Journal articles: 'Thermophilic'

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Birajdar, G. M., and Udhav Bhale. "PRODUCTION OF ENZYMES IN PREDOMINANT THERMOPHILIC FUNGI AVAILABLE FROM ORGANIC SUBSTRATES." International Journal of Scientific Research and Management 9, no. 11 (November 10, 2021): 174–83. http://dx.doi.org/10.18535/ijsrm/v9i11.b01.

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Present investigation describes that the study site comes under Aurangabad Division Maharashtra and it falls in Deccan Plateau Zone of India. It was collected different types of organic substrates viz. vermiompost, poultary manure, baggase, farm yard manure (FYM), soil, Ash etc. Isolated thermophilic predominant fungi thermophilic fungi viz.Aspergillus niger, Mucor mucedo,Humicola insolens,Trichoderma harzianum,T. viride,Penicillium duponti,Fusarium oxysporun and Chaetomium thermophilum were carried out for the production of enzymes. Isolated predominant thermophilic fungi were evaluated on different types of enzymes. Among tested thermophilic fungi, the highest ativity was observed in C. thermophilium (20mm) followed by T. harzianum (19.50mm) In lipase, M. mucedo (15.40mm) was found maximum followed by F. oxysporun. Cellulase activity was found highest in A. nige (25mm) followed by others. In case of xylanase, catalase, peroxidase and esterase activities were found maximum, minimum and medium even negative in some fungi. Maximum pectinase activity was detected from H. insolens (52.26 @ 0 min) and (74.25 @ 10 min) and in case of M. mucedo, F. oxysporun and C. thermophilium was found most extreme while least in A. niger (30.12) and P. duponti (33.47) @ 0 minute. Key words: Organic Substrates, Thermophilic Fungi, Enzymes

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Hori, Hiroyuki, Takuya Kawamura, Takako Awai, Anna Ochi, Ryota Yamagami, Chie Tomikawa, and Akira Hirata. "Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA." Microorganisms 6, no. 4 (October 20, 2018): 110. http://dx.doi.org/10.3390/microorganisms6040110.

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To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially in steps of protein synthesis at high temperatures. At high temperatures, the structure of unmodified tRNA will be disrupted. Therefore, thermophiles must possess strategies to stabilize tRNA structures. To this end, several thermophile-specific modified nucleosides in tRNA have been identified. Other factors such as RNA-binding proteins and polyamines contribute to the stability of tRNA at high temperatures. Thermus thermophilus, which is an extreme-thermophilic eubacterium, can adapt its protein synthesis system in response to temperature changes via the network of modified nucleosides in tRNA and tRNA modification enzymes. Notably, tRNA modification enzymes from thermophiles are very stable. Therefore, they have been utilized for biochemical and structural studies. In the future, thermostable tRNA modification enzymes may be useful as biotechnology tools and may be utilized for medical science.

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Vavitsas, Konstantinos, Panayiotis D. Glekas, and Dimitris G. Hatzinikolaou. "Synthetic Biology of Thermophiles: Taking Bioengineering to the Extremes?" Applied Microbiology 2, no. 1 (February 14, 2022): 165–74. http://dx.doi.org/10.3390/applmicrobiol2010011.

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Synthetic biology applications rely on a well-characterized set of microbial strains, with an established toolbox of molecular biology methods for their genetic manipulation. Since there are no thermophiles with such attributes, most biotechnology and synthetic biology studies use organisms that grow in the mesophilic temperature range. As a result, thermophiles, a heterogenous group of microbes that thrive at high (>50 °C) temperatures, are largely overlooked, with respect to their biotechnological potential, even though they share several favorable traits. Thermophilic bacteria tend to grow at higher rates compared to their mesophilic counterparts, while their growth has lower cooling requirements and is less prone to contamination. Over the last few years, there has been renewed interest in developing tools and methods for thermophile bioengineering. In this perspective, we explain why it is a good idea to invest time and effort into developing a thermophilic synthetic biology direction, which is the state of the art, and why we think that the implementation of a thermophilic synthetic biology platform—a thermochassis—will take synthetic biology to the extremes.

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Borzova, N. V., O. V. Gudzenko, K. V. Avdiyuk, L. D. Varbanets, and L. T. Nakonechna. "Thermophilic Fungi with Glucosidase and Proteolytic Activities." Mikrobiolohichnyi Zhurnal 83, no. 3 (June 17, 2021): 24–34. http://dx.doi.org/10.15407/microbiolj83.03.024.

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The directed search for extremophilic producers in order to obtain hydrolytic enzymes with increased thermal stability has an unconditional practical potential for use in the food and feed industry to improve the quality of the final product. The aim of the work was to study the ability of collection strains of thermophilic fungi to show α-L-rhamnosidase, α-galactosidase, cellulase, β-mannanase, keratinase and caseinolytic activity. Methods. Micromycetes were grown under submerged conditions in test tubes at 42°C for 8–14 days. Enzymatic activities were studied in the culture liquid supernatant. p-Nitrophenyl-α-D-galactopyranoside, naringin, guar gum galactomannan and Na-carboxymethylcellulose were used as substrates to determine α-galactosidase, α-L-rhamnosidase, β-mannanase and cellulase activities, respectively. Casein and crushed defatted feathers were served as substrates for the determination of proteolytic activity. Results. The enzymatic activity of 50 strains of micromycetes belonging to 17 species was investigated. The studied group showed high activity: 94% of the strains had at least one, 34% – two, 26% – from three to five enzyme activities. The most active keratinase producers were Thielavia terrestris 1920 and 62, Rhizomucor tauricus 1909, Chrysosporium thermophilum 2050, Thermoascus thermophilus 92 and Thermoascus aurantiаcus 2052 (10–26 U/mL). The highest α-L-rhamnosidase activity was observed in T. terrestris 62 (0.35 U/mL), and carboxymethylcellulase activity −in Thermomyces lanuginosus 2046. Six strains showed α-galactosidase (0.05–0.2 U/mL) and four strains − β-mannanase (5–130 U/mL) activity. Conclusions. As a result new strains producing proteolytic and glycolytic enzymes were isolated among thermophilic micromycetes. Soil thermophilic micromycetes can be used as producers of proteolytic and glycolytic enzymes. Of particular interest are the cultures of Acremonium thermophilum 1963, Corynascus thermophilum 2050, C. sepedonium 1899 and 65068, T. thermophilus 1946, which are capable of producing complexes of proteases and glycosidases in the culture liquid. This indicates that these strains are promising for use as destructors in various technologies processing of complex raw materials.

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Kushkevych, Ivan, Jiří Cejnar, Monika Vítězová, Tomáš Vítěz, Dani Dordević, and Yannick J. Bomble. "Occurrence of Thermophilic Microorganisms in Different Full Scale Biogas Plants." International Journal of Molecular Sciences 21, no. 1 (December 31, 2019): 283. http://dx.doi.org/10.3390/ijms21010283.

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Background: In recent years, various substrates have been tested to increase the sustainable production of biomethane. The effect of these substrates on methanogenesis has been investigated mainly in small volume fermenters and were, for the most part, focused on studying the diversity of mesophilic microorganisms. However, studies of thermophilic communities in large scale operating mesophilic biogas plants do not yet exist. Methods: Microbiological, biochemical, biophysical methods, and statistical analysis were used to track thermophilic communities in mesophilic anaerobic digesters. Results: The diversity of the main thermophile genera in eight biogas plants located in the Czech Republic using different input substrates was investigated. In total, 19 thermophilic genera were detected after 16S rRNA gene sequencing. The highest percentage (40.8%) of thermophiles was found in the Modřice biogas plant where the input substrate was primary sludge and biological sludge (50/50, w/w %). The smallest percentage (1.87%) of thermophiles was found in the Čejč biogas plant with the input substrate being maize silage and liquid pig manure (80/20, w/w %). Conclusions: The composition of the anaerobic consortia in anaerobic digesters is an important factor for the biogas plant operator. The present study can help characterizing the impact of input feeds on the composition of microbial communities in these plants.

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Wackett, Lawrence P. "Thermophiles and thermophilic enzymes." Microbial Biotechnology 4, no. 6 (October 14, 2011): 799–800. http://dx.doi.org/10.1111/j.1751-7915.2011.00311.x.

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Tang, Jie, Huizhen Zhou, Dan Yao, Lianming Du, and Maurycy Daroch. "Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria." International Journal of Molecular Sciences 24, no. 6 (March 15, 2023): 5632. http://dx.doi.org/10.3390/ijms24065632.

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Thermophilic cyanobacteria are cosmopolitan and abundant in the thermal environment. Their light-harvesting complexes, phycobilisomes (PBS), are highly important in photosynthesis. To date, there is limited information on the PBS composition of thermophilic cyanobacteria whose habitats are challenging for survival. Herein, genome-based methods were used to investigate the molecular components of PBS in 19 well-described thermophilic cyanobacteria. These cyanobacteria are from the genera Leptolyngbya, Leptothermofonsia, Ocullathermofonsia, Thermoleptolyngbya, Trichothermofonsia, Synechococcus, Thermostichus, and Thermosynechococcus. According to the phycobiliprotein (PBP) composition of the rods, two pigment types are observed in these thermophiles. The amino acid sequence analysis of different PBP subunits suggests several highly conserved cysteine residues in these thermophiles. Certain amino acid contents in the PBP of thermophiles are significantly higher than their mesophilic counterparts, highlighting the potential roles of specific substitutions of amino acid in the adaptive thermostability of light-harvesting complexes in thermophilic cyanobacteria. Genes encoding PBS linker polypeptides vary among the thermophiles. Intriguingly, motifs in linker apcE indicate a photoacclimation of a far-red light by Leptolyngbya JSC-1, Leptothermofonsia E412, and Ocullathermofonsia A174. The composition pattern of phycobilin lyases is consistent among the thermophiles, except for Thermostichus strains that have extra homologs of cpcE, cpcF, and cpcT. In addition, phylogenetic analyses of genes coding for PBPs, linkers, and lyases suggest extensive genetic diversity among these thermophiles, which is further discussed with the domain analyses. Moreover, comparative genomic analysis suggests different genomic distributions of PBS-related genes among the thermophiles, indicating probably various regulations of expression. In summary, the comparative analysis elucidates distinct molecular components and organization of PBS in thermophilic cyanobacteria. These results provide insights into the PBS components of thermophilic cyanobacteria and fundamental knowledge for future research regarding structures, functions, and photosynthetic improvement.

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Allgood, Gregory S., and Jerome J. Perry. "Oxygen defense systems in obligately thermophilic bacteria." Canadian Journal of Microbiology 31, no. 11 (November 1, 1985): 1006–10. http://dx.doi.org/10.1139/m85-190.

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Ten strains of Gram-negative, aerobic, obligately thermophilic bacteria were examined for their response to oxygen toxicity by comparing static with shaken cultures. All of the organisms tested had measurable levels of superoxide dismutase, catalase, and peroxidase. Aeration generally did not result in an increased level of superoxide dismutase in any of the thermophiles. Aeration of organisms obligate for n-alkane substrate caused an increase in cellular peroxidase levels and a corresponding decrease in catalase. The thermophiles that grew on either n-alkanes or complex media did not grow on the hydrocarbon in aerated culture but on a complex medium, aeration effected an increased level of catalase. With the exception of a pink-pigmented thermophile which, when aerated, did not have an increased level of the three oxygen defense enzymes, most of the thermophiles surveyed had an increased level of catalase or peroxidase when exposed to increased oxygen tension. The activity of the enzymes was determined at temperatures from 25 to 65 °C and the former temperature was satisfactory for these experiments.

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Korehi, Hananeh, and Axel Schippers. "Bioleaching of a Marine Hydrothermal Sulfide Ore with Mesophiles, Moderate Thermophiles and Thermophiles." Advanced Materials Research 825 (October 2013): 229–32. http://dx.doi.org/10.4028/www.scientific.net/amr.825.229.

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Marine hydrothermal polymetallic sulfide ores contain high amounts of valuable metals such as Cu, Pb, Zn, Au, Ag, as well as In, Ge, Bi, and Se. Samples from a site in the Indian Ocean were taken during a BGR ship cruise, crushed and sieved for bioleaching experiments to reveal the extraction of the various metals. Chalcopyrite was the main mineral, the total copper content was 38.5 %wt. Comparative bioleaching with mesophilic, moderate thermophilic and thermophilic acidophilic iron- and sulfur-oxidizing bacteria and archaea was investigated. Batch culture experiments were conducted at 2% (w/v) pulp density in shake flasks in the presence of Acidithiobacillus ferrooxidans, Acidiphilium sp. and Acidithiobacillus thiooxidans as mesophiles (30°C), a mixed culture of moderate thermopilic iron- and sulfur oxidizing bacteria (50°C) and the thermophile Acidianus brierleyi (70°C). The results after four weeks showed most effective dissolution of copper in the presence of A. brierleyi (up to 4.3 g/l), compared with moderate thermophiles and mesophiles (3.3 g/l and 2.5 g/l, respectively). Furthermore, the bioleaching performance was approved with dissolved iron concentrations. Conclusively, an increase in temperature from 30 °C to 70 °C had a major impact on bioleaching efficiency. Copper and iron extraction efficiency occurred in the order thermophiles, moderate thermophiles, mesophiles.

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Joshi, Chetna, and Sunil Kumar Khare. "Induction of xylanase in thermophilic fungi Scytalidium thermophilum and Sporotrichum thermophile." Brazilian Archives of Biology and Technology 55, no. 1 (February 2012): 21–27. http://dx.doi.org/10.1590/s1516-89132012000100003.

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Gregory, Steven T., Jennifer F. Carr, Daniel Rodriguez-Correa, and Albert E. Dahlberg. "Mutational Analysis of 16S and 23S rRNA Genes of Thermus thermophilus." Journal of Bacteriology 187, no. 14 (July 2005): 4804–12. http://dx.doi.org/10.1128/jb.187.14.4804-4812.2005.

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ABSTRACT Structural studies of the ribosome have benefited greatly from the use of organisms adapted to extreme environments. However, little is known about the mechanisms by which ribosomes or other ribonucleoprotein complexes have adapted to functioning under extreme conditions, and it is unclear to what degree mutant phenotypes of extremophiles will resemble those of their counterparts adapted to more moderate environments. It is conceivable that phenotypes of mutations affecting thermophilic ribosomes, for instance, will be influenced by structural adaptations specific to a thermophilic existence. This consideration is particularly important when using crystal structures of thermophilic ribosomes to interpret genetic results from nonextremophilic species. To address this issue, we have conducted a survey of spontaneously arising antibiotic-resistant mutants of the extremely thermophilic bacterium Thermus thermophilus, a species which has featured prominently in ribosome structural studies. We have accumulated over 20 single-base substitutions in T. thermophilus 16S and 23S rRNA, in the decoding site and in the peptidyltransferase active site of the ribosome. These mutations produce phenotypes that are largely identical to those of corresponding mutants of mesophilic organisms encompassing a broad phylogenetic range, suggesting that T. thermophilus may be an ideal model system for the study of ribosome structure and function.

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Angelov, Angel, Susanne Liebl, Meike Ballschmiter, Mechthild Bömeke, Rüdiger Lehmann, Heiko Liesegang, Rolf Daniel, and Wolfgang Liebl. "Genome Sequence of the Polysaccharide-Degrading, Thermophilic Anaerobe Spirochaeta thermophila DSM 6192." Journal of Bacteriology 192, no. 24 (October 8, 2010): 6492–93. http://dx.doi.org/10.1128/jb.01023-10.

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ABSTRACT Spirochaeta thermophila is a thermophilic, free-living anaerobe that is able to degrade various α- and β-linked sugar polymers, including cellulose. We report here the complete genome sequence of S. thermophila DSM 6192, which is the first genome sequence of a thermophilic, free-living member of the Spirochaetes phylum. The genome data reveal a high density of genes encoding enzymes from more than 30 glycoside hydrolase families, a noncellulosomal enzyme system for (hemi)cellulose degradation, and indicate the presence of a novel carbohydrate-binding module.

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DiGiacomo, Juliana, Christopher McKay, and Alfonso Davila. "ThermoBase: A database of the phylogeny and physiology of thermophilic and hyperthermophilic organisms." PLOS ONE 17, no. 5 (May 10, 2022): e0268253. http://dx.doi.org/10.1371/journal.pone.0268253.

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Thermophiles and hyperthermophiles are those organisms which grow at high temperature (> 40°C). The unusual properties of these organisms have received interest in multiple fields of biological research, and have found applications in biotechnology, especially in industrial processes. However, there are few listings of thermophilic and hyperthermophilic organisms and their relevant environmental and physiological data. Such repositories can be used to standardize definitions of thermophile and hyperthermophile limits and tolerances and would mitigate the need for extracting organism data from diverse literature sources across multiple, sometimes loosely related, research fields. Therefore, we have developed ThermoBase, a web-based and freely available database which currently houses comprehensive descriptions for 1238 thermophilic or hyperthermophilic organisms. ThermoBase reports taxonomic, metabolic, environmental, experimental, and physiological information in addition to literature resources. This includes parameters such as coupling ions for chemiosmosis, optimal pH and range, optimal temperature and range, optimal pressure, and optimal salinity. The database interface allows for search features and sorting of parameters. As such, it is the goal of ThermoBase to facilitate and expedite hypothesis generation, literature research, and understanding relating to thermophiles and hyperthermophiles within the scientific community in an accessible and centralized repository. ThermoBase is freely available online at the Astrobiology Habitable Environments Database (AHED; https://ahed.nasa.gov), at the Database Center for Life Science (TogoDB; http://togodb.org/db/thermobase), and in the S1 File.

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Waghmare, Pratima, Nuo Xu, Pankajkumar Waghmare, Guodong Liu, Yinbo Qu, Xuezhi Li, and Jian Zhao. "Production and Characterization of Cellulose Nanocrystals from Eucalyptus Dissolving Pulp Using Endoglucanases from Myceliophthora thermophila." International Journal of Molecular Sciences 24, no. 13 (June 26, 2023): 10676. http://dx.doi.org/10.3390/ijms241310676.

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Endoglucanase (EG) is a key enzyme during enzymatic preparation of cellulose nanocrystals (CNCs). Myceliophthora thermophila is a thermophilic fungus that has thermal properties and a high secretion of endoglucanases (EGs), and could serve as potential sources of EGs for the preparation of CNCs. In this work, four different GH families (GH5, GH7, GH12, and GH45) of EGs from M. thermophila were expressed and purified, and their enzymatic characteristics and feasibility of application in CNC preparation were investigated. It was shown that the MtEG5A from M. thermophila has good potential in the enzymatic preparation of CNCs using eucalyptus dissolving pulp as feedstock. It was also observed that there was a synergistic effect between the MtEG5A and other MtEGs in the preparation of CNCs, which improved the yield and properties of CNCs obtained by enzymatic hydrolysis. This study provides a reference for understanding the enzymatic characteristics of different families of EGs from M. thermophile and their potential application in nanocellulose production.

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Safitri, Ratu, Rika Okta Pylia, and Shabarni Gaffar. "Amylolytic Geobacillus from Kamojang Crater Hot Springs, Garut, Indonesia." Research Journal of Chemistry and Environment 26, no. 10 (September 25, 2022): 62–69. http://dx.doi.org/10.25303/2610rjce062069.

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The hot springs area of Kamojang Crater, Garut Indonesia is a prospective habitat for amylase-producing thermophile bacteria. Researchers have been drawn to thermophilic bacteria because they produce thermostable enzymes that can be used in biotechnological processes. Thermostable enzyme produced by thermophilic bacteria is used extensively in industrial processes. This study aims to isolate and characterize the amylolytic thermophilic bacteria and archaea from Kamojang Crater hot springs, Garut, Indonesia. Samples were grown in Thermus, Luria Bertani and hot spring medium at 70°C and pH 6, characterized morphologically, microscopically, biochemically etc. Two amylolytic thermophilic bacteria HSM6T1 and TM6T2SP1 were successfully identified, which have amylolytic index 1,07 dan 0,31 mm respectively. Molecular identification using 16S rDNA sequencing showed that the HSM6T1 has 99.93% similarity with Geobacillus sp. strain PCH167 and the TM6T2SP1 has 99.86% similarities with Geobacillus thermoleovorans strain CCB-US3-UF5.

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Singh, Richa, Meenu Hans, Sachin Kumar, and Yogender Kumar Yadav. "Thermophilic Anaerobic Digestion: An Advancement towards Enhanced Biogas Production from Lignocellulosic Biomass." Sustainability 15, no. 3 (January 18, 2023): 1859. http://dx.doi.org/10.3390/su15031859.

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Thermophilic anaerobic digestion (TAD) technology has been adopted worldwide mainly due to it being a pathogen-free process in addition to the enhanced biogas yield and short hydraulic retention time (HRT). Taking the high metabolic rate of the thermophilic microbial community with highly efficient enzymatic systems into consideration, thermophiles are being widely explored as efficient inocula for lignocellulosic biomass (LCB) degradation and improved biomethane production. The advantages of TAD over mesophilic anaerobic digestion (MAD), including improved kinetics, efficient degradation of organic matter, and economic and environmental sustainability, make it one of the best strategies to be operated at moderately high temperatures. This review sheds light on the relevant role of thermophilic microorganisms as inocula in the anaerobic digestion of organic matter and factors affecting the overall process stability at high temperatures. Further, the discussion explains the strategies for enhancing the efficiency of thermophilic anaerobic digestion.

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Bai, Jing, Jiang Kang Wen, Song Tao Huang, Biao Wu, and Bo Wei Chen. "The Bioleaching Characteristics of Chalcopyrite with Different Genetic Types." Advanced Materials Research 825 (October 2013): 443–46. http://dx.doi.org/10.4028/www.scientific.net/amr.825.443.

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The copper extraction yield from thermophilic bioleaching of chalcopyrite depends on temperature, pH, and the oxidation-reduction potential (ORP), the activity of the thermophile used, as well as on the different genetic type of the chalcopyrite used. The bioleaching characteristics of chalcopyrite from marine volcanic type and porphyry type, and the influence of genetic type on microbial community were studied. The results indicated that the bioleaching of chalcopyrite is controlled by the ORP rather than by the pH. The thermophiles composition of marine volcanic type bioleaching wasMetallosphaeracuprinaandSulfobus spHB59.Metallosphaeracuprinawas the dominate bacteria during porphyry chalcopyrite bioleaching. The different leachability between marine volcanic type and porphyry type is attributed to their nature which caused by genetic type.

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Adhikari, Hriush, Sangam Ghimire, Binod Khatri, and Yuvraj K.C. "Enzymatic Screening and Molecular Characterization of Thermophilic Bacterial Strains Isolated from Hotspring of Tatopani, Bhurung, Nepal." International Journal of Applied Sciences and Biotechnology 3, no. 3 (September 25, 2015): 392–97. http://dx.doi.org/10.3126/ijasbt.v3i3.12724.

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Background and Aim: In Nepal not much of study of Thermophilic area and Thermophiles have been done. Thermophilic bacteria are less studied but are important group of microorganisms due to their ability to produce industrially important enzymes. Methods: In this study, thermophilic bacteria were isolated from hot spring of Bhurung, Nepal. Wide range of bacteria that could grow at high temperatures and tolerate extreme temperature were characterized by morphology, biochemistry and sequencing of its 16S rRNA gene sequence. The isolates were screened for production of extracellular enzymes like protease, amylase, lipase, cellulase, caseinase, pectinase and xylanase activity. Phylogenetic tree construction and G+C content evaluation of the isolate was also studied.Results: 15 isolates with ability to tolerate high temperatures were identified as Bacillus sp. by morphology, biochemistry and sequencing of its 16S rRNA gene sequence. BLAST search analysis of the sequence was performed and result showed maximum identity (99% similarity) with Bacillus licheniformis, Bacillus subtilis and Bacillus pumilus. Isolated strains exhibited considerable amount of extracellular exozymes activity. Phylogenetic analysis of the isolates revealed the relatedness among the species. The G+C content of each species was also evaluated and was found to be in range of 54.87 to 55.54%.Conclusion: The study of isolates confirmed that the isolated Bacillus sp. to be a true thermophile and could be a source of various thermostable exozymes which can be exploited for pharmaceutical and industrials applications. Much detailed study of the isolates can Int J Appl Sci Biotechnol, Vol 3(3): 392-397

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COGAN, TIMOTHY M., MANUELA BARBOSA, ERIC BEUVIER, BRUNA BIANCHI-SALVADORI, PIER S. COCCONCELLI, ISABEL FERNANDES, JESUS GOMEZ, et al. "Characterization of the lactic acid bacteria in artisanal dairy products." Journal of Dairy Research 64, no. 3 (August 1997): 409–21. http://dx.doi.org/10.1017/s0022029997002185.

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In all, 4379 isolates from 35 products, including 24 artisanal cheeses, were surveyed with a view to identifying strains that could be used as starters in commercial dairy fermentations. Of the isolates, 38% were classified as Lactococcus, 17% as Enterococcus, 14% as Streptococcus thermophilus, 12% as mesophilic Lactobacillus, 10% as Leuconostoc and 9% as thermophilic Lactobacillus. Acid production by the isolates varied considerably. Of the 1582 isolates of Lactococcus and 482 isolates of mesophilic Lactobacillus tested, only 8 and 2% respectively produced sufficient acid to lower the pH of milk to <5·3 in 6 h at 30°C. In contrast, 53, 32 and 13% of Str. thermophilus, thermophilic Lactobacillus and Enterococcus isolates respectively reduced the pH to 5·3. These isolates were found only in some French, Italian and Greek cheeses. Bacteriocins were produced by 11% of the 2257 isolates tested and 26 of them produced broad-spectrum bacteriocins which inhibited at least eight of the ten target strains used, which included lactic acid bacteria, clostridia and Listeria innocua. The most proteolytic of the 2469 isolates tested were Str. thermophilus from Fontina cheese followed by Enterococcus from Fiore Sardo and Toma cheese and thermophilic Lactobacillus from all sources. Exopolysaccharides were produced by 5·3% of the 2224 isolates tested.

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Jasilionis, Andrius, Algirdas Kaupinis, Marija Ger, Mindaugas Valius, Donaldas Chitavichius, and Nomeda Kuisiene. "Gene expression and activity analysis of the first thermophilic U32 peptidase." Open Life Sciences 7, no. 4 (August 1, 2012): 587–95. http://dx.doi.org/10.2478/s11535-012-0047-y.

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AbstractPeptidase family U32 is one of the few whose catalytic type and structure has not yet been described. It is generally accepted that U32 peptidases represent putative collagenases and contribute to the pathogenicity of some bacteria. Meanwhile, U32 peptidases are also found in nonpathogenic bacteria including thermophiles and hyperthermophiles. Here we report cloning of the U32.002 peptidase gene from thermophilic Geobacillus thermoleovorans DSM 15325 and demonstrate expression and characterization of the recombinant protein. It has been determined that U32.002 peptidase is constitutively expressed in the cells of thermophilic G. thermoleovorans DSM 15325. The recombinant oligomeric enzyme showed its activity only against heat-treated collagen. It was unable to degrade albumin, casein, elastin, gelatine and keratin. In contrast to this, the monomeric recombinant protein showed no activity at all. This paper is the first report about the thermophilic U32 peptidase. As the thermophilic bacteria are non-pathogenic, the role of constitutively expressed extracellular collagenolytic U32 peptidase in these bacteria is unclear.

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Paleskava, Alena, Elena M. Maksimova, Daria S. Vinogradova, Pavel S. Kasatsky, Stanislav V. Kirillov, and Andrey L. Konevega. "Differential Contribution of Protein Factors and 70S Ribosome to Elongation." International Journal of Molecular Sciences 22, no. 17 (September 5, 2021): 9614. http://dx.doi.org/10.3390/ijms22179614.

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The growth of the polypeptide chain occurs due to the fast and coordinated work of the ribosome and protein elongation factors, EF-Tu and EF-G. However, the exact contribution of each of these components in the overall balance of translation kinetics remains not fully understood. We created an in vitro translation system Escherichia coli replacing either elongation factor with heterologous thermophilic protein from Thermus thermophilus. The rates of the A-site binding and decoding reactions decreased an order of magnitude in the presence of thermophilic EF-Tu, indicating that the kinetics of aminoacyl-tRNA delivery depends on the properties of the elongation factor. On the contrary, thermophilic EF-G demonstrated the same translocation kinetics as a mesophilic protein. Effects of translocation inhibitors (spectinomycin, hygromycin B, viomycin and streptomycin) were also similar for both proteins. Thus, the process of translocation largely relies on the interaction of tRNAs and the ribosome and can be efficiently catalysed by thermophilic EF-G even at suboptimal temperatures.

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Kobayashi, T., Y. Y. Li, and H. Harada. "Analysis of microbial community structure and diversity in the thermophilic anaerobic digestion of waste activated sludge." Water Science and Technology 57, no. 8 (April 1, 2008): 1199–205. http://dx.doi.org/10.2166/wst.2008.079.

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The microbial community structures in the thermophilic anaerobic digestion (TAD) of waste activated sludge (WAS) and WAS were analyzed with molecular biological techniques including real-time polymerase chain reaction (PCR) and cloning. The microbial community of TAD had less diversity than that of WAS, and the sequences obtained in WAS were not present in TAD by the cloning analysis. In the TAD bacterial clone library, 97.5% of total clones were affiliated with the phylum Firmicutes and 73.1% with the genus Coprothermobacter. Real-time PCR and cloning analysis revealed that the number of Methanosarcina thermophila, which is an acetoclastic methanogen, is larger than that of Methanoculleus thermophilus, which is a hydrogenotrophic methanogen, in terms of the numbers of copies of 16S ribosomal DNA (rDNA).

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Kim and Lee. "Effects of a Groundwater Heat Pump on Thermophilic Bacteria Activity." Water 11, no. 10 (October 6, 2019): 2084. http://dx.doi.org/10.3390/w11102084.

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Groundwater samples were collected from the tubular wells of a groundwater heat pump (GWHP), and the psychrophilic, mesophilic, and thermophilic bacteria inhabiting the collected groundwater were cultured and isolated. Using the isolated bacteria, we analyzed temperature-dependent changes in autochthonous bacteria based on the operation of the GWHP. Microbial culture identified eight species of bacteria: five species of thermophilic bacteria (Anoxybacillus tepidamans, Bacillus oceanisediminis, Deinococcus geothermalis, Effusibacillus pohliae, and Vulcaniibacterium thermophilum), one species of mesophilic bacteria (Lysobacter mobilis), and two species of psychrophilic bacteria (Paenibacillus elgii and Paenibacillus lautus). The results indicated A. tepidamans as the most dominant thermophilic bacterium in the study area. Notably, the Anoxybacillus genus was previous reported as a microorganism capable of creating deposits that clog above-ground wells and filters at geothermal power plants. Additionally, we found that on-site operation of the GWHP had a greater influence on the activity of thermophilic bacteria than on psychrophilic bacteria among autochthonous bacteria. These findings suggested that study of cultures of thermophilic bacteria might contribute to understanding the bio-clogging phenomena mediated by A. tepidamans in regard to GWHP-related thermal efficiency.

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Tang, Jie, Dan Yao, Huizhen Zhou, Mingcheng Wang, and Maurycy Daroch. "Distinct Molecular Patterns of Two-Component Signal Transduction Systems in Thermophilic Cyanobacteria as Revealed by Genomic Identification." Biology 12, no. 2 (February 8, 2023): 271. http://dx.doi.org/10.3390/biology12020271.

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Two-component systems (TCSs) play crucial roles in sensing and responding to environmental signals, facilitating the acclimation of cyanobacteria to hostile niches. To date, there is limited information on the TCSs of thermophilic cyanobacteria. Here, genome-based approaches were used to gain insights into the structure and architecture of the TCS in 17 well-described thermophilic cyanobacteria, namely strains from the genus Leptodesmis, Leptolyngbya, Leptothermofonsia, Thermoleptolyngbya, Thermostichus, and Thermosynechococcus. The results revealed a fascinating complexity and diversity of the TCSs. A distinct composition of TCS genes existed among these thermophilic cyanobacteria. A majority of TCS genes were classified as orphan, followed by the paired and complex cluster. A high proportion of histidine kinases (HKs) were predicted to be cytosolic subcellular localizations. Further analyses suggested diversified domain architectures of HK and response regulators (RRs), putatively in association with various functions. Comparative and evolutionary genomic analyses indicated that the horizontal gene transfer, as well as duplications events, might be involved in the evolutionary history of TCS genes in Thermostichus and Thermosynechococcus strains. A comparative analysis between thermophilic and mesophilic cyanobacteria indicated that one HK cluster and one RR cluster were uniquely shared by all the thermophilic cyanobacteria studied, while two HK clusters and one RR cluster were common to all the filamentous thermophilic cyanobacteria. These results suggested that these thermophile-unique clusters may be related to thermal characters and morphology. Collectively, this study shed light on the TCSs of thermophilic cyanobacteria, which may confer the necessary regulatory flexibility; these findings highlight that the genomes of thermophilic cyanobacteria have a broad potential for acclimations to environmental fluctuations.

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Viegas, Matilde, Maria João Ramos, and Pedro Alexandrino Fernandes. "Thermophilic Enzymes." U.Porto Journal of Engineering 7, no. 3 (April 30, 2021): 13–23. http://dx.doi.org/10.24840/2183-6493_007.003_0002.

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Substantial improvements in the industrial production of goods led to a widespread feeling of unlimited access to food, commodities, and energy. As greener alternatives for industrial processes are in demand, scientists have turned to enzymes, looking for apt biocatalysts. Focusing on extremophiles, this mini review draws a comparison between thermophiles and their mesophilic counterparts, exploring what features are instrumental to their thermostability. A higher number of ion-pairs, hydrophobicity of buried side chains, compact tertiary structure cores, and a complex network of hydrogen bonds are the four main characteristics responsible for the robustness of thermophilic enzymes.

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Arifoǧlu, Nazan, and Zümrüt B. Ögel. "Avicel-adsorbable endoglucanase production by the thermophilic fungus Scytalidium thermophilum type culture Torula thermophila." Enzyme and Microbial Technology 27, no. 8 (November 2000): 560–69. http://dx.doi.org/10.1016/s0141-0229(00)00241-6.

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Vilcáez, Javier, Koichi Suto, and Chihiro Inoue. "Studies on Thermophilic Bioleaching of Chalcopyrite toward Heap Application." Advanced Materials Research 71-73 (May 2009): 357–60. http://dx.doi.org/10.4028/www.scientific.net/amr.71-73.357.

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In a series of studies, various aspects of thermophilic bioleaching of chalcopyrite minerals and concentrates have been analyzed. Although the main objective was the elucidation of the catalytic effect of thermophiles in leaching chalcopyrite, various other new findings contributed to a better understanding of interactions among chemical, physicochemical and biological factors, which influence the bioleaching of chalcopyrite with thermophiles. Additionally, in order to bridge laboratory results and field applications, novel mathematical models as well as an alternative method to efficiently leach chalcopyrite without thermophiles are the contributions of this research.

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Arai, Hiroyuki, Haruna Kanbe, Masaharu Ishii, and Yasuo Igarashi. "Complete Genome Sequence of the Thermophilic, Obligately Chemolithoautotrophic Hydrogen-Oxidizing Bacterium Hydrogenobacter thermophilus TK-6." Journal of Bacteriology 192, no. 10 (March 26, 2010): 2651–52. http://dx.doi.org/10.1128/jb.00158-10.

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ABSTRACT Hydrogenobacter thermophilus is a thermophilic, obligately chemolithoautotrophic and aerobic hydrogen-oxidizing bacterium. It is unique in its ability to fix carbon dioxide via the reductive tricarboxylic acid cycle under aerobic conditions. It utilizes molecular hydrogen, elemental sulfur, or thiosulfate as the sole energy source. Here, we report the complete genome sequence of H. thermophilus TK-6.

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Kovács, R., P. Miháltz, and Zs Csikor. "Kinetics of autothermal thermophilic aerobic digestion – application and extension of Activated Sludge Model No 1 at thermophilic temperatures." Water Science and Technology 56, no. 9 (November 1, 2007): 137–45. http://dx.doi.org/10.2166/wst.2007.706.

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The application of an ASM1-based mathematical model for the modeling of autothermal thermophilic aerobic digestion is demonstrated. Based on former experimental results the original ASM1 was extended by the activation of facultative thermophiles from the feed sludge and a new component, the thermophilic biomass was introduced. The resulting model was calibrated in the temperature range of 20–60 °C. The temperature dependence of the growth and decay rates in the model is given in terms of the slightly modified Arrhenius and Topiwala-Sinclair equations. The capabilities of the calibrated model in realistic ATAD scenarios are demonstrated with a focus on autothermal properties of ATAD systems at different conditions.

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Wilson, Caitlin K., and Gary M. King. "Short-Term Exposure to Thermophilic Temperatures Facilitates CO Uptake by Thermophiles Maintained under Predominantly Mesophilic Conditions." Microorganisms 10, no. 3 (March 18, 2022): 656. http://dx.doi.org/10.3390/microorganisms10030656.

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Three phylogenetically and phenotypically distinct CO-oxidizing thermophiles (Alicyclobacillus macrosporangiidus CPP55 (Firmicutes), Meiothermus ruber PS4 (Deinococcus-Thermus) and Thermogemmatispora carboxidovorans PM5T (Chloroflexi)) and one CO-oxidizing mesophile (Paraburkholderia paradisi WAT (Betaproteobacteria)) isolated from volcanic soils were used to assess growth responses and CO uptake rates during incubations with constant temperatures (25 °C and 55 °C) and during multi-day incubations with a temperature regime that cycled between 20 °C and 55 °C on a diurnal basis (alternating mesophilic and thermophilic temperatures, AMTT). The results were used to test a conjecture that some thermophiles can survive in mesothermal habitats that experience occasional thermophilic temperatures. Meiothermus ruber PS4, which does not form spores, was able to grow and oxidize CO under all conditions, while the spore-forming Alicyclobacillus macrosporangiidus CPP55 grew and oxidized CO during the AMTT regime and at 55 °C, but was not active at 25 °C. Thermogemmatispora carboxidovorans PM5T, also a spore former, only grew at 55 °C but oxidized CO during AMTT and 55 °C incubations. In contrast, the non-sporing mesophile, Paraburkholderia paradisi WAT, was only able to grow and oxidize CO at 25 °C; growth and CO uptake ceased during the AMTT incubations after exposure to the initial round of thermophilic temperatures. Collectively, these results suggest that temporary, periodic exposure to permissive growth temperatures could help maintain populations of thermophiles in mesothermal habitats after deposition from the atmosphere or other sources.

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Kumar, Vijay, Nikhil Sharma, and Tek Chand Bhalla. "In Silico Analysis of β-Galactosidases Primary and Secondary Structure in relation to Temperature Adaptation." Journal of Amino Acids 2014 (March 24, 2014): 1–9. http://dx.doi.org/10.1155/2014/475839.

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β-D-Galactosidases (EC 3.2.1.23) hydrolyze the terminal nonreducing β-D-galactose residues in β-D-galactosides and are ubiquitously present in all life forms including extremophiles. Eighteen microbial β-galactosidase protein sequences, six each from psychrophilic, mesophilic, and thermophilic microbes, were analyzed. Primary structure reveals alanine, glycine, serine, and arginine to be higher in psychrophilic β-galactosidases whereas valine, glutamine, glutamic acid, phenylalanine, threonine, and tyrosine are found to be statistically preferred by thermophilic β-galactosidases. Cold active β-galactosidase has a strong preference towards tiny and small amino acids, whereas high temperature inhabitants had higher content of basic and aromatic amino acids. Thermophilic β-galactosidases have higher percentage of α-helix region responsible for temperature tolerance while cold loving β-galactosidases had higher percentage of sheet and coil region. Secondary structure analysis revealed that charged and aromatic amino acids were significant for sheet region of thermophiles. Alanine was found to be significant and high in the helix region of psychrophiles and valine counters in thermophilic β-galactosidase. Coil region of cold active β-galactosidase has higher content of tiny amino acids which explains their high catalytic efficiency over their counterparts from thermal habitat. The present study has revealed the preference or prevalence of certain amino acids in primary and secondary structure of psychrophilic, mesophilic, and thermophilic β-galactosidase.

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32

Fedorov, Roman, Natalia Nevskaya, Alphia Khairullina, Svetlana Tishchenko, Albert Mikhailov, Maria Garber, and Stanislav Nikonov. "Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 Å resolution: conformational flexibility of the molecule." Acta Crystallographica Section D Biological Crystallography 55, no. 11 (November 1, 1999): 1827–33. http://dx.doi.org/10.1107/s0907444999010227.

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The crystal structure of ribosomal protein L30 from the extreme thermophilic bacterium Thermus thermophilus has been determined at 1.9 Å resolution. The crystals are trigonal and belong to space group P3221, with unit-cell parameters a = b = 63.5, c = 77.8 Å, α = β = 90, γ = 120° and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with X-PLOR to an R value of 20.3% and an R free of 25.3% in the resolution range 8–1.9 Å. Detailed analyses of the structures of the two molecules in the asymmetric unit and comparison of T. thermophilus L30 structure with the structure of homologous L30 from Bacillus stearothermophilus reveal two flexible regions at opposite ends of the rather elongated molecule. Such flexibility could be important for the protein fitting in the ribosome. A comparison with B. stearothermophilus L30 shows a higher number of salt bridges and unbound positively charged residues and an increased accessible hydrophobic area on the surface of T. thermophilus L30. This could contribute to the stability of both the extreme thermophile protein and the ribosome as a whole.

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Taguchi, H., J. Konishi, N. Ishii, and M. Yoshida. "A chaperonin from a thermophilic bacterium, Thermus thermophilus, that controls refoldings of several thermophilic enzymes." Journal of Biological Chemistry 266, no. 33 (November 1991): 22411–18. http://dx.doi.org/10.1016/s0021-9258(18)54588-9.

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Lee, Sang-Jae, Yong-Jik Lee, Naeun Ryu, Seulki Park, Haeyoung Jeong, Sang Jun Lee, Byoung-Chan Kim, Dong-Woo Lee, and Han-Seung Lee. "Draft Genome Sequence of the Thermophilic Bacterium Anoxybacillus kamchatkensis G10." Journal of Bacteriology 194, no. 23 (November 9, 2012): 6684–85. http://dx.doi.org/10.1128/jb.01877-12.

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ABSTRACTAnoxybacillus kamchatkensisG10 is a spore-forming thermophilic bacterium isolated from a hot spring in Indonesia. Here, we report the draft genome sequence ofA. kamchatkensisG10 that may reveal insights into aerobic/anaerobic metabolisms and carbon utilization in moderate thermophiles.

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Gladden, John M., Martin Allgaier, Christopher S. Miller, Terry C. Hazen, Jean S. VanderGheynst, Philip Hugenholtz, Blake A. Simmons, and Steven W. Singer. "Glycoside Hydrolase Activities of Thermophilic Bacterial Consortia Adapted to Switchgrass." Applied and Environmental Microbiology 77, no. 16 (July 1, 2011): 5804–12. http://dx.doi.org/10.1128/aem.00032-11.

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ABSTRACTIndustrial-scale biofuel production requires robust enzymatic cocktails to produce fermentable sugars from lignocellulosic biomass. Thermophilic bacterial consortia are a potential source of cellulases and hemicellulases adapted to harsher reaction conditions than commercial fungal enzymes. Compost-derived microbial consortia were adapted to switchgrass at 60°C to develop thermophilic biomass-degrading consortia for detailed studies. Microbial community analysis using small-subunit rRNA gene amplicon pyrosequencing and short-read metagenomic sequencing demonstrated that thermophilic adaptation to switchgrass resulted in low-diversity bacterial consortia with a high abundance of bacteria related to thermophilic paenibacilli,Rhodothermus marinus, andThermus thermophilus. At lower abundance, thermophilicChloroflexiand an uncultivated lineage of theGemmatimonadetesphylum were observed. Supernatants isolated from these consortia had high levels of xylanase and endoglucanase activities. Compared to commercial enzyme preparations, the endoglucanase enzymes had a higher thermotolerance and were more stable in the presence of 1-ethyl-3-methylimidazolium acetate ([C2mim][OAc]), an ionic liquid used for biomass pretreatment. The supernatants were used to saccharify [C2mim][OAc]-pretreated switchgrass at elevated temperatures (up to 80°C), demonstrating that these consortia are an excellent source of enzymes for the development of enzymatic cocktails tailored to more extreme reaction conditions.

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Petkova, Mariana, and Stefan Shilev. "Revealing Fungal Diversity in Mesophilic and Thermophilic Habitats of Sewage Sludge Composting by Next-Generation Sequencing." Applied Sciences 13, no. 9 (April 29, 2023): 5546. http://dx.doi.org/10.3390/app13095546.

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The accumulation of sewage sludge is a severe problem in many countries. Its utilization through composting has the potential to become a widely applied technology. From this perspective, our study investigated the diversity of fungi in mesophilic and thermophilic habitats when composting biosolids, cow manure, and wheat straw. It was conducted using a metagenomic approach and next-generation Illumina HiSeq2000 sequencing to reveal the fungal diversity. We found significantly enhanced microbial activity in the thermophilic phase. In contrast, the activity of enzyme β-glucosidase was 29% higher in the mesophilic zone. The range of α-diversity values were more pronounced in the mesophilic habitats than in the thermophilic ones. At the class level, the mesophilic fungi were represented by Sordariomycetes—58.7%, Pezizomycetes—15.1%, and Agaricomycetes—12.3%, while the most abundant thermophilic fungi found were Sordariomycetes—39.5%, and Pezizomycetes—9.8%. In the further clarification of genera diversity, it is striking that, at 37.2 °C, Psathyrella was the most abundant, with 35.91%, followed by Chaetomidium, with 20.11%. Among the thermophiles, Thielavia and Mortierella were the most common. Further research on microbial diversity changes over time is needed to manage the metabolic processes in obtaining quality soil amendment.

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Maheshwari, Ramesh, Girish Bharadwaj, and Mahalingeshwara K. Bhat. "Thermophilic Fungi: Their Physiology and Enzymes." Microbiology and Molecular Biology Reviews 64, no. 3 (September 1, 2000): 461–88. http://dx.doi.org/10.1128/mmbr.64.3.461-488.2000.

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SUMMARY Thermophilic fungi are a small assemblage in mycota that have a minimum temperature of growth at or above 20°C and a maximum temperature of growth extending up to 60 to 62°C. As the only representatives of eukaryotic organisms that can grow at temperatures above 45°C, the thermophilic fungi are valuable experimental systems for investigations of mechanisms that allow growth at moderately high temperature yet limit their growth beyond 60 to 62°C. Although widespread in terrestrial habitats, they have remained underexplored compared to thermophilic species of eubacteria and archaea. However, thermophilic fungi are potential sources of enzymes with scientific and commercial interests. This review, for the first time, compiles information on the physiology and enzymes of thermophilic fungi. Thermophilic fungi can be grown in minimal media with metabolic rates and growth yields comparable to those of mesophilic fungi. Studies of their growth kinetics, respiration, mixed-substrate utilization, nutrient uptake, and protein breakdown rate have provided some basic information not only on thermophilic fungi but also on filamentous fungi in general. Some species have the ability to grow at ambient temperatures if cultures are initiated with germinated spores or mycelial inoculum or if a nutritionally rich medium is used. Thermophilic fungi have a powerful ability to degrade polysaccharide constituents of biomass. The properties of their enzymes show differences not only among species but also among strains of the same species. Their extracellular enzymes display temperature optima for activity that are close to or above the optimum temperature for the growth of organism and, in general, are more heat stable than those of the mesophilic fungi. Some extracellular enzymes from thermophilic fungi are being produced commercially, and a few others have commercial prospects. Genes of thermophilic fungi encoding lipase, protease, xylanase, and cellulase have been cloned and overexpressed in heterologous fungi, and pure crystalline proteins have been obtained for elucidation of the mechanisms of their intrinsic thermostability and catalysis. By contrast, the thermal stability of the few intracellular enzymes that have been purified is comparable to or, in some cases, lower than that of enzymes from the mesophilic fungi. Although rigorous data are lacking, it appears that eukaryotic thermophily involves several mechanisms of stabilization of enzymes or optimization of their activity, with different mechanisms operating for different enzymes.

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Dorawa, Sebastian, Magdalena Plotka, Anna-Karina Kaczorowska, Olafur H. Fridjonsson, Gudmundur O. Hreggvidsson, Arnthor Aevarsson, and Tadeusz Kaczorowski. "Characterization of DNA Polymerase from Thermus thermophilus MAT72 Phage Tt72." Proceedings 50, no. 1 (June 11, 2020): 38. http://dx.doi.org/10.3390/proceedings2020050038.

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Thermophilic phages are recognized as an untapped source of thermostable enzymes relevant in biotechnology; however, their biology is poorly explored. This has led us to start a project aimed at investigating thermophilic phages isolated from geothermal areas of Iceland. In this study, we present a structural and functional analysis of the DNA polymerase of phage Tt72, which infects thermophilic bacterium Thermus thermophilus MAT72. An in silico analysis of the Tt72 phage genome revealed the presence of a 2112-bp open reading frame (ORF) encoding protein homologous to the members of the A family of DNA polymerases. It contains a conserved nucleotidyltransferase domain and a 3′ → 5′ exonuclease domain but lacks the 5′ → 3′ exonuclease domain. The amino acid sequence of Tt72 DNA polymerase shows high similarity to two as yet uncharacterized DNA polymerases of T. thermophilus phages: ΦYS40 (91%) and ΦTMA (90%). The gene coding for Tt72 DNA polymerase was cloned and overexpressed in E. coli. The Tt72 polA gene is composed of 2112 nucleotides. The overall G+C content of this gene is 31.58%, which is lower than the G+C content of T. thermophilus genomic DNA (69.49%). The Tt72 polA gene codes for a 703-aa protein with a predicted molecular weight of 80,477. The enzyme was overproduced in E. coli, purified by heat treatment, followed by HiTrap TALON column and HiTrap Heparin HP column chromatography, then biochemically characterized. The optimum activity was found at 55 °C, pH 8.5, 25 mM KCl, and 0.5 mM Mg2+. Furthermore, the Tt72 DNA polymerase shows strong 3′ → 5′ exonucleolytic activity.

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Fateev, Ilja V., Ekaterina V. Sinitsina, Aiguzel U. Bikanasova, Maria A. Kostromina, Elena S. Tuzova, Larisa V. Esipova, Tatiana I. Muravyova, Alexei L. Kayushin, Irina D. Konstantinova, and Roman S. Esipov. "Thermophilic phosphoribosyltransferases Thermus thermophilus HB27 in nucleotide synthesis." Beilstein Journal of Organic Chemistry 14 (December 21, 2018): 3098–105. http://dx.doi.org/10.3762/bjoc.14.289.

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Phosphoribosyltransferases are the tools that allow the synthesis of nucleotide analogues using multi-enzymatic cascades. The recombinant adenine phosphoribosyltransferase (TthAPRT) and hypoxanthine phosphoribosyltransferase (TthHPRT) from Thermus thermophilus HB27 were expressed in E.coli strains and purified by chromatographic methods with yields of 10–13 mg per liter of culture. The activity dependence of TthAPRT and TthHPRT on different factors was investigated along with the substrate specificity towards different heterocyclic bases. The kinetic parameters for TthHPRT with natural substrates were determined. Two nucleotides were synthesized: 9-(β-D-ribofuranosyl)-2-chloroadenine 5'-monophosphate (2-Сl-AMP) using TthAPRT and 1-(β-D-ribofuranosyl)pyrazolo[3,4-d]pyrimidine-4-one 5'-monophosphate (Allop-MP) using TthНPRT.

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GIRAFFA, GIORGIO, DOMENICO CARMINATI, and GIOVANNA TORRI TARELLI. "Inhibition of Listeria innocua in Milk by Bacteriocin-Producing Enterococcus faecium 7C5." Journal of Food Protection 58, no. 6 (June 1, 1995): 621–23. http://dx.doi.org/10.4315/0362-028x-58.6.621.

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Enterococcus faecium 7C5 produces a bacteriocin active against Listeria monocytogenes and Listeria innocua. In co-cultures of the strain 7C5 with a thermophilic starter, which was composed of Streptococcus thermophilus and Lactobacillus delbrueckii subsp. bulgaricus, the acidifying activity of the latter was not affected. In contrast, the rate of bacteriocin production was lower when compared with the pure culture of strain 7C5. In co-cultures of L. innocua CNRZ LIN 11 with the thermophilic starter or with strain 7C5, a bacteriostatic effect on Listeria growth was observed. In the co-culture of L. innocua with both strain 7C5 and the thermophilic starter, a complete listerial inhibition occurred. The combined inhibitory effect of the pH decrease and bacteriocin production, which were shown to be synergistic, was demonstrated both at 37°C and under temperature conditions reproducing the first 24 h of a soft-cheese technology. This data substantially supported the potential of using bacteriocin-producing strains as a culture adjunct to inhibit Listeria during cheese manufacturing.

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Shinkai, Akeo, Naomi Ohbayashi, Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, and Shigeyuki Yokoyama. "Identification of Promoters Recognized by RNA Polymerase-σE Holoenzyme from Thermus thermophilus HB8." Journal of Bacteriology 189, no. 23 (September 28, 2007): 8758–64. http://dx.doi.org/10.1128/jb.01076-07.

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ABSTRACT Thermus thermophilus σE, an extracytoplasmic function σ factor from the extremely thermophilic bacterium Thermus thermophilus HB8, bound to the RNA polymerase core enzyme and showed transcriptional activity. With the combination of in vitro transcription assay and GeneChip technology, we identified three promoters recognized by σE. The predicted consensus promoter sequence for σE is 5′-CA(A/T)(A/C)C(A/C)-N15-CCGTA-3′.

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Hamana, Koei, Teruhiko Akiba, Fuji Uchino, and Shigeru Matsuzaki. "Distribution of spermine in bacilli and lactic acid bacteria." Canadian Journal of Microbiology 35, no. 4 (April 1, 1989): 450–55. http://dx.doi.org/10.1139/m89-069.

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Obligate moderately thermophilic bacilli and obligate moderately thermoacidophilic bacilli contained spermine as the major polyamine in addition to putrescine and spermidine. The identity of spermine was confirmed by thin-layer chromatography and high-performance liquid chromatography before and after treatment with putrescine oxidase. Using these methods, thermospermine and spermine can be separated; thermospermine was not present in these organisms. On the other hand, various facultative thermophiles and mesophilic strains of the genus Bacillus, including alkalophiles and halophiles, lack spermine and other tetraamines. No spermine was detected in several strains of mesophilic or facultative slightly thermophilic lactic acid bacteria, Lactobacillus and Streptococcus.Key words: polyamine, spermine, Bacillus, Lactobacillus, Streptococcus.

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Nguyen, Tri H. "Isolation and optimization of the growth conditions of thermophilic microorganism from hot springs." Journal of Agriculture and Development 17, no. 03 (June 28, 2018): 55–60. http://dx.doi.org/10.52997/jad.8.03.2018.

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The aim of this study was to isolate and optimize the growth conditions of thermophilic microorganism from hot springs. The isolation was conducted by using the mineral salt basal medium supplemented with 0.6% yeast extract at 50oC. Totally, 33 isolates of thermophilic microorganism were isolated from hot springs at Truong Xuan (Khanh Hoa province) and Binh Chau (Ba Ria - Vung Tau province). The effects of temperature (45 - 80oC), pH (pH 6 - 9) and carbon sources (malate, pyruvate, acetate, glucose, fructose, or carbon dioxide) on the growth of isolates were examined. In addition, the isolate morphology was also investigated by Gram and spore staining. The isolated thermophilic microorganism showed the diversity in colony morphology and color appearance. Most of them were rod shaped, spore-forming and most grew well at 50oC and pH 7. The highest growth of all isolates was observed under malate, glucose, or fructose, as an organic carbon source and unable to use carbon dioxide. Six out of 33 thermophilic microorganism isolates (namely BM7, BS5, NS1, NS3, NS4, and NW6) grew rapidly under high temperatures from 50 - 55oC and their morphology characteristics showed high similarity to Bacillus sp. The study evidenced the polymorphic diversity of thermophiles in the geothermal hot spring ecosystems.

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Džupponová, Veronika, Nataša Tomášková, Andrea Antošová, Erik Sedlák, and Gabriel Žoldák. "Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2." International Journal of Molecular Sciences 24, no. 7 (April 5, 2023): 6787. http://dx.doi.org/10.3390/ijms24076787.

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Thermophilic proteins and enzymes are attractive for use in industrial applications due to their resistance against heat and denaturants. Here, we report on a thermophilic protein that is stable at high temperatures (Ttrs, hot 67 °C) but undergoes significant unfolding at room temperature due to cold denaturation. Little is known about the cold denaturation of thermophilic proteins, although it can significantly limit their applications. We investigated the cold denaturation of thermophilic multidomain protein translation initiation factor 2 (IF2) from Thermus thermophilus. IF2 is a GTPase that binds to ribosomal subunits and initiator fMet-tRNAfMet during the initiation of protein biosynthesis. In the presence of 9 M urea, measurements in the far-UV region by circular dichroism were used to capture details about the secondary structure of full-length IF2 protein and its domains during cold and hot denaturation. Cold denaturation can be suppressed by salt, depending on the type, due to the decreased heat capacity. Thermodynamic analysis and mathematical modeling of the denaturation process showed that salts reduce the cooperativity of denaturation of the IF2 domains, which might be associated with the high frustration between domains. This characteristic of high interdomain frustration may be the key to satisfying numerous diverse contacts with ribosomal subunits, translation factors, and tRNA.

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Lyon, Pierre-François, Trello Beffa, Michel Blanc, Georg Auling, and Michel Aragno. "Isolation and characterization of highly thermophilic xylanolyticThermus thermophilusstrains from hot composts." Canadian Journal of Microbiology 46, no. 11 (November 1, 2000): 1029–35. http://dx.doi.org/10.1139/w00-075.

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This is the first detailed report of xylanolytic activity in Thermus strains. Two highly thermophilic xylanolytic bacteria, very closely related to non-xylanolytic T. thermophilus strains, have been isolated from the hottest zones of compost piles. Strain X6 was investigated in more detail. The growth rate (optical density monitoring) on xylan was 0.404·h-1at 75°C. Maximal growth temperature was 81°C. Xylanase activity was mainly cell-bound, but was solubilized into the medium by sonication. It was induced by xylan or xylose in the culture medium. The temperature and pH optima of the xylanases were determined to be around 100°C and pH 6, respectively. Xylanase activity was fairly thermostable; only 39% of activity was lost after an incubation period of 48 h at 90°C in the absence of substrate. Xylanolytic T. thermophilus strains could contribute to the degradation of hemicellulose during the thermogenic phase of industrial composting.Key words: Thermus, thermophilic aerobic bacteria, xylanase, thermostable enzyme, compost.

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46

Yamada, Takeshi, Yuji Sekiguchi, Hiroyuki Imachi, Yoichi Kamagata, Akiyoshi Ohashi, and Hideki Harada. "Diversity, Localization, and Physiological Properties of Filamentous Microbes Belonging to Chloroflexi Subphylum I in Mesophilic and Thermophilic Methanogenic Sludge Granules." Applied and Environmental Microbiology 71, no. 11 (November 2005): 7493–503. http://dx.doi.org/10.1128/aem.71.11.7493-7503.2005.

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ABSTRACT We previously reported that the thermophilic filamentous anaerobe Anaerolinea thermophila, which is the first cultured representative of subphylum I of the bacterial phylum Chloroflexi, not only was one of the predominant constituents of thermophilic sludge granules but also was a causative agent of filamentous sludge bulking in a thermophilic (55°C) upflow anaerobic sludge blanket (UASB) reactor in which high-strength organic wastewater was treated (Y. Sekiguchi, H. Takahashi, Y. Kamagata, A. Ohashi, and H. Harada, Appl. Environ. Microbiol. 67:5740-5749, 2001). To further elucidate the ecology and function of Anaerolinea-type filamentous microbes in UASB sludge granules, we surveyed the diversity, distribution, and physiological properties of Chloroflexi subphylum I microbes residing in UASB granules. Five different types of mesophilic and thermophilic UASB sludge were used to analyze the Chloroflexi subphylum I populations. 16S rRNA gene cloning-based analyses using a 16S rRNA gene-targeted Chloroflexi-specific PCR primer set revealed that all clonal sequences were affiliated with the Chloroflexi subphylum I group and that a number of different phylotypes were present in each clone library, suggesting the ubiquity and vast genetic diversity of these populations in UASB sludge granules. Subsequent fluorescence in situ hybridization (FISH) of the three different types of mesophilic sludge granules using a Chloroflexi-specific probe suggested that all probe-reactive cells had a filamentous morphology and were widely distributed within the sludge granules. The FISH observations also indicated that the Chloroflexi subphylum I bacteria were not always the predominant populations within mesophilic sludge granules, in contrast to thermophilic sludge granules. We isolated two mesophilic strains and one thermophilic strain belonging to the Chloroflexi subphylum I group. The physiological properties of these isolates suggested that these populations may contribute to the degradation of carbohydrates and other cellular components, such as amino acids, in the bioreactors.

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47

Pentecost, Allan. "British thermophilic cyanobacteria." Archiv für Hydrobiologie 132, no. 4 (March 10, 1995): 407–14. http://dx.doi.org/10.1127/archiv-hydrobiol/132/1995/407.

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Pennacchio, Angela, Biagio Pucci, Francesco Secundo, Francesco La Cara, Mosè Rossi, and Carlo A. Raia. "Purification and Characterization of a Novel Recombinant Highly Enantioselective Short-Chain NAD(H)-Dependent Alcohol Dehydrogenase from Thermus thermophilus." Applied and Environmental Microbiology 74, no. 13 (May 2, 2008): 3949–58. http://dx.doi.org/10.1128/aem.00217-08.

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ABSTRACT The gene encoding a novel alcohol dehydrogenase (ADH) that belongs to the short-chain dehydrogenase/reductase (SDR) superfamily was identified in the extremely thermophilic, halotolerant gram-negative eubacterium Thermus thermophilus HB27. The T. thermophilus ADH gene (adh Tt) was heterologously overexpressed in Escherichia coli, and the protein (ADHTt) was purified to homogeneity and characterized. ADHTt is a tetrameric enzyme consisting of identical 26,961-Da subunits composed of 256 amino acids. The enzyme has remarkable thermophilicity and thermal stability, displaying activity at temperatures up to ∼73°C and a 30-min half-inactivation temperature of ∼90°C, as well as good tolerance to common organic solvents. ADHTt has a strict requirement for NAD(H) as the coenzyme, a preference for reduction of aromatic ketones and α-keto esters, and poor activity on aromatic alcohols and aldehydes. This thermophilic enzyme catalyzes the following reactions with Prelog specificity: the reduction of acetophenone, 2,2,2-trifluoroacetophenone, α-tetralone, and α-methyl and α-ethyl benzoylformates to (S)-(−)-1-phenylethanol (>99% enantiomeric excess [ee]), (R)-α-(trifluoromethyl)benzyl alcohol (93% ee), (S)-α-tetralol (>99% ee), methyl (R)-(−)-mandelate (92% ee), and ethyl (R)-(−)-mandelate (95% ee), respectively, by way of an efficient in situ NADH-recycling system involving 2-propanol and a second thermophilic ADH. This study further supports the critical role of the D37 residue in discriminating NAD(H) from NADP(H) in members of the SDR superfamily.

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Wouters, Jeroen A., Frank M. Rombouts, Willem M. de Vos, Oscar P. Kuipers, and Tjakko Abee. "Cold Shock Proteins and Low-Temperature Response ofStreptococcus thermophilus CNRZ302." Applied and Environmental Microbiology 65, no. 10 (October 1, 1999): 4436–42. http://dx.doi.org/10.1128/aem.65.10.4436-4442.1999.

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ABSTRACT Low-temperature adaptation and cryoprotection were studied in the thermophilic lactic acid bacterium Streptococcus thermophilus CNRZ302. S. thermophilus actively adapts to freezing during a pretreatment at 20°C, resulting in an approximately 1,000-fold increased survival after four freeze-thaw cycles compared to mid-exponential-phase cells grown at an optimal temperature of 42°C. No adaptation is observed when cells are exposed to a temperature (10°C) below the minimal growth temperature of the strain (just below 15°C). By two-dimensional gel electrophoresis several 7-kDa cold-induced proteins were identified, which are the major induced proteins after a shift to 20°C. These cold shock proteins were maximally expressed at 20°C, while the induction level was low after cold shock to 10°C. To confirm the presence ofcsp genes in S. thermophilus, a PCR strategy was used which yielded products of different sizes. Sequence analysis revealed csp-like sequences that were up to 95% identical to those of csp genes of S. thermophilus ST1-1,Streptococcus dysgalactiae, Streptococcus pyogenes, and Lactococcus lactis. Northern blot analysis revealed a seven- to ninefold induction of cspmRNA after a temperature shift to 20°C, showing that this thermophilic bacterium indeed contains at least one cold-induciblecsp gene and that its regulation takes place at the transcriptional level.

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50

Takai, Ken, Hisako Hirayama, Yuri Sakihama, Fumio Inagaki, Yu Yamato, and Koki Horikoshi. "Isolation and Metabolic Characteristics of Previously Uncultured Members of the Order Aquificales in a Subsurface Gold Mine." Applied and Environmental Microbiology 68, no. 6 (June 2002): 3046–54. http://dx.doi.org/10.1128/aem.68.6.3046-3054.2002.

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ABSTRACT Culture-dependent and -independent techniques were combined to characterize the physiological properties and the ecological impacts of culture-resistant phylotypes of thermophiles within the order Aquificales from a subsurface hot aquifer of a Japanese gold mine. Thermophilic bacteria phylogenetically associated with previously uncultured phylotypes of Aquificales were successfully isolated. 16S ribosomal DNA clone analysis of the entire microbial DNA assemblage and fluorescence in situ whole-cell hybridization analysis indicated that the isolates dominated the microbial population in the subsurface aquifer. The isolates were facultatively anaerobic, hydrogen- or sulfur/thiosulfate-oxidizing, thermophilic chemolithoautotrophs utilizing molecular oxygen, nitrate, ferric iron, arsenate, selenate, and selenite as electron acceptors. Their versatile energy-generating systems may reflect the geochemical conditions of their habitat in the geothermally active subsurface gold mine.

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Journal articles on the topic 'Thermophilic'

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