Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase

Abdallah, Noreldeen Hassan.; Schlumpberger, Miriam.; Gaffney, Darragh; Hanrahan, John P.; Tobin, Joseph M.; Magner, Edmond

doi:10.1016/j.molcatb.2014.06.007

Cited by 13 publications

(5 citation statements)

References 42 publications

(60 reference statements)

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“…In this study, the surface-displayed Tm1350 retained 84 % of its original activity after three uses, which was higher than that reported for lipase SMG1 immobilized on macroporous resin , and was similar to that reported for CALB immobilized on PPS and spore surface-displayed Neu5Ac aldolase (Xu et al 2011;Abdallah et al 2014). Therefore, display of enzymes on the surface of B. subtilis spores may be an effective approach for enzyme immobilization and has great potential for application in the harsh conditions required in the biochemical industry.…”

Section: Discussionsupporting

confidence: 85%

Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein

Chen

Tian

et al. 2015

Extremophiles

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Lipases expressed in microbial hosts have great commercial value, but their applications are restricted by the high costs of production and harsh conditions used in industrial processes, such as high temperature and alkaline environment. In this study, an Escherichia coli-Bacillus subtilis shuttle vector (pHS-cotB-Tm1350) was constructed for the spore surface display of the lipase Tm1350 from hyperthermophilic bacterium Thermotoga maritima MSB8. Successful display of the CotB-Tm1350 fusion protein on spore surface was confirmed by Western blot analysis and activity measurements. The optimal catalytic temperature and pH of the spore surface-displayed Tm1350 were 80 °C and 9, respectively, which were higher than non-immobilized Tm1350 (70 °C and pH 7.5). Analysis of thermal and pH stability showed that spore surface-displayed Tm1350 retained 81 or 70 % of its original activity after 8 h of incubation at pH 8 or pH 9 (70 °C), which were 18 % higher than the retained activity of the non-immobilized Tm1350 under the same conditions. Meanwhile, recycling experiments showed that the recombinant spores could be used for up to three reaction cycles without a significant decrease in the catalytic rate (84 %). These results suggested that enzyme display on the surface of the B. subtilis spore could serve as an effective approach for enzyme immobilization, which has potential applications in the harsh biochemical industry.

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Section: Discussionsupporting

confidence: 85%

Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein

Chen

Tian

et al. 2015

Extremophiles

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“…O processo de imobilização por adsorção física depende do pH da solução enzimática, uma vez que a alteração do pH modifica as cargas da proteína: em geral, quando a carga líquida da proteína é pequena, a repulsão eletrostática entre as moléculas é minimizada e a eficiência da imobilização aumenta (CAI et al, 2016;ABDALLAH et al, 2014). Além disso, há a possibilidade de mudança conformacional da enzima em função do pH, que pode alterar a adsorção da enzima no suporte e sua atividade após a imobilização.…”

Section: Resultsunclassified

Revitalização De Processadoras Automáticas Kodak M35 X-Omat Prox Processor

Cerutti¹,

Reis²,

Santos³

et al. 2019

Impactos Das Tecnologias Nas Ciências Biológicas E Da Saúde 2

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“…Ammonium fluoride (NH 4 F) was from Alfa Aesar (Heysham, U.K.), and potassium chloride and hydrochloric acid were from Panreac (Barcelona, Spain). Porous spherical silicate particles (PSSP) 50 were from Glantreo Limited (Cork, Ireland). All reagents and solvents were of analytical grade.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica

et al. 2017

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Mesoporous silica materials are promising carriers for enzyme immobilization in heterogeneous biocatalysis applications. By tailoring their pore structural framework, these materials are designable for appropriate enzyme binding capacity and internal diffusivity. To supply O 2 efficiently to solid-supported immobilized enzymes represents a core problem of heterogeneously catalyzed oxidative biotransformations. In this study, therefore, we synthesized and compared three internally well-ordered and two amorphous silica materials as enzyme carriers, each of those with pore sizes of ≥10 nm, to enable the co-immobilization of D-aminoacid oxidase (93 kDa) and catalase (245 kDa). Both enzymes were fused to the silica-binding module Z basic2 to facilitate their selective and oriented immobilization directly from crude protein mixtures on native silica materials. Analyzing the effects of varied pore architecture and internal surface area on the performance of the immobilized bienzymatic system, we showed that a uniform pore structural framework was beneficial for enzyme loading (≥ 70 mg protein/g carrier), immobilization yield (≥ 90%), surface and pore volume filling without hindered adsorption, and catalytic effectiveness (≥ 60%) of the co-immobilizate. Using the best carrier LP-SBA-15, we obtained a solid oxidase-catalase preparation with an activity of 2000 µmol/(min g_material) that was recyclable and stable during oxidation of D-methionine. These results affirm a strategy of optimizing immobilized O 2 -dependent enzymes via tunable internal structuring of the silica material used as carrier. They thus make a significant advance towards the molecular design of heterogeneous oxidation biocatalysts on mesoporous silica supports.

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Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase

Cited by 13 publications

References 42 publications

Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein

Surface display of the thermophilic lipase Tm1350 on the spore of Bacillus subtilis by the CotB anchor protein

Revitalização De Processadoras Automáticas Kodak M35 X-Omat Prox Processor

Oriented Coimmobilization of Oxidase and Catalase on Tailor-Made Ordered Mesoporous Silica

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