Thermophiles organization

Yogurt. Yogurt is a fermented milk product that is rapidly increasing in consumption in the United States. Milk is fermented with Uactobacillus bulgaricus and Streptococcus thermophilous organisms that produce lactic acid. Usually some cream or nonfat dried milk is added to the milk in order to obtain a heavy-bodied product. 

Recently, several thermophilic organisms have been reported to be capable of sulfur-specific biodesulfurization. These include the Paenibacillus [87,151], Mycobacterium [30,31,85,94,294,295], etc. The ability to desulfurize sulfur compounds other than DBT derivatives, including benzothiophene, naphthothiophene, and benzonaphthothio-phene derivatives has also been demonstrated, thus widening the substrate specificity of the biodesulfurization process. Second, the thermophilic ability of the organisms offers temperature and operational advantages to further improve the commercialization potential of the BDS process. 

Kargi, F., and Robinson, J. M., Microbial Oxidation of Dibenzothiophene by the Thermophilic Organism Sulfolobus Acidocaldarius. Biotechnology and Bioengineering, 1984. 26 p. 687. 

Several NMR studies have been carried out in order to reveal the three-dimensional structure of CBMs and to understand the mechanism by which CBMs from thermophilic organisms bind to their polysaccharide ligands (CBM22, CBM4, and CBM4-2 ). It has been found that CBMs are composed mainly of jS-strand and contain a planar hydrophobic platform comprising aromatic residues that bind to the surface of the polysaccharide. 

In the context of the desirability of removing sulfur compounds from fuels, a bacterial strain has been identified that will metabolize thianthrene to water-soluble products under aerobic conditions (83MI5). A thermophilic organism, Sulfolobus acidocaldarius, removed 38% of the sulfur, as measured by sulfate release, in 4 weeks at 70°C (87MI2). 

Sequence comparisons may also suggest new ligands. Recently, the complete amino acid sequence for a ferredoxin from the thermophilic organism Pyrococcus furiosus was determined (Eccleston et al., 1991). All... 

When looking for a suitable biocatalyst, one has also to consider the (operational) activity that is required for commercial application and the operational conditions that will be used in the process (e.g. temperature, salt concentration, pH, organic solvents, substrate and product concentration) will have to be addressed as well. If the reaction is optimally performed at for instance high temperatures, thermophilic organisms are more likely to provide the desired enzymes than mesophilic strains (see paragraph 5.4.1). And vice versa, /isychrophiles operate well at lower temperatures and, since they do not require excessive heat treatment to be inactivated, are easily killed following the process. 

In Thermotoga maritima, the most thermophilic organism known, tungsten promotes synthesis of an Fe-contain-ing hydrogenase as well as some other enzymes but seems to have a regulatory rather than a structural role.688... 

Biological oxygen demand (BOD) Pseudomonas sp., Bacillus subtilus, Trichosporon cutaneum, Thermophilic organisms 86,87,88,89 90... 

Some good hints to help answer this question have been obtained by studying thermophilic proteins which are in turn obtained from thermophilic organisms. The optimum growth temperature for thermophilic organisms is between 40° and 65°C (moderate thermophiles) and 70° and 105°C (extreme thermophiles). Their respective enzymes have catalytically indistinguishable reactivity and catalytic sites from those isolated from mesophilic organisms. 

Although assays based on the retention of room temperature activity after heat treatment are convenient, the constraints imposed during the laboratory evolution can be quite different Ifom anything an enzyme in a natural thermophilic organism might have encountered. Retaining activity at moderate temperatures is probably not relevant for enzymes... 

Summit, M., Scott, B., Nielson, K., Mathur, E., and Baross, J.A. 1998. Pressure enhances thermal stability of DNA polymerase from three thermophilic organisms. Extremophiles 2 339-345. 

Acidophilic and thermophilic organisms and their enzymes in the stabilization of chemistry. Stabilization of enzymes. 

A thermostable dimer was therefore considered as an alternative starting point for the design of a stable monomeric mutase. A large number of EcCM sequence homo-logues, some from thermophilic organisms, are known. For example, the hyperther-mophilic archaeon Methanococcus jannaschii produces a chorismate mutase (MjCM) that is 25 °C more stable than EcCM [37]. Despite only 21 % sequence identity, six prominent residues that line the active site are strictly conserved and the two enzymes have comparable activities. Since the hydrophobic core of MjCM is very similar to that of EcCM, interactions distant from the dimer interface must be responsible for its additional stability. These same interactions were expected to stabilize the desired monomer. 

Knowing that peptides and amines confer thermal stability on enzymes from certain thermophilic organisms (47-49) led some workers to examine protein stabilization by antibodies. It was found that the presence of specific polyclonal antibodies stabilize several enzymes (50, 51). In addition, not only did antibodies increjise the thermostability of a-amylase, glucoamylase, and subtilisin, but some stability toward acid denaturation, oxidizing agent, and organic solvent exposure was increased in specific cases (52, 53). 

---