Characterization of novel metagenomic–derived lipase from Indian hot spring

Extreme environments are the main source of industrially suitable biocatalysts. The non-cultivable approach of searching enzymes is known to provide ample scope to accomplish novelty for their industrial applications. Lip479 clone out of seven lipase-producing clones obtained from Taptapani hot spri...

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Bibliographic Details
Published in:International microbiology 2020-05, Vol.23 (2), p.233-240
Main Authors: Sahoo, Rajesh Kumar, Das, Aradhana, Sahoo, Kalpana, Sahu, Anshuman, Subudhi, Enketeswara
Format: Article
Language:English
Subjects:
Amino acid sequence
Amino acids
Applied Microbiology
Biocatalysts
Biomedical and Life Sciences
Calcium ions
Conserved sequence
Dichloromethane
Eukaryotic Microbiology
Extreme environments
Hot springs
Industrial applications
Iron
Life Sciences
Lipase
Medical Microbiology
Metagenomics
Microbial Ecology
Microbiology
Molecular chains
Open reading frames
Organic solvents
Original Article
Phylogeny
Proteins
Zinc
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Summary:Extreme environments are the main source of industrially suitable biocatalysts. The non-cultivable approach of searching enzymes is known to provide ample scope to accomplish novelty for their industrial applications. Lip479 clone out of seven lipase-producing clones obtained from Taptapani hot spring was found to be optimally active at pH 8.0 and temperature 65 °C. The recombinant Lip479 was highly stable in organic solvents, methanol, DMF, DMSO, acetone, and dichloromethane. Lip479 lipase activity was enhanced in the presence of K + , Mn 2+ , Na + , Zn 2+ , and Ca 2+ except for Fe 3+ . The ability of Lip479 lipase to act on long carbon chain of 4-nitrophenyl myristate suggests it might be a true lipase. Lip479 clone was found to have ORF of 1251 bp encoding 416 amino acid residues of 42.57 KDa size (theoretically calculated). The presence of conserved motif Ala-His-Ser-Gln-Gly and Zn 2+ -binding consensus sequence (GAAHAAKH) of the clone assigns the protein to lipase family 1.5. Phylogenetic lineage of the protein sequence of Lip479 was traced to family 1.5 as it was clubbed up with those of reported lipases of the same family. The above biochemical features indicated that Lip479 lipase can be a potential biocatalyst for its use in various industries.
ISSN:1139-6709
1618-1905
DOI:10.1007/s10123-019-00095-z