scholarly journals Characterization of a Novel Moderately Thermophilic Solvent-Tolerant Esterase Isolated From a Compost Metagenome Library

2020 ◽  
Vol 10 ◽  
Author(s):  
Ji-Min Park ◽  
Chul-Hyung Kang ◽  
Sung-Min Won ◽  
Ki-Hoon Oh ◽  
Jung-Hoon Yoon
Keyword(s):  
Moderately Thermophilic ◽  
Metagenome Library ◽  
Solvent Tolerant

Protocols for the Characterization of Solvent Tolerant Microorganisms: Construction and Characterization of Mutants

2010 ◽  
pp. 3957-3967 ◽  
Author(s):  
E. Duque ◽  
J. de la Torre ◽  
V. García ◽  
C. Pini ◽  
S. Rodríguez-Conde ◽  
...  
Keyword(s):  
Solvent Tolerant

scholarly journals Identification and Characterization of a Novel Thermostable and Salt-Tolerant β-1,3 Xylanase from Flammeovirga pacifica Strain WPAGA1

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1287
Author(s):  
Zhiwei Yi ◽  
Zhengwen Cai ◽  
Bo Zeng ◽  
Runying Zeng ◽  
Guangya Zhang
Keyword(s):  
Thermal Stability ◽  
Salt Tolerance ◽  
3D Structure ◽  
Catalytic Efficiency ◽  
Dynamics Simulation ◽  
Carbohydrate Binding ◽  
Salt Tolerant ◽  
Excellent Thermal Stability ◽  
Moderately Thermophilic

β-1,3 xylanase is an important enzyme in the biorefinery process for some algae. The discovery and characterization of new β-1,3 xylanase is a hot research topic. In this paper, a novel β-1,3 xylanase (Xyl88) is revealed from the annotated genome of Flammeovirga pacifica strain WPAGA1. Bioinformatic analysis shows that Xyl88 belongs to the glycoside hydrolase 26 (GH26) with a suspected CBM (carbohydrate-binding module) sequence. The activity of rXyl88 is 75% of the highest enzyme activity (1.5 mol/L NaCl) in 3 mol/L NaCl buffer, which suggests good salt tolerance of rXy188. The optimum reaction temperature in the buffer without NaCl and with 1.5 mol/L NaCl is 45 °C and 55 °C, respectively. Notably, the catalytic efficiency of rXyl88 (kcat/Km) is approximately 20 higher than that of the thermophilic β-1,3 xylanase that has the highest catalytic efficiency. Xyl88 in this study becomes the most efficient enzyme ever found, and it is also the first reported moderately thermophilic and salt-tolerant β-1,3 xylanase. Results of molecular dynamics simulation further prove the excellent thermal stability of Xyl88. Moreover, according to the predicted 3D structure of the Xyl88, the surface of the enzyme is distributed with more negative charges, which is related to its salt tolerance, and significantly more hydrogen bonds and Van der Waals force between the intramolecular residues, which is related to its thermal stability.

scholarly journals ISOLATION, PURIFICATION, AND CHARACTERIZATION OF LIPASE FROM BACILLUS SP. FROM KITCHEN GREASE

2018 ◽  
Vol 11 (6) ◽  
pp. 224
Author(s):  
Jaiganesh R ◽  
Jaganathan Mk
Keyword(s):  
16S Rdna ◽  
Solvent Tolerance ◽  
16S Rdna Sequencing ◽  
Bacillus Sp ◽  
Purification And Characterization ◽  
Lipase Enzyme ◽  
Sequencing Method ◽  
Rdna Sequencing ◽  
Solvent Tolerant

Objective: The objective of this work was to isolation, purification and characterization of solvent tolerant lipase from Bacillus sp. The objective of this work was to isolation, purification and characterization of solvent tolerant lipase from Bacillus sp. from kitchen grease for a variety of applications including organic synthetic reactions and preparation of enantiomerically pure pharmaceuticals.Methods: Lipase producing isolates were screened from kitchen grease on a selective medium rhodamine B olive oil agar, and tributyrin agar was used to screen the lipase and esterase producing an organism, respectively. The isolate identified using 16S rDNA sequencing method and enzyme activity was quantitatively assayed. Lipase production was characterized in different conditions.Results: The isolate showed highest lipase activity was which later was identified as Bacillus sp. using 16S rDNA sequencing method. The lipase was purified using ammonium sulfate precipitation. The isolate showed excellent tolerance to methanol, ethanol, acetonitrile, and moderate tolerance to butanol. The increased biomass concentration, maximum production, and activity were achieved at 37°C in 24 h incubation, then gradual reduction in production was observed. The maximum activity of lipase enzyme was obtained at pH between 6 and 9.Conclusion: The isolate produce solvent tolerance lipase enzyme and it can be a promising candidate of solvent tolerance lipase enzyme for variety of industrial applications.

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