scholarly journals A ‘Split-Gene’ Transketolase From the Hyper-Thermophilic Bacterium Carboxydothermus hydrogenoformans: Structure and Biochemical Characterization

2020 ◽  
Vol 11 ◽  
Author(s):  
Paul James ◽  
Michail N. Isupov ◽  
Simone Antonio De Rose ◽  
Christopher Sayer ◽  
Isobel S. Cole ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Thermophilic Bacterium ◽  
Split Gene ◽  
Carboxydothermus Hydrogenoformans

Identification, Heterologous Expression and Biochemical Characterization of a Novel Cellulase-free Xylanase B from the Thermophilic Bacterium Cohnella sp.A01

2021 ◽  
Author(s):  
Hemad Rahimian Gavaseraei ◽  
Raheleh Hasanzadeh ◽  
Moslem Afsharnezhad ◽  
Ali Foroutan Kalurazi ◽  
S. Shirin Shahangian ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Biochemical Characterization ◽  
Thermophilic Bacterium

scholarly journals A Lysine Substitute for K+

2002 ◽  
Vol 277 (51) ◽  
pp. 49651-49654 ◽  
Author(s):  
Georgiy A. Belogurov ◽  
Reijo Lahti
Keyword(s):  
Escherichia Coli ◽  
Heterologous Expression ◽  
Phylogenetic Analyses ◽  
Functional Characterization ◽  
Membrane Vesicles ◽  
Thermophilic Bacterium ◽  
Inorganic Pyrophosphatase ◽  
Inner Membrane ◽  
Carboxydothermus Hydrogenoformans

The H+proton-translocating inorganic pyrophosphatase (H+-PPase) family is composed of two phylogenetically distinct types of enzymes: K+-dependent and K+-independent. However, to date, the sequence criteria governing this dichotomy have remained unknown. In this study, we describe the heterologous expression and functional characterization of H+-PPase from the thermophilic bacteriumCarboxydothermus hydrogenoformans. Both PPi-hydrolyzing and PPi-energized H+translocation activities of the recombinant enzyme inEscherichia coliinner membrane vesicles are strictly K+-dependent. Here we deduce the K+requirement of all available H+-PPase sequences based on the K+dependence ofC. hydrogenoformansH+-PPase in conjunction with phylogenetic analyses. Our data reveal that K+-independent H+-PPases possess conserved Lys and Thr that are absent in K+-dependent H+-PPases. We further demonstrate that a A460K substitution inC. hydrogenoformansH+-PPase is sufficient to confer K+independence to both PPihydrolysis and PPi-energized H+translocation. In contrast, a A463T mutation does not affect the K+dependence of H+-PPase.

scholarly journals Expression and Characterization ofCoprothermobacter proteolyticusAlkaline Serine Protease

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Tanveer Majeed ◽  
Romana Tabassum ◽  
William J. Orts ◽  
Charles C. Lee
Keyword(s):  
Bacillus Subtilis ◽  
Serine Protease ◽  
Biochemical Characterization ◽  
Thermophilic Bacterium ◽  
Protease Gene ◽  
Optimum Temperature ◽  
Optimal Activity ◽  
Potential Applications ◽  
Alkaline Conditions ◽  
Putative Protease

A putative protease gene (aprE) from the thermophilic bacteriumCoprothermobacter proteolyticuswas cloned and expressed inBacillus subtilis. The enzyme was determined to be a serine protease based on inhibition by PMSF. Biochemical characterization demonstrated that the enzyme had optimal activity under alkaline conditions (pH 8–10). In addition, the enzyme had an elevated optimum temperature (60°C). The protease was also stable in the presence of many surfactants and oxidant. Thus, theC. proteolyticusprotease has potential applications in industries such as the detergent market.

scholarly journals Comparative Analysis and Biochemical Characterization of Two Endo-β-1,3-Glucanases from the Thermophilic Bacterium Fervidobacterium sp.

Catalysts ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 830 ◽  
Author(s):  
Burkhardt ◽  
Schäfers ◽  
Claren ◽  
Schirrmacher ◽  
Antranikian
Keyword(s):  
Elevated Temperatures ◽  
Biochemical Characterization ◽  
Hot Spring ◽  
Biomass Conversion ◽  
Catalytic Efficiency ◽  
Industrial Applications ◽  
Thermophilic Bacterium ◽  
Metagenomic Sample ◽  
Wide Range ◽  
Active Site Cleft

Laminarinases exhibit potential in a wide range of industrial applications including the production of biofuels and pharmaceuticals. In this study, we present the genetic and biochemical characteristics of FLamA and FLamB, two laminarinases derived from a metagenomic sample from a hot spring in the Azores. Sequence comparison revealed that both genes had high similarities to genes from Fervidobacterium nodosum Rt17-B1. The two proteins showed sequence similarities of 62% to each other and belong to the glycoside hydrolase (GH) family 16. For biochemical characterization, both laminarinases were heterologously produced in Escherichia coli and purified to homogeneity. FLamA and FLamB exhibited similar properties and both showed highest activity towards laminarin at 90 °C and pH 6.5. The two enzymes were thermostable but differed in their half-life at 80 °C with 5 h and 1 h for FLamA and FLamB, respectively. In contrast to other laminarinases, both enzymes prefer β-1,3-glucans and mixed-linked glucans as substrates. However, FLamA and FLamB differ in their catalytic efficiency towards laminarin. Structure predictions were made and showed minor differences particularly in a kink adjacent to the active site cleft. The high specific activities and resistance to elevated temperatures and various additives make both enzymes suitable candidates for application in biomass conversion.

scholarly journals Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Xiaojing Jia ◽  
Weibo Qiao ◽  
Wenli Tian ◽  
Xiaowei Peng ◽  
Shuofu Mi ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Thermophilic Bacterium

Structural and biochemical characterization of a nitrilase from the thermophilic bacterium, Geobacillus pallidus RAPc8

2010 ◽  
Vol 88 (1) ◽  
pp. 143-153 ◽  
Author(s):  
Dael S. Williamson ◽  
Kyle C. Dent ◽  
Brandon W. Weber ◽  
Arvind Varsani ◽  
Joni Frederick ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Thermophilic Bacterium ◽  
Geobacillus Pallidus

Plant Pathology Diagnosed by X-Ray Microanalysis

1987 ◽  
Vol 45 ◽  
pp. 974-975
Author(s):  
J. H. Resau ◽  
N. Howell ◽  
S. H. Chang
Keyword(s):  
Electron Microscopy ◽  
Plant Pathology ◽  
Biochemical Characterization ◽  
Nutrient Deficiency ◽  
Green Leaf ◽  
Parasitic Infestation ◽  
X Ray

Spinach grown in Texas developed “yellow spotting” on the peripheral portions of the leaves. The exact cause of the discoloration could not be determined as there was no evidence of viral or parasitic infestation of the plants and biochemical characterization of the plants did not indicate any significant differences between the yellow and green leaf portions of the spinach. The present study was undertaken using electron microscopy (EM) to determine if a micro-nutrient deficiency was the cause for the discoloration.Green leaf spinach was collected from the field and sent by express mail to the EM laboratory. The yellow and equivalent green portions of the leaves were isolated and dried in a Denton evaporator at 10-5 Torr for 24 hrs. The leaf specimens were then examined using a JEOL 100 CX analytical microscope. TEM specimens were prepared according to the methods of Trump et al.

Sign in / Sign up

Export Citation Format

Share Document