hu Ma
Keyword(s):  
Wheat Protein ◽  
Beta Glucosidase

Characterization of a novel Aspergillus niger beta-glucosidase tolerant to saccharification of lignocellulosic biomass products and fermentation inhibitors

2015 ◽  
Vol 69 (8) ◽  
Author(s):  
Alesandra Oriente ◽  
Robson Tramontina ◽  
Diandra de Andrades ◽  
Caroline Henn ◽  
Jose L. C. Silva ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Lignocellulosic Biomass ◽  
Culture Conditions ◽  
Industrial Wastes ◽  
Fermentation Inhibitors ◽  
State Culture ◽  
Solid State Culture ◽  
Atlantic Rainforest Biome ◽  
Beta Glucosidase

AbstractProperties of beta-glucosidase produced by Aspergillus niger URM 6642 recently isolated from the Atlantic rainforest biome and its potential tolerance to saccharification of lignocellulosic biomass products and fermentation inhibitors was evaluated. The fungus was cultivated under solid state culture conditions at 37°C with different agro-industrial wastes. High levels of beta-glucosidase (3778.9 U g

scholarly journals Structural and Catalytic Characterization of TsBGL, a β-Glucosidase From Thermofilum sp. ex4484_79

2021 ◽  
Vol 12 ◽  
Author(s):  
Anke Chen ◽  
Dan Wang ◽  
Rui Ji ◽  
Jixi Li ◽  
Shaohua Gu ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Specific Activity ◽  
Maximum Activity ◽  
Homologous Proteins ◽  
Glycosidic Bonds ◽  
Catalytic Sites ◽  
Potential Applications ◽  
Beta Glucosidase ◽  
Hydrolysis Of

Beta-glucosidase is an enzyme that catalyzes the hydrolysis of the glycosidic bonds of cellobiose, resulting in the production of glucose, which is an important step for the effective utilization of cellulose. In the present study, a thermostable β-glucosidase was isolated and purified from the Thermoprotei Thermofilum sp. ex4484_79 and subjected to enzymatic and structural characterization. The purified β-glucosidase (TsBGL) exhibited maximum activity at 90°C and pH 5.0 and displayed maximum specific activity of 139.2μmol/min/mgzne against p-nitrophenyl β-D-glucopyranoside (pNPGlc) and 24.3μmol/min/mgzen against cellobiose. Furthermore, TsBGL exhibited a relatively high thermostability, retaining 84 and 47% of its activity after incubation at 85°C for 1.5h and 90°C for 1.5h, respectively. The crystal structure of TsBGL was resolved at a resolution of 2.14Å, which revealed a classical (α/β)8-barrel catalytic domain. A structural comparison of TsBGL with other homologous proteins revealed that its catalytic sites included Glu210 and Glu414. We provide the molecular structure of TsBGL and the possibility of improving its characteristics for potential applications in industries.

scholarly journals Purification and Characterization of Ginsenoside-.BETA.-Glucosidase from Ginseng.

2001 ◽  
Vol 49 (7) ◽  
pp. 795-798 ◽  
Author(s):  
Chunzhi ZHANG ◽  
Hongshan YU ◽  
Yongming BAO ◽  
Lijia AN ◽  
Fengxie JIN
Keyword(s):  
Purification And Characterization ◽  
Beta Glucosidase

scholarly journals Characterization of a beta-glucosidase from Bacillus licheniformis and its effect on bioflocculant degradation

AMB Express ◽  
2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Zhen Chen ◽  
Tong Meng ◽  
Zhipeng Li ◽  
Peize Liu ◽  
Yuanpeng Wang ◽  
...  
Keyword(s):  
Bacillus Licheniformis ◽  
Beta Glucosidase
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