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Genome Sequencing Revealed the Biotechnological Potential of an Obligate Thermophile Strain RL Isolated from Hot Water Spring

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Specialty Microbiology
Date 2019 Aug 8
PMID 31388213
Citations 5
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Abstract

In the present study, we report the draft genome sequence of an obligate thermophile strain RL isolated from Manikaran hot water spring located atop the Himalayan ranges, India. Strain RL grew optimally at 70 °C but not below 45 °C. The draft genome (3.39 Mb) obtained by Illumina sequencing contains 138 contigs with an average G + C content of 52.30%. RAST annotation showed that amino acid metabolism pathways were most dominant followed by carbohydrate metabolism. Genome-wide analysis using NCBI's Prokaryotic Genome Annotation Pipeline revealed that strain RL encodes for a cocktail of industrially important hydrolytic enzymes glycoside hydrolase, α-and β-glucosidase, xylanase, amylase, neopullulanase, pullulanase and lipases required for white biotechnology. In addition, the presence of genes encoding green biocatalyst multicopper polyphenol oxidase (laccase) and an anticancer enzyme l-glutaminase reflects the significance of strain RL in gray and red biotechnology, respectively. Strain RL is a thermophilic multi-enzyme encoding bacterium which could be the source for the recombinant production of biotechnologically significant enzymes. In, addition whole cells of strain RL may be used in bioremediation studies.

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References
1.
Vieille C, Zeikus G . Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev. 2001; 65(1):1-43. PMC: 99017. DOI: 10.1128/MMBR.65.1.1-43.2001. View

2.
Beg Q, Kapoor M, Mahajan L, Hoondal G . Microbial xylanases and their industrial applications: a review. Appl Microbiol Biotechnol. 2001; 56(3-4):326-38. DOI: 10.1007/s002530100704. View

3.
Lee H, Kim M, Cho H, Kim J, Kim T, Choi J . Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other. J Biol Chem. 2002; 277(24):21891-7. DOI: 10.1074/jbc.M201623200. View

4.
Takata H, Kuriki T, Okada S, Takesada Y, Iizuka M, Minamiura N . Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1----4)- and alpha-(1----6)-glucosidic linkages. J Biol Chem. 1992; 267(26):18447-52. View

5.
Teplitsky A, Mechaly A, Stojanoff V, Sainz G, Golan G, FEINBERG H . Structure determination of the extracellular xylanase from Geobacillus stearothermophilus by selenomethionyl MAD phasing. Acta Crystallogr D Biol Crystallogr. 2004; 60(Pt 5):836-48. DOI: 10.1107/S0907444904004123. View