Recombinant Strain Producing Thermostable Lipase from Thermomyces lanuginosus Immobilized into Nanocarbonin Silica Matrices and Properties of the Prepared Biocatalysts | Sciact - CRIS-system of Boreskov Institute of Catalysis

Recombinant Strain Producing Thermostable Lipase from Thermomyces lanuginosus Immobilized into Nanocarbonin Silica Matrices and Properties of the Prepared Biocatalysts Full article

Journal

Applied Biochemistry and Microbiology
ISSN: 0003-6838 , E-ISSN: 1608-3024

Output data

Year: 2013, Volume: 49, Number: 3, Pages: 296-305 Pages count : 10 DOI: 10.1134/S0003683813030113

Tags

Lipase; Apply Biochemistry; Silica Aerogel; Lipolytic Activity; Reaction Cycle

Authors

Kovalenko G.A. ^1,2 , Beklemishev A.B. ³ , Perminova L.V. ¹ , Chuenko T.V. ¹ , Mamaev A.L. ³ , Ivanov I.D. ³ , Moseenkov S.I. ¹ , Kuznetsov V.L. ^1,2

Affiliations

1	Boreskov Institute of Catalysis, Siberian Division, Russian Academy of Sciences, pr. akademika Lavrent’eva 5, Novosibirsk, 630090 Russia
2	Novosibirsk State University, Novosibirsk, Russia
3	Research Institute for Biochemistry, Siberian Division, Russian Academy of Medical Sciences, Novosibirsk, 630117 Russia

Multicomponent composite biocatalysts with lipolytic activity have been studied. These biocatalysts were prepared via the immobilization of a recombinant strain-producer of thermostable lipase from Thermomyces lanuginosus into SiO2 xerogel, which contains a nanocarbon component, i.e., multiwalled carbon nanotubes with varying diameters, and also bulb-like structured carbon nanospheres (“nano-onion”). The properties of lipase were studied both in cell suspensions of a recombinant strain-producer constructed on the basis of E. coli BL21(DE3) and in the immobilized state with regard to the structure and dispersity of the nanocarbon included inside the biocatalysts. It was shown that the recombinant intracellular lipase exerted its activity in a reaction of tributyrine hydrolysis on average value of 50 U/mg of dry cells and had a high thermostability. Upon heating in olive oil at 100°C, the inactivation constant and the half-life inactivation time comprised 6 × 10−3 min−1 and 2 h, respectively, exceeding by one order the thermostability of lipase in a buffer solution. Biocatalysts that contained aggregated thick carbon nanotubes with a diameter of 20–22 nm had the maximum initial activity ca. 250 U/g.

Kovalenko G.A. , Beklemishev A.B. , Perminova L.V. , Chuenko T.V. , Mamaev A.L. , Ivanov I.D. , Moseenkov S.I. , Kuznetsov V.L.
Recombinant Strain Producing Thermostable Lipase from Thermomyces lanuginosus Immobilized into Nanocarbonin Silica Matrices and Properties of the Prepared Biocatalysts
Applied Biochemistry and Microbiology. 2013. V.49. N3. P.296-305. DOI: 10.1134/S0003683813030113 WOS Scopus РИНЦ ANCAN OpenAlex

Коваленко Г.А. , Беклемишев А.Б. , Перминова Л.В. , Чуенко Т.В. , Мамаев А.Л. , Иванов И.Д. , Мосеенков С.И. , Кузнецов В.Л.
Иммобилизация рекомбинантного штамма–продуцента термостабильной липазы из Thermomyces lanuginosus в наноуглерод-силикатные матрицы и свойства приготовленных биокатализаторов
Прикладная биохимия и микробиология. 2013. Т.49. №3. С.301-311. DOI: 10.7868/S0555109913030112 Scopus РИНЦ OpenAlex

Submitted:	May 11, 2012
Published print:	May 1, 2013
Published online:	May 9, 2013

Web of science:	WOS:000318798500012
Scopus:	2-s2.0-84877342039
Elibrary:	20427338
Chemical Abstracts:	2013:729902
Chemical Abstracts (print):	160:157099
OpenAlex:	W2473605603

DB	Citing
Web of science	7
Scopus	8
Elibrary	7
OpenAlex	9