Extremely thermophilic microorganisms and their polymer-hidrolytic enzymes

Andrade, Carolina M. M. C.; Pereira, Nei; Antranikian, G.

doi:10.1590/s0001-37141999000400001

Cited by 39 publications

(20 citation statements)

References 51 publications

(27 reference statements)

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“…Those from Nonomuraea flexuosa and Dictyoglomus thermophilum are among the most stable, with apparent temperature optima of 80 and 85°C, respectively. In addition to the above mentioned xylanase producing bacteria a number of xylanase producing hyperthermophilic archaea have also been recently reported: Thermococcus zilligii [143], Pyrococcus furiosus [143], Sulfolobus solfataricus [140], Pyrodictium abyssi [151,152] and a number of Thermofilum strains [153].…”

Section: Thermophilesmentioning

confidence: 99%

“…strain FjSS3-B.1 is one of the most thermostable xylanases reported to date with an apparent optimum temperature for activity of 105°C and a halflife of 90 minutes at 95°C [148]. In addition to the above mentioned xylanase producing bacteria a number of xylanase producing hyperthermophilic archaea have also been recently reported: Thermococcus zilligii [143], Pyrococcus furiosus [143], Sulfolobus solfataricus [140], Pyrodictium abyssi [151,152] and a number of Thermofilum strains [153]. [133], Dictyoglomus thermophilum [121], Chaetomium thermophilum [120], Nonomuraea flexuosa [120] and Bacillus strain D3 [128,150] being the most thoroughly investigated.…”

Section: Thermophilesmentioning

confidence: 99%

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Xylanases, xylanase families and extremophilic xylanases

2005

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Xylanases are hydrolytic enzymes which randomly cleave the beta 1,4 backbone of the complex plant cell wall polysaccharide xylan. Diverse forms of these enzymes exist, displaying varying folds, mechanisms of action, substrate specificities, hydrolytic activities (yields, rates and products) and physicochemical characteristics. Research has mainly focused on only two of the xylanase containing glycoside hydrolase families, namely families 10 and 11, yet enzymes with xylanase activity belonging to families 5, 7, 8 and 43 have also been identified and studied, albeit to a lesser extent. Driven by industrial demands for enzymes that can operate under process conditions, a number of extremophilic xylanases have been isolated, in particular those from thermophiles, alkaliphiles and acidiphiles, while little attention has been paid to cold-adapted xylanases. Here, the diverse physicochemical and functional characteristics, as well as the folds and mechanisms of action of all six xylanase containing families will be discussed. The adaptation strategies of the extremophilic xylanases isolated to date and the potential industrial applications of these enzymes will also be presented.

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Section: Thermophilesmentioning

confidence: 99%

Section: Thermophilesmentioning

confidence: 99%

Xylanases, xylanase families and extremophilic xylanases

2005

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“…Thermophilic enzymes are ideal biocatalysts for modern biotechnology because of their thermostability (38) and better yields under extreme operational conditions (4). The wide range of applications of thermophilic cellulases is being listed in Table 2.…”

Section: Physiological and Adaptive Aspects Of Thermophilic Microorgamentioning

confidence: 99%

Bioprospecting thermophiles for cellulase production: a review

Acharya

Chaudhary

2012

Braz. J. Microbiol.

105

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Most of the potential bioprospecting is currently related to the study of the extremophiles and their potential use in industrial processes. Recently microbial cellulases find applications in various industries and constitute a major group of industrial enzymes. Considerable amount of work has been done on microbial cellulases, especially with resurgence of interest in biomass ethanol production employing cellulases and use of cellulases in textile and paper industry. Most efficient method of lignocellulosic biomass hydrolysis is through enzymatic saccharification using cellulases. Significant information has also been gained about the physiology of thermophilic cellulases producers and process development for enzyme production and biomass saccharification. The review discusses the current knowledge on cellulase producing thermophilic microorganisms, their physiological adaptations and control of cellulase gene expression. It discusses the industrial applications of thermophilic cellulases, their cost of production and challenges in cellulase research especially in the area of improving process economics of enzyme production.

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“…There are a few thermophilic bacteria that are potent producers of cellulases, including Bacillus subtilis, Geobacillus pallidus, Bacillus licheniformis, Bacillus pumilis, Aneurinibacillus thermoaerophilus, and Clostridium thermocellum [10]. Thermophilic enzymes are ideal biocatalysts for the present day biotechnology because of their thermo-stability [11] and better yields under intense operational conditions [12].…”

Section: Introductionmentioning

confidence: 99%

Endoglucanase gene of M42 aminopeptidase/endoglucanase family from thermophilic Bacillus sp. PW1 and PW2 isolated from Tattapani hot spring, Himachal Pradesh, India

Sharma

Dev

et al. 2019

Journal of Genetic Engineering and Biotechnology

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BackgroundThermostable cellulases are in constant demand for several biotechnological applications. Two thermophilic bacterial strains PW1 and PW2 isolated from Tattapani hot spring were found to have cellulolytic activity. Subsequently, PW1 and PW2 were identified and mined for genes encoding cellulase activity.ResultsSequencing of the 16S rDNA of PW1 and PW2 identified them as Bacillus sp. PW1 (Acc no. KU711837) and Bacillus sp. PW2 (Acc no. KU711838), respectively, which clustered in the clades containing thermophilic members of Bacillus sp. and Geobacillus species. Phylogenetic analysis revealed that despite the morphological and sequence identities, Bacillus sp. PW1 and Bacillus sp. PW2 are different at the genetic level. The cellulase genes (~ 1.1 kb) of the two bacterial strains were amplified using primers designed against related thermophilic cellulases. Sequencing of the cellulase gene amplicons of PW1 and PW2 revealed that they encode proteins of 280 and 206 amino acid residues, respectively. Sequence and domain analysis of the protein products of PW1 and PW2 revealed that they belong to M42 family of aminopeptidase/endoglucanase. The PW2 endoglucanase coding sequence was submitted to Genbank under accession no. MH049504. The structures of putative endoglucanases of PW1 and PW2 were generated using 1VHE.A as template, which showed the presence of vast proportion of random coils. Molecular docking of the modeled endoglucanase proteins with various substrates and products of cellulases showed that carboxymethyl cellulose and maltose exhibit the highest binding affinity, while xylan and glucose the least.ConclusionsThe two thermophilic bacteria PW1 and PW2 and their endoglucanase gene can be further utilized for recombinant production of thermostable cellulases for their application in industries.Electronic supplementary materialThe online version of this article (10.1186/s43141-019-0001-8) contains supplementary material, which is available to authorized users.

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Extremely thermophilic microorganisms and their polymer-hidrolytic enzymes

Cited by 39 publications

References 51 publications

Xylanases, xylanase families and extremophilic xylanases

Xylanases, xylanase families and extremophilic xylanases

Bioprospecting thermophiles for cellulase production: a review

Endoglucanase gene of M42 aminopeptidase/endoglucanase family from thermophilic Bacillus sp. PW1 and PW2 isolated from Tattapani hot spring, Himachal Pradesh, India

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