Publications by authors named "Ekaterina V Durdenko"

2 Publications

  • Page 1 of 1

New member of the hormone-sensitive lipase family from the permafrost microbial community.

Bioengineered 2017 Jul 18;8(4):420-423. Epub 2016 Oct 18.

b Institute of Physicochemical and Biological Problems in Soil Science , Russian Academy of Sciences , Pushchino , Russia.

Siberian permafrost is a unique environment inhabited with diverse groups of microorganisms. Among them, there are numerous producers of biotechnologically relevant enzymes including lipases and esterases. Recently, we have constructed a metagenomic library from a permafrost sample and identified in it several genes coding for potential lipolytic enzymes. In the current work, properties of the recombinant esterases obtained from this library are compared with the previously characterized lipase from Psychrobacter cryohalolentis and other representatives of the hormone-sensitive lipase family.
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http://dx.doi.org/10.1080/21655979.2016.1230571DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5553336PMC
July 2017

Expression and characterization of a new esterase with GCSAG motif from a permafrost metagenomic library.

FEMS Microbiol Ecol 2016 May 28;92(5):fiw046. Epub 2016 Feb 28.

Institute of Physicochemical and Biological Problems in Soil Science, Russian Academy of Sciences, Institutskaya str., 2, 142290, Pushchino, Moscow Region, Russia.

As a result of construction and screening of a metagenomic library prepared from a permafrost-derived microcosm, we have isolated a novel gene coding for a putative lipolytic enzyme that belongs to the hormone-sensitive lipase family. It encodes a polypeptide of 343 amino acid residues whose amino acid sequence displays maximum likelihood with uncharacterized proteins from Sphingomonas species. A putative catalytic serine residue of PMGL2 resides in a new variant of a recently discovered GTSAG sequence in which a Thr residue is replaced by a Cys residue (GCSAG). The recombinant PMGL2 was produced in Escherichia coli cells and purified by Ni-affinity chromatography. The resulting protein preferably utilizes short-chain p-nitrophenyl esters (C4 and C8) and therefore is an esterase. It possesses maximum activity at 45°C in slightly alkaline conditions and has limited thermostability at higher temperatures. Activity of PMGL2 is stimulated in the presence of 0.25-1.5 M NaCl indicating the good salt tolerance of the new enzyme. Mass spectrometric analysis demonstrated that N-terminal methionine in PMGL2 is processed and cysteine residues do not form a disulfide bond. The results of the study demonstrate the significance of the permafrost environment as a unique genetic reservoir and its potential for metagenomic exploration.
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http://dx.doi.org/10.1093/femsec/fiw046DOI Listing
May 2016
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