Improvement of Trehalose Production by Immobilized Trehalose Synthase from Thermus thermophilus HB27

Sun, Jing; Wang, Shizeng; Li, Wenna; Li, Ruimin; Chen, Sheng; Ri, Hyon Il; Kim, Tae Mun; Kang, Myong Su; Sun, Lu; Sun, Xinxiao; Yuan, Qipeng

doi:10.3390/molecules23051087

Cited by 9 publications

(6 citation statements)

References 33 publications

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“…Furthermore, after immobilization the reusability, thermal, pH, and operational stability of the enzymes was often increased [128,262,263]. In particular cases, enzyme immobilization even created a more favorable micro-environment for enzyme activity [264] and selectivity [265,266].…”

Section: Reactor Engineering For (Non)-leloir Glycosyltransferasesmentioning

confidence: 99%

“…tank vs. tube/column and the mode of operation: periodic/batch vs. continuous flow. Conventional stirred tank reactors (STR) [259,266,270,271] are still frequently applied, but basket and in particular rotating bed reactors [272] are increasingly used in batch operations. In continuous flow applications, packed-bed (micro)reactors [273] have been most popular, but structural (micro)reactors [274,275], lab-on-a-chip [276], and capillary microreactors are on the rise [277].…”

Section: Reactor Engineering For (Non)-leloir Glycosyltransferasesmentioning

confidence: 99%

“…Different examples of reactors that have been used with glycosyltransferases are shown in Figure 15. Stirred tank reactors are flexible in design and operation conditions, but often require high operation costs and vary in the product quality per batch [128,259,266,270,271]. Microchannel reactors feature flow-through channels of micrometric sizes that contain the enzyme immobilized on their wall surface [277].…”

Section: Reactor Engineering For (Non)-leloir Glycosyltransferasesmentioning

confidence: 99%

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Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Mestrom

Przypis

Kowalczykiewicz

et al. 2019

IJMS

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Enzymes are nature's catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio-and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.hydroxynitrile lyases catalyzed the enzymatic hydrolysis of the glycoside amygdalin [3]. Moving almost two centuries forward, the largest volumetric biocatalytic industrial process is the application of glucose isomerase for the production of high fructose syrup for food and drink applications, producing fructose from glucose at 10 7 tons per year [4]. The secret of the success of enzymes in the production or treatment of carbohydrates and glycosides is their exquisite stereo-and regioselectivity. The excellent selectivity of enzymes is required due to the diversity of structural features of carbohydrates [5], comprising d-and l-epimers, ring size, anomeric configuration, linkages, branching, and oxidation state(s). Since drug targets often exhibit specificity for all of these structural features, the production process should not contain any side-products to prevent undesired side-effects [6].The challenge in the synthesis of carbohydrates is their wide variety of functionalities and stereochemistry ( Figure 1). (Poly)hydroxyaldehydes containing a terminal aldehyde are referred to as aldoses and (poly)hydroxyketones are defined as ketoses. In aqueous solutions, monosaccharides form equilibrium mixtures of linear open-chain and ring-closed 5-or 6-membered furanoses or pyranoses, respectively. For aldoses, the asymmetric ring forms at C-1. For ketoses, it closes at C-2 as an axial (α) or equatorial (β) hemiacetal or hemiketal, respectively (commonly defined as the anomeric center). A glycosidic linkage is a covalent O-, S-, N-, or C-bond connecting a monosaccharide to another residue resulting in a glycoside, while glucoside is specific for a glucose moiety. The equatorial or axial position of the glycosidic bond is referred to as α-(axial) or β-linkage (equatorial). The number of carbohydrates linked via glycosidic bonds can be subdivided into oligosaccharides with two to ten linked carbohydrates, while polysaccharides (glycans) contain more than ten glycosidic bonds. A glycan either con...

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Section: Reactor Engineering For (Non)-leloir Glycosyltransferasesmentioning

confidence: 99%

Section: Reactor Engineering For (Non)-leloir Glycosyltransferasesmentioning

confidence: 99%

Section: Reactor Engineering For (Non)-leloir Glycosyltransferasesmentioning

confidence: 99%

See 1 more Smart Citation

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Mestrom

Przypis

Kowalczykiewicz

et al. 2019

IJMS

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“…One of the primary advantages of the utilization of immobilization enzyme techniques is the potential for reuse of the enzyme [55,56,57,58]. The operational stability of co-immobilized tri-enzymes is illustrated in Figure 7.…”

Section: Resultsmentioning

confidence: 99%

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

Shi

et al. 2019

Molecules

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Acting as a “green” manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address this, galactose oxidase, catalase, and horseradish peroxidase were co-immobilized into Cu3(PO4)2 nanoflowers in this study. The resulting co-immobilized tri-enzymes possessed better tolerance towards the oxidative damage caused by hydroxymethylfurfural at high concentrations, as compared to free tri-enzymes. Moreover, the 2,5-diformylfuran yield of co-immobilized tri-enzymes (95.7 ± 2.7%) was 1.06 times higher than that of separately immobilized enzymes (90.4 ± 1.9%). This result could be attributed to the boosted protective effect provided by catalase to the activity of galactose oxidase, owing to the physical proximity between them on the same support. After 30 recycles, co-immobilized tri-enzymes still achieves 86% of the initial yield. Moreover, co-immobilized tri-enzymes show enhanced thermal stability compared with free tri-enzymes. This work paves the way for the production of 2,5-diformylfuran from hydroxymethylfurfural via co-immobilized tri-enzymes.

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“…16) is used to produce trehalose from maltose. This one-step process, through intermolecular rearrangement mechanism, is considered advantageous for its simplicity and cost effectiveness [5]. Most studies on trehalose production by TreS have focused on the use of recombinant enzymes, and several TreS genes have been cloned from different bacterial strains and heterologously expressed in Escherichia coli [4].…”

Section: Introductionmentioning

confidence: 99%

Integrated Whole-Cell Biocatalysis for Trehalose Production from Maltose Using Permeabilized Pseudomonas monteilii Cells and Bioremoval of Byproduct

Trakarnpaiboon

Champreda

2022

J. Microbiol. Biotechnol.

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Trehalose is a non-conventional sugar with potent applications in the food, healthcare and biopharma industries. In this study, trehalose was synthesized from maltose using whole-cell Pseudomonas monteilii TBRC 1196 producing trehalose synthase (TreS) as the biocatalyst. The reaction condition was optimized using 1% Triton X-100 permeabilized cells. According to our central composite design (CCD) experiment, the optimal process was achieved at 35 o C and pH 8.0 for 24 h, resulting in the maximum trehalose yield of 51.60 g/g after 12 h using an initial cell loading of 94 g/l. Scale-up production in a lab-scale bioreactor led to the final trehalose concentration of 51.91 g/l with a yield of 51.60 g/g and productivity of 4.37 g/l/h together with 8.24 g/l glucose as a byproduct. A one-pot process integrating trehalose production and byproduct bioremoval showed 53.35% trehalose yield from 107.4 g/l after 15 h by permeabilized P. moteilii cells. The residual maltose and glucose were subsequently removed by Saccharomyces cerevisiae TBRC 12153, resulting in trehalose recovery of 99.23% with 24.85 g/l ethanol obtained as a co-product. The present work provides an integrated alternative process for trehalose production from maltose syrup in bio-industry.

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Improvement of Trehalose Production by Immobilized Trehalose Synthase from Thermus thermophilus HB27

Cited by 9 publications

References 33 publications

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran

Integrated Whole-Cell Biocatalysis for Trehalose Production from Maltose Using Permeabilized Pseudomonas monteilii Cells and Bioremoval of Byproduct

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