Prof. Vladimir Elisashvili, DSc. - Agricultural University of Georgia - Head of laboratory

Prof. Vladimir Elisashvili

DSc.

Agricultural University of Georgia

Head of laboratory

Tbilisi | Georgia

Main Specialties: Biotechnology

ORCID logohttps://orcid.org/0000-0003-0856-6589

Prof. Vladimir Elisashvili, DSc. - Agricultural University of Georgia - Head of laboratory

Prof. Vladimir Elisashvili

DSc.

Introduction

Prof. Vladimir Elisashvili has received his PhD from the St Petersburg University (Russia) in 1974 and DSc from the Institute of Biochemistry and Biotechnology (Tbilisi, Georgia) in 1993. He did his postdoctoral training at the Institute of Molecular Biology, Paris, France and worked in institutes and companies of Finland, Israel, Belgium, USA, and Sweden. Currently, he is a head of laboratory of Plant Substrates Bioconversion at the Agricultural University of Georgia and director of the Center for Microbial Technology. He is serving as an Editorial board member of three international journals. He has published more than 180 papers in reputed journals and supervised 21 PhD theses.

Primary Affiliation: Agricultural University of Georgia - Tbilisi , Georgia

Specialties:

Research Interests:

Education

Jan 1974 - Jan 1974
Saint Petersburg State University
PhD

Experience

Jan 2012
Agricultural University of Georgia
Head
Plant Substrates Bioconversion

Publications

80Publications

126Reads

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3PubMed Central Citations

Bacillus amyloliquefaciens Spore Production Under Solid-State Fermentation of Lignocellulosic Residues.

Probiotics Antimicrob Proteins 2018 12;10(4):755-761

Health Promoting Naturals Laboratory, School of Environmental and Biological Sciences, Rutgers State University, New Brunswick, NJ, USA.

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http://dx.doi.org/10.1007/s12602-017-9371-xDOI Listing
December 2018
69 Reads

Recent Advances in the Physiology of Spore Formation for Bacillus Probiotic Production.

Probiotics Antimicrob Proteins 2018 Dec 5. Epub 2018 Dec 5.

Health Promoting Naturals Laboratory, School of Environmental and Biological Sciences, Rutgers, The State University of New Jersey, New Brunswick, NJ, 08901, USA.

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http://link.springer.com/10.1007/s12602-018-9492-x
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http://dx.doi.org/10.1007/s12602-018-9492-xDOI Listing
December 2018
34 Reads

Isolation and Characterization of Lectins Formed by Cerrena unicolor (Higher Basidiomycetes) in Solid-State Fermentation of Sorghum and Wheat Straw.

Int J Med Mushrooms 2015 ;17(5):427-34

S. Durmishidze Institute of Biochemistry and Biotechnology of N.L.E. Georgian Agrarian University, Tbilisi 0159, Georgia.

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April 2016
11 Reads
1 Citation

Trinitrotoluene and mandarin peels selectively affect lignin-modifying enzyme production in white-rot basidiomycetes.

Springerplus 2016 1;5:252. Epub 2016 Mar 1.

Department of Plant Substrates Bioconversion, Agricultural University of Georgia, 240 David Agmashenebeli alley, 0159 Tbilisi, Georgia.

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http://dx.doi.org/10.1186/s40064-016-1895-0DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4773374PMC
March 2016
12 Reads
2 Citations

BIOSYNTHESIS AND SOME PROPERTIES OF LACCASE FROM LENTINUS-TIGRINUS IBR-101

BIOCHEMISTRY-MOSCOW, 1993, 58(12):1448-1452 DEC 1993

BIOCHEMISTRY

The laccase and Mn-dependent peroxidase activities of Lentinus tigrinus IBR-101 were studied in relation to the procedure for cultivation of the fungus and the composition of the nutrient medium. Submerged culture of the basidiomycete in the presence of 4%; citric pulp produces the highest laccase activity, while stationary cultivation on synthetic medium with 1% glucose promotes the highest Mn-dependent peroxidase activity of L. tigrinus IBR-101. The purified laccase is homogeneous by electrophoresis with molecular weight 59.5 kD and has temperature optimum at 50 degrees C and pH optima for laccase activity in the presence of syringaldazine, pyrocatechol, and potassium ferricyanide at 5.3, 4.0, and 3.5, respectively The half-time for laccase inactivation is 2 h at 50 degrees C. The laccase is stable at pH 6-7 and is rapidly inactivated below pH 4.5. The K-m of laccase is 0.57 mM for pyrocatechol and 3.25 mu M for syringaldazine.

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December 1993
12 Reads

MANGANESE PEROXIDASE FROM PLEUROTUS-OSTREATUS - ISOLATION, PURIFICATION, AND PROPERTIES

BIOCHEMISTRY-MOSCOW 57 (8): 863-868

Three manganese peroxidase isoenzymes have been isolated from Pleurotus ostreatus and their biochemical properties and substrate specificities studied The thermal stability and pH dependence of manganese peroxidase III were determined The enzyme is stable at 20-degrees-C, but not at higher temperatures. The pH optimum is 4.5. The K(m) values with Mn2+ and H2O2 are 0.075 and 0.03 mM, respectively.

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August 1992
10 Reads