98%
921
2 minutes
20
The DNA extracted from a high-temperature environment in which micro-organisms are living will be a good source for the isolation of thermostable enzymes. Using a metagenomic approach, we aimed to isolate thermostable β-xylosidases that will be exploited for biofuel production from lignocellulosic biomass. DNA samples obtained from the soil near a spout of a hot spring (70°C, pH7.2) were subjected to sequencing, which generated a total of 84.2 Gbp with 967,925 contigs of >500 bp in length. Similarity search for β-xylosidase in the contigs revealed the presence of 168 candidate sequences, each of which may have arisen from more than one gene. Individual genes were amplified by PCR using sequence-specific primers. The resultant DNA fragments were cloned and introduced into Escherichia coli BL21 Star(DE3). Consequently, 269 proteins were successfully expressed in the E. coli cells and then examined for β-xylosidase activity. A total of 82 proteins exhibited β-xylosidase activity at 50°C, six of which retained the activity even at 90°C. Out of the six, three proteins were originated from a single candidate sequence, AR19M-311. An amino acid sequence comparison suggested the amino acid residues that appeared to be crucial for thermal stability of the enzymes.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5726482 | PMC |
http://dx.doi.org/10.1093/dnares/dsx032 | DOI Listing |
J Biomol Struct Dyn
September 2025
Department of Biology, Faculty of Science, University of Sistan and Baluchestan, Zahedan, Iran.
Acetylesterase, produced by , plays a crucial role in deacetylating hemicellulose during pulp production. Thermostable variants of this enzyme, although rare, can significantly enhance industrial efficiency by retaining activity at high temperatures. This research aims to design a thermostable variant of acetylesterase from (EC 3.
View Article and Find Full Text PDFJ Agric Food Chem
September 2025
School of Chemical Engineering and Technology, Zhengzhou University, Zhengzhou 450001, China.
d-Amino acid oxidase from (DAAO) is valuable for pharmaceutical and chemical synthesis due to its high enantioselectivity, but its poor thermostability limits extensive application. This study proposed a synergistic strategy of "sequence consensus design coupled with structure modification" to enhance DAAO thermostability. Through homologous sequence analysis and greedy algorithm-based optimization, a triple mutant M3 (S18T/V7I/Y132F) was obtained, showing a 3.
View Article and Find Full Text PDFAppl Environ Microbiol
September 2025
Biofuels Institute, School of Emergency Management, School of the Environment and Safety Engineering, Jiangsu University, Zhenjiang, Jiangsu, PR China.
is a thermophilic acetogenic bacterium capable of thriving at elevated temperatures up to 66°C. It metabolizes carbohydrates such as glucose, mannose, and fructose and can also grow lithotrophically utilizing hydrogen (H) and carbon dioxide (CO) or carbon monoxide (CO), with acetate serving as its main product. A simple and efficient genome editing system for would not only facilitate the understanding of the physiological function of enzymes involved in energy and carbon metabolism but also enable metabolic engineering.
View Article and Find Full Text PDFJ Biomol Struct Dyn
September 2025
Enzyme and Microbial Technology Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
A thermostable paraoxonase (S3wahi-PON) from sp. strain S3wahi was recently characterised and shown to possess stability across a broad temperature range. This study expands upon the initial biochemical characterisation of S3wahi-PON by investigating the structural determinants and conformational adaptability that contribute to its thermostability, using an integrated approach that combines biophysical techniques and molecular dynamics (MD) simulations across a temperature range of 10 °C to 90 °C.
View Article and Find Full Text PDFBiochem Biophys Res Commun
September 2025
Beamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai, 400085, India. Electronic address:
The UPF0235 UniProt family proteins are conserved across archaea, bacteria, and eukaryotes; however, they remain functionally uncharacterized. Here, we report the high resolution (1.3 Å) crystal structure of UPF0235 protein (PF1765, UniProt: Q8U052) from Pyrococcus furiosus.
View Article and Find Full Text PDF