Recombinant strain producing thermostable lipase from Thermomyces lanuginosus immobilized into nanocarbon-in-silica matrices and properties of the prepared biocatalysts

• Published in: Applied biochemistry and microbiology Vol. 49; no. 3; pp. 296 - 305
• Main Authors: Kovalenko, G. A, Beklemishev, A. B, Perminova, L. B, Chuenko, T. V, Mamaev, A. L, Ivanov, I. D, Moseenkov, S. I, Kuznetsov, V. L
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer-Verlag 01.05.2013; SP MAIK Nauka/Interperiodica; Springer Nature B.V
• Subjects: Biochemistry; Biomedical and Life Sciences; Biosynthesis; carbon; carbon nanotubes; cell suspension culture; Enzymes; Escherichia coli; Fungi; half life; heat treatment; hydrolysis; Life Sciences; Medical Microbiology; Microbiology; nanospheres; Olea; olive oil; thermal stability; Thermomyces lanuginosus; triacylglycerol lipase; Lipase; Apply Biochemistry; Silica Aerogel; Reaction Cycle; Lipolytic Activity
• ISSN: 0003-6838; 1608-3024
• DOI: 10.1134/S0003683813030113

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.