Hooked on α-<scp>d</scp>-galactosidases: from biomedicine to enzymatic synthesis

Bakunina, I. Yu.; Balabanova, Larissa; Pennacchio, Anna; Trincone, Antonio

doi:10.3109/07388551.2014.949618

Cited by 16 publications

(13 citation statements)

References 186 publications

(167 reference statements)

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“…The interest of synthetic chemists for the production of α-galactosides has been present since 1970s, and it has been traced in the literature as being generally prompted by the discovery of the biological functions of these molecules. From an in-depth analysis recently published [ 66 ], a direct influence of substrate availability in enzyme discovery has been recognized. In fact, α-1,6-galactosides are more common and easily used in the investigation of substrate specificity with respect to rarer α-1,3- and α-1,4-regioisomers that have been obtained by somewhat troublesome synthetic strategies.…”

Section: Galactosidasementioning

confidence: 99%

“…A detailed and critical analysis of the literature for the production of α-galactosides with more tabular-based cross-comparisons has been already published [ 66 ] and excluded from this review, as well as the transfer of the anomer sugar β-galactose, operated by β-galactosidases, which is a much more common reaction with respect to α-galactosyl transfer. However, a study collecting different enzymes for the production of glycosylated oligosaccharides that recently appeared [ 73 ] is important.…”

Section: Galactosidasementioning

confidence: 99%

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Uncommon Glycosidases for the Enzymatic Preparation of Glycosides

Trincone

2015

Biomolecules

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Most of the reports in literature dedicated to the use of glycosyl hydrolases for the preparation of glycosides are about gluco- (α- and β-form) and galacto-sidase (β-form), reflecting the high-availability of both anomers of glucosides and of β-galactosides and their wide-ranging applications. Hence, the idea of this review was to analyze the literature focusing on hardly-mentioned natural and engineered glycosyl hydrolases. Their performances in the synthetic mode and natural hydrolytic potential are examined. Both the choice of articles and their discussion are from a biomolecular and a biotechnological perspective of the biocatalytic process, shedding light on new applicative ideas and on the assortment of biomolecular diversity. The hope is to elicit new interest for the development of biocatalysis and to gather attention of biocatalyst practitioners for glycosynthesis.

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Section: Galactosidasementioning

confidence: 99%

Section: Galactosidasementioning

confidence: 99%

Uncommon Glycosidases for the Enzymatic Preparation of Glycosides

Trincone

2015

Biomolecules

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“…Thus, many enzymatic biosensors have been developed to determine the concentration of one specific component inside a very complex mixture (e.g., glucose in blood [30,31]). Another application of enzymes can be found in the field of medicine, where they can be supplemented in order to supply some endogenous enzyme deficiencies or to degrade some target deleterious compounds [32,33]. In this case, enzyme specificity and selectivity are both required, as only the target compound must be degraded, without generating any toxic side-product.…”

Section: Introductionmentioning

confidence: 99%

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

et al. 2019

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Dextran aldehyde (dexOx), resulting from the periodate oxidative cleavage of 1,2-diol moiety inside dextran, is a polymer that is very useful in many areas, including as a macromolecular carrier for drug delivery and other biomedical applications. In particular, it has been widely used for chemical engineering of enzymes, with the aim of designing better biocatalysts that possess improved catalytic properties, making them more stable and/or active for different catalytic reactions. This polymer possesses a very flexible hydrophilic structure, which becomes inert after chemical reduction; therefore, dexOx comes to be highly versatile in a biocatalyst design. This paper presents an overview of the multiple applications of dexOx in applied biocatalysis, e.g., to modulate the adsorption of biomolecules on carrier surfaces in affinity chromatography and biosensors design, to serve as a spacer arm between a ligand and the support in biomacromolecule immobilization procedures or to generate artificial microenvironments around the enzyme molecules or to stabilize multimeric enzymes by intersubunit crosslinking, among many other applications.

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“…The GH 27 and GH 36 family members are classical retaining glycoside hydrolyses in accordance with Koshland’s classification [ 3 ]. These enzymes catalyze the hydrolysis of O-glycosidic bonds by a double displacement mechanism through the galactosyl-enzyme covalent intermediate, as well as the transglycosylation reaction under the specific conditions [ 4 ].…”

Section: Introductionmentioning

confidence: 99%

Characterization of Properties and Transglycosylation Abilities of Recombinant α-Galactosidase from Cold-Adapted Marine Bacterium Pseudoalteromonas KMM 701 and Its C494N and D451A Mutants

et al. 2018

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A novel wild-type recombinant cold-active α-d-galactosidase (α-PsGal) from the cold-adapted marine bacterium Pseudoalteromonas sp. KMM 701, and its mutants D451A and C494N, were studied in terms of their structural, physicochemical, and catalytic properties. Homology models of the three-dimensional α-PsGal structure, its active center, and complexes with D-galactose were constructed for identification of functionally important amino acid residues in the active site of the enzyme, using the crystal structure of the α-galactosidase from Lactobacillus acidophilus as a template. The circular dichroism spectra of the wild α-PsGal and mutant C494N were approximately identical. The C494N mutation decreased the efficiency of retaining the affinity of the enzyme to standard p-nitrophenyl-α-galactopiranoside (pNP-α-Gal). Thin-layer chromatography, matrix-assisted laser desorption/ionization mass spectrometry, and nuclear magnetic resonance spectroscopy methods were used to identify transglycosylation products in reaction mixtures. α-PsGal possessed a narrow acceptor specificity. Fructose, xylose, fucose, and glucose were inactive as acceptors in the transglycosylation reaction. α-PsGal synthesized -α(1→6)- and -α(1→4)-linked galactobiosides from melibiose as well as -α(1→6)- and -α(1→3)-linked p-nitrophenyl-digalactosides (Gal2-pNP) from pNP-α-Gal. The D451A mutation in the active center completely inactivated the enzyme. However, the substitution of C494N discontinued the Gal-α(1→3)-Gal-pNP synthesis and increased the Gal-α(1→4)-Gal yield compared to Gal-α(1→6)-Gal-pNP.

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Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

Cited by 16 publications

References 186 publications

Uncommon Glycosidases for the Enzymatic Preparation of Glycosides

Uncommon Glycosidases for the Enzymatic Preparation of Glycosides

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

Characterization of Properties and Transglycosylation Abilities of Recombinant α-Galactosidase from Cold-Adapted Marine Bacterium Pseudoalteromonas KMM 701 and Its C494N and D451A Mutants

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