Combined CLEAs of invertase and soy protein for economically feasible conversion of sucrose in a fed-batch reactor

Mafra, Agnes Cristina Oliveira; Beltrame, Maisa Bontorin; Ulrich, Letícia Gazzotto; Giordano, Raquel de Lima Camargo; Ribeiro, Marcelo Perencin de Arruda; Tardioli, Paulo Waldir

doi:10.1016/j.fbp.2018.05.006

Cited by 18 publications

(12 citation statements)

References 74 publications

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“…Several groups have reported sucrose hydrolyzation using different invertases (Table 4). Compared with such invertases, GspInv has high sucrose concentration and conversion factor, which implies its application potential in producing inverted sugars (Amaya-Delgado et al, 2006;Gómez et al, 2006;Sanjay and Sugunan, 2006;Tomotani and Vitolo, 2007;Koli and Gaikar, 2016;Oliveira et al, 2018).…”

Section: Reusability Of the Immobilized Invertase During Hfs Preparationmentioning

confidence: 99%

Identification and Immobilization of an Invertase With High Specific Activity and Sucrose Tolerance Ability of Gongronella sp. w5 for High Fructose Syrup Preparation

et al. 2020

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Invertases catalyze the hydrolysis of sucrose into fructose and glucose and can be employed as an alternative in producing high fructose syrup. In this study, we reported the heterologous expression of an invertase gene (GspInv) of Gongronella sp. w5 in Komagataella pastoris. GspInv activity reached 147.6 ± 0.4 U/mL after 5 days of methanol induction. GspInv is invertase with a high specific activity of 2,776.1 ± 124.2 U/mg toward sucrose. GspInv showed high tolerance to sucrose (IC 50 = 1.2 M), glucose (IC 50 > 2 M), fructose (IC 50 = 1.5 M), and a variety of metal ions that make it an ideal candidate for high fructose syrup production. A carbohydratebinding module was sequence-optimized and fused to the N-terminus of GspInv. The fusion protein had the highest immobilization efficiency at room temperature within 1 h adsorption, with 1 g of cellulose absorption up to 8,000 U protein. The celluloseimmobilized fusion protein retained the unique properties of GspInv. When applied in high fructose syrup preparation by using 1 M sucrose as the substrate, the sucrose conversion efficiency of the fused protein remained at approximately 95% after 50 h of continuous hydrolysis on a packed bed reactor. The fused protein can also hydrolyze completely the sucrose in sugarcane molasses. Our results suggest that GspInv is an unusual invertase and a promising candidate for high fructose syrup preparation.

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Section: Reusability Of the Immobilized Invertase During Hfs Preparationmentioning

confidence: 99%

Identification and Immobilization of an Invertase With High Specific Activity and Sucrose Tolerance Ability of Gongronella sp. w5 for High Fructose Syrup Preparation

et al. 2020

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“…Some modifications have been made to the CLEAs such as, for example, the addition of bovine serum albumin to improve crosslinking or the incorporation of pores to reduce diffusion limitation problems . The advantages of this method include the non‐dilution of the enzyme after immobilization, cost reduction by not having to use a solid (and, in some cases, expensive) support, less mass transfer limitation, and greater activity per biocatalyst mass . Among the disadvantages of the method are its low mechanical stability and the unfortunate lack of exact methodologies for the synthesis of crosslinked enzymes that allow the size, selectivity and stability of the enzymes to be controlled.…”

Section: Polymer Supports For Degradation Of Organic Pollutantsmentioning

confidence: 99%

Polymer supports for the removal and degradation of hazardous organic pollutants: an overview

Urbano

Bustamante

Palacio

et al. 2020

Polymer International

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Over the last decades, the presence of highly organic pollutants has increased and become an environmental problem that affects all forms of life. To solve or reduce this problem, multiple strategies have been proposed for the elimination and degradation of organic compounds in aqueous media. This review aims to revise and critically discuss the most recent advances in polymer supports to be used for the adsorption and degradation of organic pollutants. However, the greatest challenge with respect to this issue is the industrial scale‐up of bioremediation processes that allow the removal and degradation of compounds in a continuous and large‐scale manner. © 2019 Society of Chemical Industry

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“…Another likely problem is when one enzyme is poor in Lys groups, and intermolecular crosslinking of the enzyme aggregate is difficult. This may be solved using a feeder protein or an aminated polymer, or by chemically aminating the enzyme [14,[41][42][43][44][45][46][47][48][49][50][51][52][53]. The feeders also reduce the enzyme volumetric load, and as a consequence, the substrate diffusional problems.…”

Section: Introductionmentioning

confidence: 99%

Combi-CLEAs of Glucose Oxidase and Catalase for Conversion of Glucose to Gluconic Acid Eliminating the Hydrogen Peroxide to Maintain Enzyme Activity in a Bubble Column Reactor

et al. 2019

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In this study combined cross-linked aggregates of catalase from bovine liver and glucose-oxidase from Aspergillus niger were prepared, and the effects of the precipitant and crosslinking agents, as well as the use of bovine serum albumin (BSA) as a feeder protein, on enzyme immobilization yield and thermal stability of both enzymes, were evaluated. Combi- crosslinking of enzyme aggregates (CLEAs) prepared using dimethoxyethane as precipitant, 25 mM glutaraldehyde and BSA/enzymes mass ratio of 5.45 (w/w), exhibited the highest enzyme activities and stabilities at 40 °C, pH 6.0, and 250 rpm for 5 h. The stability of both immobilized enzymes was fairly similar, eliminating one of the problems of enzyme coimmobilization. Combi-CLEAs were used in gluconic acid (GA) production in a bubble column reactor operated at 40 °C, pH 6.0 and 10 vvm of aeration, using 26 g L−1 glucose as the substrate. Results showed conversion of around 96% and a reaction course very similar to the same process using free enzymes. The operational half-life was 34 h, determined from kinetic profiles and the first order inactivation model. Combi-CLEAs of glucose-oxidase and catalase were shown to be a robust biocatalyst for applications in the production of gluconic acid from glucose.

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Combined CLEAs of invertase and soy protein for economically feasible conversion of sucrose in a fed-batch reactor

Cited by 18 publications

References 74 publications

Identification and Immobilization of an Invertase With High Specific Activity and Sucrose Tolerance Ability of Gongronella sp. w5 for High Fructose Syrup Preparation

Identification and Immobilization of an Invertase With High Specific Activity and Sucrose Tolerance Ability of Gongronella sp. w5 for High Fructose Syrup Preparation

Polymer supports for the removal and degradation of hazardous organic pollutants: an overview

Combi-CLEAs of Glucose Oxidase and Catalase for Conversion of Glucose to Gluconic Acid Eliminating the Hydrogen Peroxide to Maintain Enzyme Activity in a Bubble Column Reactor

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