Thermus thermophilus ATCC 33923 contains a thermostable enzyme that can efficiently catalyze the conversion of maltose into trehalose. Here we report a 2.15-Mb assembly of its genome sequence and other useful information, including the coding sequences (CDS) responsible for biological processes such as DNA replication, DNA repair, and RNA maturation.

INTRODUCTIONThis protocol describes the oligonucleotide ligation assay (OLA), which uses a set of three oligonucleotides, in combination with a thermostable Taq DNA ligase enzyme, to discriminate single-nucleotide polymorphism (SNP) alleles. Sixteen-plex OLA genotyping reactions are carried out, and allele-specific OLA products are detected on membrane arrays using radiolabeled probes.

A thermostable lytic endopeptidase from Bacillus stearothermophilus 1503-4R was purified 14,500-fold, with a 34% recovery of lytic activity. The enzyme is a basic protein (pI, 9.7) with a molecular weight of 15,100 and is composed of approximately 129 amino acid residues.

A bacterial strain was isolated from dhal industry red gram waste and identified as Bacillus. A thermostable extracellular amylase was partially purified from the strain. Optimum temperature and pH for the enzyme were found to be 60°C and 6.5, respectively. The maximum amylase production was achieved with maltose as carbon source. Among the nitrogen sources, peptone and yeast extract produced m...

Directed evolution of p-nitrobenzyl esterase (pNB E) has yielded eight generations of increasingly thermostable variants. The most stable esterase, 8G8, has 13 amino acid substitutions, a melting temperature 17 degrees C higher than the wild-type enzyme, and increased hydrolytic activity toward p-nitrophenyl acetate (pNPA), the substrate used for evolution, at all temperatures. Room-temperature...

In general, the enzymes of thermophilic organisms are more resistant to thermal denaturation than are those of mesophilic or psychrophilic organisms. Further, as is true for their mesophilic and psychrophilic counterparts, the activities of thermophilic enzymes are smaller at temperatures that are less than the optimal temperature. In an effort to characterize the properties that would improve ...

1. The effect of temperature on the conformation of the protease from Bacillus thermoproteolyticus was examined. 2. The thermostable enzyme is stable at room temperature against such denaturing reagents as urea, alcohol, and detergent. 3. However, these reagents accelerate the denaturation of the enzyme by heat. Materials-The crystalline protease of B. thermoproteolyticus was kindly supplied by...

background: today a large number of bacterial amylases are available commercially in industry. the goal of the present study was purification and biochemical characterization of an extracellular thermostable alkaline α-amylase from the novel moderately halophilic, bacillus persicus from the aran-bidgol, iran.   methods : purification of enzyme, was carried out by acetone precipitation, ultrafil...

Lk2 and Lk3 were thermostable recombinant lipase highly expressed in Escherichia coli BL21 (DE3). However, accumulated as an inclusion body. To further characterize both lipases, the soluble enzyme must be obtained first. This study aimed to optimize disruption of cell membrane order obtain active lipases. The effects temperature lysis, pH, SDS concentration on lipolytic activity investigated u...