Production and capture of β-glucosidase from Thermoascus aurantiacus using a tailor made anionic cryogel

Mól, Paula Chequer Gouveia; Veríssimo, Lizzy Ayra Alcântara; Minim, Luís Antônio; Boscolo, Maurício; Gomes, Eleni; Silva, Roberto da

doi:10.1016/j.procbio.2019.03.029

Cited by 15 publications

(13 citation statements)

References 39 publications

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“…The hydraulic permeability was calculated by Darcy-Weisbach Eq. ( 6) (𝐾 𝑤 = 2.51x10 -13 m 2 ), which is a result close to other polyacrylamide cryogels reported by Mól et al (2019), Fontan et al (2018), Mól et al (2017) and Carvalho et al (2014). This value is related to the resistance to flow through the activated cryogel and it is considered low, compared to fixed bed columns.…”

Section: Characterization Of the Affinity Cryogelsupporting

confidence: 90%

“…These analyses show that the cryogel mass occupies a large volume when hydrated, reinforcing the nature of the pores of its structure, as well as a sponge and elastic characteristic and consistent, confirming what several authors have reported for other types of activated cryogels (NEVES et al, 2020;DE OLIVEIRA et al, 2019;MÓL et al, 2019;YAO et al, 2006).…”

Section: Characterization Of the Affinity Cryogelsupporting

confidence: 89%

“…1 shows the infrared absorption spectra of the pure and activated cryogels. It was verified that the activated cryogel presented a wider and higher band than pure cryogel at 3100-3600 cm -1 , which indicates the presence of water (O-H) and stretching vibrations of -N- MÓL et al, 2019;TAO, SUN et al, 2014). This evidences the immobilization of the paminobenzenesulfonamide ligand on the cryogel, since the epoxy groups of the cryogel react with the amino group of the ligand.…”

Section: Characterization Of the Affinity Cryogelmentioning

confidence: 90%

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Desenvolvimento de estratégias de purificação de lactoferrina e lactoperoxidase do soro de leite

Maciel¹

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Processos de purificação da lactoferrina e da lactoperoxidase têm sido relatados na literatura. No entanto, é apresentado um grande número de operações unitárias, alto custo dos suportes cromatográficos, baixa pureza e rendimento da molécula. Nesse sentido, a redução de etapas, a busca por novos adsorventes e, consequentemente, a redução de custos é crucial nesses processos. Além disso, a utilização de sistemas com maior porosidade oferecem alternativas por permitir a captura direta da molécula a partir de soluções particuladas e viscosas, sem a necessidade de tratamento prévio. Nesse sentido, estudar os parâmetros operacionais que afetam a porosidade do meio é determinante para otimizar as condições experimentais. A fim de melhor avaliar estes mecanismos, foram realizados estudos hidrodinâmicos e de capacidade adsortiva em colunas macroporosas de leito expandido e fixo, e posteriormente, a captura das proteínas alvo. Portanto, esse trabalho apresenta uma nova estratégia de purificação para as proteínas lactoferrina (Capítulo I) e lactoperoxidase (Capítulo II) a partir do soro de leite utilizando colunas de leito expandido e de criogel de afinidade, respectivamente. Os suportes cromatográficos analisados foram uma resina de troca catiônica Streamline SP XL e uma matriz polimérica esponjosa altamente interconectada ativada com p-aminobenzenosulfonamida para interação específica com a lactoferrina e a lactoperoxidase, respectivamente. Com o objetivo de avaliar a eficiência da separação das proteínas de cada processo, parâmetros de purificação foram investigados. Palavras-chave: Colunas macroporosas. Propriedades hidrodinâmicas. Capacidade adsortiva. Separação. Proteínas.

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Section: Characterization Of the Affinity Cryogelsupporting

confidence: 90%

Section: Characterization Of the Affinity Cryogelsupporting

confidence: 89%

Section: Characterization Of the Affinity Cryogelmentioning

confidence: 90%

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Desenvolvimento de estratégias de purificação de lactoferrina e lactoperoxidase do soro de leite

Maciel¹

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“…Macroporous structure and pore sizes of the SAM‐cryogel were evaluated using a scanning electron microscope (LEO 1430 VP, Zeiss, Jena, Germany) operated at 15 kV. A sample from the center of the cryogel was cut and then coated with a layer of gold and the gel structure was examined [21].…”

Section: Methodsmentioning

confidence: 99%

Synthesis and characterization of supermacroporous cryogel with immobilized p‐aminobenzenesulfonamide as affinity ligand for the purification of lactoperoxidase from whey

Maciel

Mól

Veríssimo

et al. 2022

J of Separation Science

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This study proposed the development of a monolithic supermacroporous affinity column for direct capture of lactoperoxidase, a glycoprotein present in milk, whey, and colostrum, with several applications due to its wide antimicrobial activity. A poly(acrylamide)-based cryogel was produced by radical co-polymerization of monomers in frozen aqueous solution and activated with p-aminobenzenesulfonamide as a ligand for specific interaction with the lactoperoxidase. The axial liquid dispersion coefficients at different liquid flow rates were determined by measuring residence time distributions using the tracer pulse-response method. The axial dispersion coefficient was low and the height equivalent to theoretical plate was not dependent on the flow velocity. The adsorptive capacity of affinity cryogel was studied as a function of flow velocity and the best condition was 0.9 cm/min. The response surface methodology was applied to optimize the capture of the enzyme, as a function of pH and salt concentration. Higher purification factor value was found at a salt concentration of 80 mmol/L and pH of 8.0 (p < 0.05). There was no influence of the variables under study on the yield (p > 0.05). The results indicated that affinity cryogel is a promising chromatography support for the use in high-throughput one-step purification of lactoperoxidase from whey.

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“…Beta-glucosidase may also be reused by the immobilization, and hence the activity of BGL and the stability over various pH and temperature ranges can also be enhanced [188]. In a recent study by Moi et al, the β-glucosidase produced from Thermoascus aurantiacus was captured in anionic cryogel, which may function as a chromatographic media and as an immobilizer for β-glucosidase [189]. In a study by Chen et al, the immobilization of BGL was done on a nanoparticle of Fe 3 O 4 with agarose, and after 15 consecutive cycles, ~90% of the enzymatic activity was recorded [190].…”

Section: Challenges and Future Prospectsmentioning

confidence: 99%

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

et al. 2019

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The biomass to biofuels production process is green, sustainable, and an advanced technique to resolve the current environmental issues generated from fossil fuels. The production of biofuels from biomass is an enzyme mediated process, wherein β-glucosidase (BGL) enzymes play a key role in biomass hydrolysis by producing monomeric sugars from cellulose-based oligosaccharides. However, the production and availability of these enzymes realize their major role to increase the overall production cost of biomass to biofuels production technology. Therefore, the present review is focused on evaluating the production and efficiency of β-glucosidase enzymes in the bioconversion of cellulosic biomass for biofuel production at an industrial scale, providing its mechanism and classification. The application of BGL enzymes in the biomass conversion process has been discussed along with the recent developments and existing issues. Moreover, the production and development of microbial BGL enzymes have been explained in detail, along with the recent advancements made in the field. Finally, current hurdles and future suggestions have been provided for the future developments. This review is likely to set a benchmark in the area of cost effective BGL enzyme production, specifically in the biorefinery area.

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Production and capture of β-glucosidase from Thermoascus aurantiacus using a tailor made anionic cryogel

Cited by 15 publications

References 39 publications

Desenvolvimento de estratégias de purificação de lactoferrina e lactoperoxidase do soro de leite

Desenvolvimento de estratégias de purificação de lactoferrina e lactoperoxidase do soro de leite

Synthesis and characterization of supermacroporous cryogel with immobilized p‐aminobenzenesulfonamide as affinity ligand for the purification of lactoperoxidase from whey

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

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