Isolation, Expression and Characterization of the Thermophilic Recombinant Esterase from Geobacillus thermodenitrificans PS01

2020 ◽  
Vol 191 (1) ◽  
pp. 112-124
Author(s):  
Po-Ting Chen ◽  
Cheng-Huan Liu ◽  
Yu-Ting Chen ◽  
Fang-Yu Hsu ◽  
Jei-Fu Shaw
Keyword(s):  
Geobacillus Thermodenitrificans

Characterization of a mannose-6-phosphate isomerase from Geobacillus thermodenitrificans that converts monosaccharides

2009 ◽  
Vol 31 (8) ◽  
pp. 1273-1278 ◽  
Author(s):  
Soo-Jin Yeom ◽  
Nam-Hee Kim ◽  
Ran-Young Yoon ◽  
Hyun-Jung Kwon ◽  
Chang-Su Park ◽  
...  
Keyword(s):  
Geobacillus Thermodenitrificans ◽  
Mannose 6 Phosphate

Characterization of a F280N variant of l-arabinose isomerase from Geobacillus thermodenitrificans identified as a d-galactose isomerase

2014 ◽  
Vol 98 (22) ◽  
pp. 9271-9281 ◽  
Author(s):  
Baek-Joong Kim ◽  
Seung-Hye Hong ◽  
Kyung-Chul Shin ◽  
Ye-Seul Jo ◽  
Deok-Kun Oh
Keyword(s):  
Geobacillus Thermodenitrificans ◽  
Arabinose Isomerase

scholarly journals Cloning, purification and characterization of halotolerant xylanase from Geobacillus thermodenitrificans C5

2016 ◽  
Vol 05 (06) ◽  
pp. 523-529 ◽  
Author(s):  
Muhammad Irfan ◽  
Halil Ibrahim Guler ◽  
Aamer Ali Shah ◽  
Fulya Ay Sal ◽  
Kadriye Inan ◽  
...  
Keyword(s):  
Geobacillus Thermodenitrificans ◽  
Purification And Characterization

Microbial and genomic characterization of Geobacillus thermodenitrificans OS27, a marine thermophile that degrades diverse raw seaweeds

2018 ◽  
Vol 102 (11) ◽  
pp. 4901-4913 ◽  
Author(s):  
Kenta Fujii ◽  
Yurie Tominaga ◽  
Jyumpei Okunaka ◽  
Hisashi Yagi ◽  
Takashi Ohshiro ◽  
...  
Keyword(s):  
Geobacillus Thermodenitrificans ◽  
Genomic Characterization

scholarly journals Characterization of a Mannose-6-Phosphate Isomerase fromThermus thermophilusand Increased l-Ribose Production by Its R142N Mutant

2010 ◽  
Vol 77 (3) ◽  
pp. 762-767 ◽  
Author(s):  
Soo-Jin Yeom ◽  
Eun-Sun Seo ◽  
Bi-Na Kim ◽  
Yeong-Su Kim ◽  
Deok-Kun Oh
Keyword(s):  
Specific Activity ◽  
Thermus Thermophilus ◽  
Catalytic Efficiency ◽  
Maximal Activity ◽  
Wild Type ◽  
Active Site Residues ◽  
Geobacillus Thermodenitrificans ◽  
Wild Type Enzyme ◽  
Mannose 6 Phosphate

ABSTRACTAn uncharacterized gene fromThermus thermophilus, thought to encode a mannose-6-phosphate isomerase, was cloned and expressed inEscherichia coli. The maximal activity of the recombinant enzyme forl-ribulose isomerization was observed at pH 7.0 and 75°C in the presence of 0.5 mM Cu2+. Among all of the pentoses and hexoses evaluated, the enzyme exhibited the highest activity for the conversion ofl-ribulose tol-ribose, a potential starting material for manyl-nucleoside-based pharmaceutical compounds. The active-site residues, predicted according to a homology-based model, were separately replaced with Ala. The residue at position 142 was correlated with an increase inl-ribulose isomerization activity. The R142N mutant showed the highest activity among mutants modified with Ala, Glu, Tyr, Lys, Asn, or Gln. The specific activity and catalytic efficiency (kcat/Km) forl-ribulose using the R142N mutant were 1.4- and 1.6-fold higher than those of the wild-type enzyme, respectively. Thekcat/Kmof the R142N mutant was 3.8-fold higher than that ofGeobacillus thermodenitrificansmannose-6-phosphate isomerase, which exhibited the highest activity to date for the previously reportedkcat/Km. The R142N mutant enzyme produced 213 g/literl-ribose from 300 g/literl-ribulose for 2 h, with a volumetric productivity of 107 g liter−1h−1, which was 1.5-fold higher than that of the wild-type enzyme.

Sign in / Sign up

Export Citation Format

Share Document