Influence of precursors and additives on microbial lipases stabilized by sol-gel entrapment

Péter, Fráncisc; Poppe, László; Kiss, Claudia; Szocs-Bíró, Emese; Preda, Gabriela; Zarcula, Cristina; Olteanu, Alina

doi:10.1080/10242420500190225

Cited by 15 publications

(7 citation statements)

References 24 publications

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“…Although increased porosity of the matrix is commonly associated with higher activity of the immobilized enzyme, structural characteristics most probably play the main role. Our previous results demonstrated that higher content of hydrophobic groups in the silica matrix was propitious for the catalytic efficiency of microbial lipases [26] and such a conclusion is in accordance with the findings of other groups [16, 20]. The hydrophobic phenyl and vinyl groups of the silane precursors that are retrieved in the xerogel are beneficial for the catalytic activity of lipases, particularly in the case of conversion of hydrophobic substrates in non-polar solvents.…”

Section: Resultssupporting

confidence: 87%

Influence of the Physico-Chemical Characteristics of the Hybrid Matrix on the Catalytic Properties of Sol-Gel Entrapped Pseudomonas Fluorescens Lipase

Paul

Borza

Marcu

et al. 2016

Nanomaterials and Nanotechnology

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Lipase from Pseudomonas fluorescens (Amano AK) was immobilized using the sol-gel entrapment technique and sol-gel entrapment combined with adsorption on a solid support (Celite 545). The sol-gel matrices were obtained using as precursors ternary mixtures of tetramethoxysilane and trimethoxysilanes substituted with phenyl or vinyl groups, at different molar ratios, and 1-octyl-3-methyl-immidazolium tetrafluoroborate as additive. The obtained enzymatic preparates were efficient biocatalysts in the acylation reaction of racemic secondary alcohols. Several methods were employed for the characterization of the resulting bioactive materials, in order to correlate the catalytic performance with the morphological and physico-chemical properties of the matrix: Fourier transform infrared spectroscopy (FTIR), BET-analysis of specific surface and porosity, laser scanning confocal microscopy (LSCM), scanning electron microscopy (SEM), atomic force microscopy (AFM) and thermogravimetric analysis (TGA). An extensive study attested the excellent temperature stability and reusability of the immobilized lipases, thus indicating their possible utilization in industrial applications.

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Section: Resultssupporting

confidence: 87%

Influence of the Physico-Chemical Characteristics of the Hybrid Matrix on the Catalytic Properties of Sol-Gel Entrapped Pseudomonas Fluorescens Lipase

Paul

Borza

Marcu

et al. 2016

Nanomaterials and Nanotechnology

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“…Although several researchers have reported on the positive correlation between the ratio of alkyl monomers in the matrix and the lipolytic activity, here we revealed an improvement in catalytic performance in the less preferable known network comprising aromatic side chains . This increase in activity in the aromatic environment relative to that in the aliphatic counterpart may be possibly explained by interaction of the lysate proteins with the matrix surface (statistically, representing most of the protein–network interactions inside the sol–gel particles).…”

Section: Resultscontrasting

confidence: 43%

“…The ability to use the biocatalyst for several successive reaction cycles is an important feature in industrial applications, in general, and for large‐scale biodiesel production, in particular. Sol–gel immobilization is considered an inexpensive, easy, and straightforward approach, and it is scalable for mass production of encapsulating enzymes ,. The use of the crude cell extract containing the lipase without the need for costly affinity purifications can reduce financial costs and avoid complicated downstream processing .…”

Section: Resultsmentioning

confidence: 99%

Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel

et al. 2016

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Two ternary sol-gel matrices, an octyltriethoxysilane-based aliphatic matrix and a phenyltriethoxysilane (PTEOS)-based aromatic matrix, were used to immobilize a methanol-stable variant of lipase from Geobacillus stearothermophilus T6 for the synthesis of biodiesel from waste oil. Superior thermal stability of the mutant versus the wildtype in methanol was confirmed by intrinsic protein fluorescence measurements. The influence of skim milk and soluble E. coli lysate proteins as bulking and stabilizing agents in conjunction with sol-gel entrapment were investigated. E. coli lysate proteins were better stabilizing agents of the purified lipase mutant than skim milk, as evidenced by reverse engineering of the aromatic-based system. This was also shown for commercial Candida antarctica lipase B (CaLB) and Thermomyces lanuginosus lipase (TLL). Uniform, dense, and nonaggregated particles imaged by scanning electron microscopy and a small particle size of 13 μm pertaining to the system comprising PTEOS and E. coli lysate proteins correlated well with high esterification activity. Combining protein and immobilization engineering resulted in a durable biocatalyst with efficient recycling ability and high biodiesel conversion rates.

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“…Mesoporous silica supports were proven particularly efficient for applications related to retention and release of various biomolecules [ 15 ]. Sol-gel encapsulation has proved to be a particularly easy and effective way to immobilize purified enzymes and other proteins or even whole cells [ 1 , 3 , 14 , 16 , 17 , 18 , 19 , 20 , 21 , 22 ]. The main advantages of this immobilization technique are enhanced operational and thermal stability of the obtained preparates.…”

Section: Introductionmentioning

confidence: 99%

Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols

et al. 2012

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Sol-gel entrapment is an efficient immobilization technique that allows preparation of robust and highly stable biocatalysts. Lipase from Candida antarctica B was immobilized by sol-gel entrapment and by sol-gel entrapment combined with adsorption on Celite 545, using a ternary silane precursor system. After optimization of the immobilization protocol, the best enzyme loading was 17.4 mg/g support for sol-gel entrapped lipase and 10.7 mg/g support for samples obtained by entrapment and adsorption. Sol-gel immobilized enzymes showed excellent values of enantiomeric ratio E and activity when ionic liquid 1-octyl-3-methyl-imidazolium tetrafluoroborate was used as additive. Immobilization increased the stability of the obtained biocatalysts in several organic solvents. Excellent operational stability was obtained for the immobilized lipase, maintaining unaltered catalytic activity and enantioselectivity during 15 reuse cycles. The biocatalysts were characterized using scanning electron microscopy (SEM) and fluorescence microscopy. The improved catalytic efficiency of entrapped lipases recommends their application for large-scale kinetic resolution of optically active secondary alcohols.

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Influence of precursors and additives on microbial lipases stabilized by sol-gel entrapment

Cited by 15 publications

References 24 publications

Influence of the Physico-Chemical Characteristics of the Hybrid Matrix on the Catalytic Properties of Sol-Gel Entrapped Pseudomonas Fluorescens Lipase

Influence of the Physico-Chemical Characteristics of the Hybrid Matrix on the Catalytic Properties of Sol-Gel Entrapped Pseudomonas Fluorescens Lipase

Creating an Efficient Methanol‐Stable Biocatalyst by Protein and Immobilization Engineering Steps towards Efficient Biosynthesis of Biodiesel

Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols

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