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 |
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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 | ||||
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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
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 |