Designing continuous flow reaction of xylan hydrolysis for xylooligosaccharides production in packed-bed reactors using xylanase immobilized on methacrylic polymer-based supports

Romero‐Fernández, María; Moreno-Pérez, Sonia; Orrego, Alejandro H.; Oliveira, Solange; Santamaría, Ramón I.; Díaz, Margarita; Guisán, José M.

doi:10.1016/j.biortech.2018.06.070

Cited by 44 publications

(38 citation statements)

References 45 publications

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“…Based on the maximum protein loading and thermal stability of the biocatalyst, the support Relizyme R403/S was selected to set up a packed‐bed reactor for continuous production of XOS. The specific productivity was 3.277 g XOS g enzyme −1 h −1 in a packed‐bed reactor, leading to a robust biocatalyst that kept >90 % of its initial activity after 120 h of continuous operation . Likewise, another case study of aqueous continuous packed‐bed bioreactor (with high substrate loadings) is the lactulose syrup synthesis from fructose and lactose catalyzed by Aspergillus oryzae β‐galactosidase immobilized in glyoxyl‐agarose .…”

Section: Aqueous Media For Continuous Biocatalysismentioning

confidence: 99%

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Guajardo

Marı́a²

2019

ChemCatChem

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Enzyme catalysis (biocatalysis) is a mature strategy to perform organic synthesis with high selectivity and under mild reaction conditions. However, despite their origin and biodegradability, the simple use of enzymes is not sufficient to validate a process as green or sustainable. To reinforce the value that biocatalysis may offer, enzymatic processes can be established in environmentally‐friendly media, such as water, neoteric solvents (e. g. deep‐eutectic‐solvents, DES), biogenic solvents (e. g. 2‐MeTHF or terpenes), or even solvent‐free systems (if substrates allow that). Furthermore, these options can be conducted in continuous biocatalytic processes, which are more efficient and sustainable. Hence, a triple synergy is generated, and very promising environmentally‐friendly options can be envisaged. This conceptual paper discusses these alternatives, providing relevant, recently reported, successful examples.

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Section: Aqueous Media For Continuous Biocatalysismentioning

confidence: 99%

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Guajardo

Marı́a²

2019

ChemCatChem

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“…3.2.1.37), α-glucuronidase (EC 3.2.1.139) acetylxylan esterase (EC 3.1.1.72), α-l-arabinofuranosidases (E.C. 3.2.1.55), p-coumaric esterase (3.1.1.B10) and ferulic acid esterase (EC 3.1.1.73) involved in the depolymerization of xylan into simple monosaccharide and xylooligosaccharides (Gomez et al 2008;Juturu and Wu 2014;Walia et al 2017;Romero-Fernández et al 2018).…”

Section: Introductionmentioning

confidence: 99%

A detailed overview of xylanases: an emerging biomolecule for current and future prospective

Bhardwaj

Kumar

Verma

2019

Bioresour. Bioprocess.

277

105

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Xylan is the second most abundant naturally occurring renewable polysaccharide available on earth. It is a complex heteropolysaccharide consisting of different monosaccharides such as l-arabinose, d-galactose, d-mannoses and organic acids such as acetic acid, ferulic acid, glucuronic acid interwoven together with help of glycosidic and ester bonds. The breakdown of xylan is restricted due to its heterogeneous nature and it can be overcome by xylanases which are capable of cleaving the heterogeneous β-1,4-glycoside linkage. Xylanases are abundantly present in nature (e.g., molluscs, insects and microorganisms) and several microorganisms such as bacteria, fungi, yeast, and algae are used extensively for its production. Microbial xylanases show varying substrate specificities and biochemical properties which makes it suitable for various applications in industrial and biotechnological sectors. The suitability of xylanases for its application in food and feed, paper and pulp, textile, pharmaceuticals, and lignocellulosic biorefinery has led to an increase in demand of xylanases globally. The present review gives an insight of using microbial xylanases as an "Emerging Green Tool" along with its current status and future prospective.

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“…Among the covalent methods, one of the most effective approaches are enzyme immobilization by multipoint covalent attachment on supports functionalized with glyoxyl (short aliphatic aldehydes) groups [8,9]. This attachment consists of the irreversible immobilization of proteins to an insoluble support such as silica [17], agarose [18], or methacrylic polymers [19,20], magnetic nanoparticles [21], even lignocellulosic wastes [22,23]. One of these supports is cross-linked agarose, which consists of macroporous agarose beads functionalized with glyoxyl groups (GA).…”

Section: Introductionmentioning

confidence: 99%

“…This immobilization chemistry promotes a very intense multipoint covalent attachment through Schiff base formation between the aldehydes of the support surface and the non-protonated amino groups of the enzyme surface [9,18]. Moreover, this immobilization protocol can be applied to commercial polyacrylic supports (e.g., Sepabeads and Purolite) containing epoxy groups [20]. Usually, these supports also contain glyceryl groups that derive from the epoxide groups.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, the conventional immobilization on GA of five of the enzymes used in this study have been previously published: a xylanase from Streptomyces halstedii [37] (Xys1∆), D-amino acid oxidase from Trigonopsis variabilis [38] (DAAO), penicillin G acylase from Escherichia coli [39] (PGA), and two dehydrogenases [11,29] (a glycerol dehydrogenase from Celullomonas sp., GlyDH, and an alcohol dehydrogenase from Thermus thermophilus HB27, ADH2). These supported biocatalysts have been used for the production of different value-added products, such as xylooligosaccharides for the Xys1∆ biocatalyst [20,40], keto-esters from D-amino acids, or 7-aminocephalosporanic acid from cephalosporin C for the DAAO biocatalyst [38,39] and the production of cephalosporins for the PGA biocatalyst in the pharmaceutical industry [39]. Finally, GlyDH oxidizes glycerol to 1,3-dihydroxyacetone [11], and ADH2 is a catalyst with anti-Prelog selectivity for prochiral aryl ketones, and that preferentially produces R-profens [29].…”

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confidence: 99%

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Stabilization of Enzymes by Multipoint Covalent Attachment on Aldehyde-Supports: 2-Picoline Borane as an Alternative Reducing Agent

et al. 2018

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Enzyme immobilization by multipoint covalent attachment on supports activated with aliphatic aldehyde groups (e.g., glyoxyl agarose) has proven to be an excellent immobilization technique for enzyme stabilization. Borohydride reduction of immobilized enzymes is necessary to convert enzyme–support linkages into stable secondary amino groups and to convert the remaining aldehyde groups on the support into hydroxy groups. However, the use of borohydride can adversely affect the structure–activity of some immobilized enzymes. For this reason, 2-picoline borane is proposed here as an alternative milder reducing agent, especially, for those enzymes sensitive to borohydride reduction. The immobilization-stabilization parameters of five enzymes from different sources and nature (from monomeric to multimeric enzymes) were compared with those obtained by conventional methodology. The most interesting results were obtained for bacterial (R)-mandelate dehydrogenase (ManDH). Immobilized ManDH reduced with borohydride almost completely lost its catalytic activity (1.5% of expressed activity). In contrast, using 2-picoline borane and blocking the remaining aldehyde groups on the support with glycine allowed for a conjugate with a significant activity of 19.5%. This improved biocatalyst was 357-fold more stable than the soluble enzyme at 50 °C and pH 7. The results show that this alternative methodology can lead to more stable and active biocatalysts.

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Designing continuous flow reaction of xylan hydrolysis for xylooligosaccharides production in packed-bed reactors using xylanase immobilized on methacrylic polymer-based supports

Cited by 44 publications

References 45 publications

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

Continuous Biocatalysis in Environmentally‐Friendly Media: A Triple Synergy for Future Sustainable Processes

A detailed overview of xylanases: an emerging biomolecule for current and future prospective

Stabilization of Enzymes by Multipoint Covalent Attachment on Aldehyde-Supports: 2-Picoline Borane as an Alternative Reducing Agent

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