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Immobilization of Recombinant E. coli Thermostable Lipase by Entrapment Inside Silica Xerogel and Nanocarbon-in-Silica Composites Full article

Journal Journal of Molecular Catalysis B: Enzymatic
ISSN: 1381-1177 , E-ISSN: 1873-3158
Output data Year: 2013, Volume: 98, Pages: 78-86 Pages count : 9 DOI: 10.1016/j.molcatb.2013.09.022
Tags Entrapment, Heterogeneous biocatalysts, Nanocarbon-in-silica composites, Recombinant strain-producer rE.coli/lip, Thermostable lipase
Authors Kovalenko Galina A. 1 , Beklemishev Anatoly B. 2 , Perminova Larisa V. 1 , Mamaev Aleksey L. 2 , Rudina Nina A. 1 , Moseenkov Sergey I. 1 , Kuznetsov Vladimir L. 1
Affiliations
1 Institute of Catalysis, Novosibirsk 630090, Russia
2 Institute of Biochemistry, Novosibirsk 630117, Russia

Abstract: The multi-component heterogeneous biocatalysts were prepared by entrapment of whole cells or cells’lysates of a recombinant strain Escherichia coli producing of thermostable lipase from Thermomyces lanugi-nosus (rE.coli/lip) inside silica xerogel and nanocarbon-in-silica composites. The properties of intracellularrecombinant lipase and the prepared heterogeneous biocatalysts, such as enzymatic activity and stability,were studied in periodic process of triglycerides’ hydrolysis and interesterification. The thermal stabilityof recombinant lipase was studied by the heating bacteria rE.coli/lip in a buffer and olive oil at 60–100◦C.The effects of nanocarbons included inside SiO2-xerogel, such as multi-walled carbon nanotubes withdifferent diameters and dispersity, and “nano-onion”, on the properties of multi-component biocata-lysts were investigated. The {nanocarbon-in-silica} biocatalysts prepared by entrapping cells’ lysates ofrE.coli/lip together with aggregated “thick” nanotubes (20–22 nm in diameter) were found to possessthe highest hydrolytic activity close to 1000 LU/g. The activity of composite biocatalysts containing cells’lysates of rE.coli/lip and dispersed “thin” nanotubes (9–11 nm in diameter) did not exceed 400 LU/g.The similar effect of nanocarbons’ inclusion inside multi-component biocatalysts on the activities ofentrapped whole cells, cells’ lysates and purified recombinant lipase was revealed.
Cite: Kovalenko G.A. , Beklemishev A.B. , Perminova L.V. , Mamaev A.L. , Rudina N.A. , Moseenkov S.I. , Kuznetsov V.L.
Immobilization of Recombinant E. coli Thermostable Lipase by Entrapment Inside Silica Xerogel and Nanocarbon-in-Silica Composites
Journal of Molecular Catalysis B: Enzymatic. 2013. V.98. P.78-86. DOI: 10.1016/j.molcatb.2013.09.022 WOS Scopus РИНЦ ANCAN OpenAlex
Dates:
Submitted: Mar 4, 2013
Accepted: Sep 23, 2013
Published online: Oct 9, 2013
Published print: Dec 30, 2013
Identifiers:
Web of science: WOS:000328237400012
Scopus: 2-s2.0-84886192557
Elibrary: 21883718
Chemical Abstracts: 2013:1795579
Chemical Abstracts (print): 161:417368
OpenAlex: W2003142756
Citing:
DB Citing
Web of science 20
Scopus 21
Elibrary 22
OpenAlex 28
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