Deep Eutectic Solvents as New Reaction Media to Produce Alkyl-Glycosides Using Alpha-Amylase from Thermotoga maritima

Miranda-Molina, Alfonso; Xolalpa, Wendy; Strompen, Simon; Arreola-Barroso, Rodrigo; Olvera, Leticia; López-Munguı́a, Agustı́n; Castillo, Edmundo; Saab‐Rincón, Gloria

doi:10.3390/ijms20215439

Cited by 12 publications

(14 citation statements)

References 38 publications

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“…Circular dichroism measurements of Amy A showed that large conformational changes were observed above 60 • C, changes not observed in aqueous medium. The authors claim that this is the first report on the effect of DES and temperature on an enzyme, to establish the temperature limit for a thermostable enzyme in DES [10].…”

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confidence: 89%

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Carbohydrate-Active Enzymes: Structure, Activity, and Reaction Products

Benini¹

2020

IJMS

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Carbohydrate-active enzymes are responsible for both the biosynthesis and breakdown of carbohydrates and glycoconjugates. They are involved in many metabolic pathways, in the biosynthesis and degradation of various biomolecules, such as bacterial exopolysaccharides, starch, cellulose, and lignin, and in the glycosylation of proteins and lipids. Their interesting reactions have attracted the attention of researchers belonging to different scientific fields ranging from basic research to biotechnology. Interest in carbohydrate-active enzymes is due not only to their ability to build and degrade biopolymers, which is highly relevant in biotechnology, but also because they are involved in bacterial biofilm formation, and in the glycosylation of proteins and lipids, which has important health implications.This Special Issue features a collection of research papers and reviews representing an up-to-date state of the art in this growing field of research to broaden our understanding about carbohydrate-active enzymes, their mutants, and their reaction products at the molecular level.Tindara Venuto et al. wrote a paper about alpha2,8-sialyltransferases from ray-finned fish and showed that, in tetrapods, duplicated st8sia genes like st8sia7, st8sia8, and st8sia9 have disappeared while orthologues are maintained in teleosts [1]. They reconstructed the evolutionary history of st8sia genes in fish genomes and by bioinformatics analysis showed changes in the conserved polysialyltransferase domain of the fish sequences possibly accounting for variable enzymatic activities [1].PhNah20A, a β-N-acetylhexosaminidase from the marine bacterium Paraglaciecola hydrolytica S66T, was identified and characterized. By phylogenetic analysis, the authors discovered that PhNah20A is located outside clusters of other studied β-N-acetylhexosaminidases, in a unique position between bacterial and eukaryotic enzymes. PhNah20A is the first characterized member of a distinct subgroup within GH20 β-N-acetylhexosaminidases. The recombinant PhNah20A showed optimum hydrolytic activity on GlcNAc β-1,4 and β-1,3 linkages in chitobiose (GlcNAc)2 and GlcNAc-1,3-β-Gal-1,4-β-Glc (LNT2), the core structure of a human milk oligosaccharide, at pH 6.0 and 50 • C. Interestingly PhNah20A catalyzed the formation of LNT2, the non-reducing trisaccharide β-Gal-1,4-β-Glc-1,1-β-GlcNAc, and in low amounts the β-1,2or β-1,3-linked trisaccharide β-Gal-1,4(β-GlcNAc)-1,x-Glc by a transglycosylation of lactose using 2-methyl-(1,2-dideoxy-α-d-glucopyrano)-oxazoline (NAG-oxazoline) as the donor [2].The production of biofuels from lignocellulosic biomasses is hampered by the saccharification step of the biomasses requiring the concerted action of lignocellulose cellulases and hemicellulases.Zhang et al. characterized the secretome of Trichoderma harzianum EM0925 under induction of lignocellulose cellulases and hemicellulases [3]. Compared with the commercial enzyme preparations, the T. harzianum EM0925 enzyme cocktail presented significantly higher lignocellulolytic enzyme activi...

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confidence: 89%

“…The use of deep eutectic solvents (DES) for the synthesis of alkyl glycosides catalyzed by the thermostable α-amylase from Thermotoga maritima Amy A was investigated by Miranda-Molina et al [10]. While DES containing alcohols, sugars, and amides as hydrogen-bond donors (HBD) as cosolvents performed best, pure DES almost completely deactivated the enzyme.…”

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confidence: 99%

Carbohydrate-Active Enzymes: Structure, Activity, and Reaction Products

Benini¹

2020

IJMS

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“…The enzyme was almost completely deactivated when assayed in a series of pure DES, but as cosolvents, DES containing alcohols, sugars, and amides as hydrogen‐bond donors (HBD) performed best. [146] …”

Section: Organic Synthesis In Dessmentioning

confidence: 99%

“…The enzyme was almost completely deactivated when assayed in a series of pure DES, but as cosolvents, DES containing alcohols, sugars, and amides as hydrogen-bond donors (HBD) performed best. [146] 6.12. Peptide Synthesis DESs have proved to be a good alternative to traditional organic solvents and in many biocatalytic processes, [147] including enzymatic peptide synthesis.…”

Section: Glycosylationsmentioning

confidence: 99%

Deep Eutectic Solvents and Multicomponent Reactions: Two Convergent Items to Green Chemistry Strategies

Calvo‐Flores

Mingorance-Sánchez

2021

ChemistryOpen

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One of the highlights of green chemistry is the development of techniques and procedures with low environmental impact. In the last years, deep eutectic solvents (DES) have become an important alternative to conventional organic solvents. For a period ionic liquids have provoked remarkable interest, but they have been displaced by DES because they show easier preparation methods, lower prices, many of them are biode-gradable and compatible with biological systems. In addition, they show adjustable physicochemical properties, high thermal stability, low volatility and are compatible with water. In this paper is reviewed the state of the art of the use of DES paying special attention to the role of reaction media in organic synthesis.

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“…In that report the authors concluded that the moderate increase in Y (10%) justifies the use of an ionic liquid in terms of practical considerations (productivity and cost). Similarly, in the synthesis of alkyl-glycoside with the α-amylase from Thermotoga maritima the use of deep eutectic solvents (DES) provoked a reduction in enzyme stability and a decrease in enzyme activity, but favored transglycosylation (alcoholysis) over hydrolysis at concentration lower than 10% v/v (Miranda-Molina et al, 2019). In the synthesis of hexyl-β-galactoside with A. oryzae β-galactosidase (Vera et al, 2017a), the addition of 30% (v/v) acetone produced a significant increase in Y, mainly because of a decrease in secondary hydrolysis.…”

Section: Synthesis Of Butyl-β-galactoside In a Ternary Systemmentioning

confidence: 99%

Synthesis of Butyl-β-D-Galactoside in the Ternary System: Acetone/1-Butanol/Aqueous Solution

Ahumada

Arenas

Martínez‐Gómez

et al. 2020

Front. Bioeng. Biotechnol.

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The enzymatic synthesis of short-tailed alkyl glucosides is generally carried out in an aqueous-organic biphasic reaction medium with a rather low fatty alcohol concentration in the aqueous phase (where the synthesis occurs). Thus, hydrolytic reactions have a significant impact on the synthesis performance. Given this background, the use of acetone as cosolvent was studied for the synthesis of butyl-β-galactoside with Aspergillus oryzae β-galactosidase. The liquid-liquid equilibrium of the reaction mixture components (acetone/1-butanol/aqueous solution) was determined and the single-and two-phase regions were defined at 30, 40, and 50 • C. It was observed that the liquidliquid equilibrium of the ternary system acetone/1-butanol/water differs significantly from the one obtained using an aqueous solution (50 mM McIlvaine buffer pH 4.5; 5 g L −1) instead of water. This is mainly because of the salting-out effect of the buffer; nevertheless, the presence of lactose also altered the equilibrium. Having this in mind, the effects of temperature (30 and 50 • C) and reaction mixture composition were assessed. Three general conditions were evaluated: single-phase ternary system (30% acetone), two-phase ternary system (10% acetone) and two-phase binary system (0% acetone). Acetone had a deleterious effect on enzyme stability at 50 • C, leading to low reaction yields. However, no enzyme deactivation was detected at 30 • C. Moreover, a reaction yield of 0.98 mol mol −1 was attained in the 30/50/20% (w/w) mixture of acetone/1-butanol/aqueous solution. This very high yield can be explained by the huge increase in the concentration of 1-butanol and the reduction of water activity. The synthesis was carried out using also the β-galactosidase immobilized in glyoxalagarose and amino-glyoxal-agarose, and by aggregation and crosslinking. In the case of agarose-derived catalysts, two average particle diameters were assessed to evaluate the presence of internal mass transfer limitations. Best yield (0.88 mol mol −1) was obtained with glyoxal-agarose derivatives and the particle size had non-effect on yield. The chemical structure of butyl-β-galactoside was determined by NMR and FT-IR.

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Deep Eutectic Solvents as New Reaction Media to Produce Alkyl-Glycosides Using Alpha-Amylase from Thermotoga maritima

Cited by 12 publications

References 38 publications

Carbohydrate-Active Enzymes: Structure, Activity, and Reaction Products

Carbohydrate-Active Enzymes: Structure, Activity, and Reaction Products

Deep Eutectic Solvents and Multicomponent Reactions: Two Convergent Items to Green Chemistry Strategies

Synthesis of Butyl-β-D-Galactoside in the Ternary System: Acetone/1-Butanol/Aqueous Solution

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