Isolation and Characterization of Thermophilic Bacteria from Jordanian Hot Springs:<i>Bacillus licheniformis</i>and<i>Thermomonas hydrothermalis</i>Isolates as Potential Producers of Thermostable Enzymes

Mohammad, Balsam T.; Daghistani, Hala I. Al; Jaouani, Atef; Abdel-Latif, Saleh; Kennes, Christian

doi:10.1155/2017/6943952

Cited by 124 publications

(87 citation statements)

References 44 publications

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“…The ability of Bacillus spp. isolated from hot springs to produce these enzymes was established previously by Lele and Deshmukh (2016) and Mohammad et al (2017).…”

Section: Resultsmentioning

confidence: 99%

In vitro biocontrol and biofertilization features study of a Bacillus amyloliquefaciens (4RH) strain isolated from a hot spring soil in Algeria

Kaki¹,

Ali²,

Milet³

et al. 2017

Afr. J. Microbiol. Res.

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Several Bacillus strains were isolated from "Ouled Yelass" hot spring soil, located in Setif city (Eastern Algeria). Three isolates of them coded (4RH), (14 RH), and (Set-oxy), were screened for their ability to inhibit the growth of some phytopathogenic fungi, such as Fusarium oxysporium, Botrytis cinerea, Aspergillus niger, Cladosporium cucumerinium and Alternaria alternata. The molecular identification of the strain (4RH) based on the 16S-DNA and gyrase-A genes sequences analysis, showed that it is closely related (99.9%) to the Bacillus amyloliquefaciens species. This bacterium was characterized by a high sporulation yield reaching 22±0.86 × 10 8 spores/ml and had important inhibition rates up to 80 and 70%, against F. oxysporium and B. cinerea, respectively. The bacterium (4RH) was able to produce cell wall degrading enzymes of cellulase and protease, in contrast to chitinase activity which was negative. Furthermore, it produced the three lipopeptides families, which are, iturins A (C14; C15), fengycin A (C14, C15, C16, C17, and C18), and surfactin (C12, C13, C14, C15, C16). Interestingly, LC-MS profiles of 80% acetonitrile fengycin extract of the (4RH) strain, showed the presence of some new molecular ions (MH+) with masses different, but near to conventional fengycin variants, which correspond to new variants described for the first time in this work. The isolate (4RH) produced 5 µg/ml of the phytohormone (IAA), on TGE medium and sidérophores with more than 10 mm of yellow-orange zones, on CAS medium. To conclude, B. amyloliquefaciens (4RH) strain possessed interesting biocontrol and biofertilization characteristics, in vitro, in addition to its high sporulation yield, which make it a potential agent for future biopesticide that could be efficient in the integrate pest management and organic agricultural production systems.

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“…The ability of Bacillus spp. isolated from hot springs to produce these enzymes was established previously by Lele and Deshmukh (2016) and Mohammad et al (2017).…”

Section: Resultsmentioning

confidence: 99%

In vitro biocontrol and biofertilization features study of a Bacillus amyloliquefaciens (4RH) strain isolated from a hot spring soil in Algeria

Kaki¹,

Ali²,

Milet³

et al. 2017

Afr. J. Microbiol. Res.

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“…Our results also corroborated well with Cordova et al, (2003) who suggested that the optimal temperature was 5-35°C for the growth of mesophiles, at or above 50°C for growth of thermophiles whereas microorganisms with maximum temperature near 50°C were classified as thermotolerant. According to Mohammad et al, (2017) thermophilic microorganisms require a maximum temperature for growth at or above 50°C and a minimum temperature for growth at or above 20°C. Ahmed et al, (2012) also reported that the optimal temperature of thermophilic/thermotolerant fungi is 40-50 o C. Similarly, the majority of mesophiles grew between 5°C and 37°C, with an optimum temperature of 25-30°C (Dix & Webster, 1995).…”

Section: Discussionmentioning

confidence: 99%

A comparative study of cow dung compost, goat pellets, poultry waste manure and plant debris for thermophilic, thermotolerant and mesophilic microflora with some new reports from Pakistan

Noreen¹,

Ramzan²,

Parveen³

et al. 2019

PAK.J.BOT.

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Isolations from the cow dung, goat pellets, poultry waste manure and plant debris samples yielded 44 fungal and 15 bacterial species. The isolated fungi included 13 mesophilic, 11 thermotolerant and 20 thermophilic species. Similarly, six mesophilic, five thermotolerant, and four thermophilic bacteria were isolated. Of these, three species of fungi viz., Annelophora africana, Conidiobolus thermophilus and Haplotrichum croceum appeared to be new records from Pakistan, not hitherto reported. The highest percentage of thermophilic fungi and bacteria occurred in cow dung followed by goat pellet, poultry waste and plant debris in descending order. Similarly, highest percentage of thermotolerant fungi and bacteria occurred in goat pellet followed by poultry waste, cow dung and plant debris, respectively. The highest percentage of mesophilic fungi and bacteria occurred in plant debris followed by poultry waste, goat pellet and cow dung. The growth of thermophilic fungi was better on yeast starch agar (YSA) as compared to potato sucrose agar (PSA) medium. However, the thermotolerant fungi showed better growth on PSA medium. Among the mesophilic fungi, Aspergillus flavus, Penicillium dipodomyis, Stachybotrys chartarum and Syncephalastrum racemosum showed better growth on YSA medium, whereas, PSA was more suitable for the remaining mesophilic fungi. The optimal temperature for growth of the mesophilic microorganisms was 28°C whereas thermotolerant and thermophilic microorganisms grew best at 40 and 50°C, respectively.

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“…The enzymatic activity of proteins from hyperthermophilic microorganisms thriving in extreme conditions has been an active area of research for several decades 1,2 . These microbes have an optimal temperature range for their growth and survival of about 80°C -100°C 3 . In addition to extreme temperatures, these microorganisms can also withstand high hydrostatic pressures the one hand, flexibility is required by a protein to function.…”

Section: Introductionmentioning

confidence: 99%

Mesophilic enzyme function at high temperature: molecular dynamics of hyperthermophilic and mesophilic pyrophosphatases

Agarwal

Shrestha

Chu

et al. 2020

Preprint

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The mesophilic inorganic pyrophosphatase from Escherichia coli (EcPPase) retains function at 353 K, the physiological temperature of hyperthermophilic Thermoccoccus thioreducens, whereas, the homolog protein from the hyperthermophilic organism (TtPPase) cannot function at room temperature. To explain this asymmetric behavior, we examined structural and dynamical properties of the two proteins using molecular dynamics simulations. The global flexibility of TtPPase is significantly higher than its mesophilic homolog at all tested temperature/pressure conditions. However, at 353 K, EcPPase reduces its solvent-exposed surface area and increases subunit compaction while maintaining flexibility in its catalytic pocket. In contrast, TtPPase lacks this adaptability and has increased rigidity and reduced protein:water interactions in its catalytic pocket at room temperature, providing a plausible explanation for its inactivity near room temperature.ranging from 60 to 100 MPa (the atmospheric pressure at sea-level is 0.1 MPa) 1,4 . Since most mesophilic proteins denature under such high temperatures 5 and pressures 6 , it is intriguing to examine how proteins from hyperthermophilic organisms retain activity. Previous studies have suggested structural characteristics 7-9 of proteins that enable these extremophilic microbes to thrive in severe conditions. However, there appears to be no universal adaptive mechanism, but rather a complex combination of different factors, which frequently differs according to the protein or protein family and is thus difficult to generalize 8,10 . Furthermore, the role of dynamic characteristics such as conformational stability 11 12 and flexibility 13 , for protein adaptability is still not well understood 1,14 .Recent studies have reported that the conformational sub-states of a protein are significantly perturbed by changes in temperature and pressure 13,[15][16][17][18][19] . Temperature enhances the internal fluctuations of a protein 20 , and an optimum temperature may provide an appropriate balance of flexibility and rigidity required for function 13,21,22 . Temperatures higher than the optimum can lead to loss of function through unfolding or denaturation 23 . However in the case of hyperthermophilic proteins, high native-state flexibility can reduce their entropy of unfolding, thus increasing their melting temperature 24 . Similarly, high pressure conditions can cause a protein to become inactive by the collapse of its intra-protein cavities, giving rise to an unfolded state 25 .Pressure drives the reduction in the volume of a protein, which results in a negative entropy change of the system, which may destabilize the native state 26 . Nonetheless, there are exceptions, and the stability and/or activity of some proteins, such as a thermolysin 27 and a hydrogenase from Methanococcus jannaschii 28 , have been shown to increase with pressure.Overall, a dualistic picture of protein flexibility 24,29 and rigidity 30,31 has been recognized as a possible factor behind thermostability of ther...

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Isolation and Characterization of Thermophilic Bacteria from Jordanian Hot Springs:Bacillus licheniformisandThermomonas hydrothermalisIsolates as Potential Producers of Thermostable Enzymes

Cited by 124 publications

References 44 publications

In vitro biocontrol and biofertilization features study of a Bacillus amyloliquefaciens (4RH) strain isolated from a hot spring soil in Algeria

In vitro biocontrol and biofertilization features study of a Bacillus amyloliquefaciens (4RH) strain isolated from a hot spring soil in Algeria

A comparative study of cow dung compost, goat pellets, poultry waste manure and plant debris for thermophilic, thermotolerant and mesophilic microflora with some new reports from Pakistan

Mesophilic enzyme function at high temperature: molecular dynamics of hyperthermophilic and mesophilic pyrophosphatases

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