Functional and biotechnological insights into diglycosidases*

Mazzaferro, Laura S.; Breccia, Javier D.

doi:10.3109/10242422.2011.594882

Cited by 31 publications

(21 citation statements)

References 51 publications

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“…Deglycosylation of these compounds most often involves the sequential action of two β-glycosidases in contrast to the one-step hydrolytic release of the disaccharide moiety from the aglycone by β-diglycosidases [55]. The characterized enzymes are a hesperidin 6-O-α-L-rhamnosyl-β-glucosidase (EC 3.2.1.168) from Stilbella fimetaria from which a partial sequence has been obtained [56] and a reported β-primeverosidase (EC 3.2.1.149) from Penicillium multicolor TS-5 [57].…”

Section: Resultsmentioning

confidence: 99%

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

et al. 2012

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BackgroundThe large Glycoside Hydrolase family 5 (GH5) groups together a wide range of enzymes acting on β-linked oligo- and polysaccharides, and glycoconjugates from a large spectrum of organisms. The long and complex evolution of this family of enzymes and its broad sequence diversity limits functional prediction. With the objective of improving the differentiation of enzyme specificities in a knowledge-based context, and to obtain new evolutionary insights, we present here a new, robust subfamily classification of family GH5.ResultsAbout 80% of the current sequences were assigned into 51 subfamilies in a global analysis of all publicly available GH5 sequences and associated biochemical data. Examination of subfamilies with catalytically-active members revealed that one third are monospecific (containing a single enzyme activity), although new functions may be discovered with biochemical characterization in the future. Furthermore, twenty subfamilies presently have no characterization whatsoever and many others have only limited structural and biochemical data. Mapping of functional knowledge onto the GH5 phylogenetic tree revealed that the sequence space of this historical and industrially important family is far from well dispersed, highlighting targets in need of further study. The analysis also uncovered a number of GH5 proteins which have lost their catalytic machinery, indicating evolution towards novel functions.ConclusionOverall, the subfamily division of GH5 provides an actively curated resource for large-scale protein sequence annotation for glycogenomics; the subfamily assignments are openly accessible via the Carbohydrate-Active Enzyme database at http://www.cazy.org/GH5.html.

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Section: Resultsmentioning

confidence: 99%

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

et al. 2012

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“…[6,19] In order to gain some insight into the structural diversity of diglycosidases, we performed a phy- logenetic analysis of the rutinosidase with 6 known diglycosidases from plants and fungi, 9 GH-5-subfamily-23 sequences in the CAZy database, and the 15 putative fungal glycosidases, which best matched to the rutinosidase-encoding sequence in a BLASTP search (Supporting Information, Figure S26). The search revealed that the cloned rutinosidase most closely resembled 4 glycosidases from Aspergillus strains with protein sequence identities of 69-99%.…”

Section: Expression and Purification Of Recombinant Rutinosidasementioning

confidence: 99%

“…[1][2][3][4][5] This highlights the potential of these enzymes, which can often catalyze both hydrolytic and transglycosylation reactions, for agricultural, biomedical and food chemistry applications. [6] Rutin ( plants (mainly buckwheat and common rue, and also tobacco) and fruits, such as apple, tomato, grape and citrus. [6] Waste products of the agro-and fruit juiceproducing industry contain large amounts of rutin and hesperidin, which represent inexpensive starting materials for the synthesis of rutinosylated glycoconjugates with potentially interesting biological and pharmacological activities and for the preparation of rutinose.…”

mentioning

confidence: 99%

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

et al. 2014

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Abstract:We report the first heterologous production of a fungal rutinosidase (6-O-a-l-rhamnopyranosyl-b-d-glucopyranosidase) in Pichia pastoris. The recombinant rutinosidase was purified from the culture medium to apparent homogeneity and biochemically characterized. The enzyme reacts with rutin and cleaves the glycosidic linkage between the disaccharide rutinose and the aglycone. Furthermore, it exhibits high transglycosylation activity, transferring rutinose from rutin as a glycosyl donor onto various alcohols and phenols. The utility of the recombinant rutinosidase was demonstrated by its use for the synthesis of a broad spectrum of rutinosides of primary (saturated and unsaturated), secondary, acyclic and phenolic alcohols as well as for the preparation of free rutinose. Moreover, the a-l-rhamnosidase-catalyzed synthesis of a chromogenic substrate for a rutinosidase assay -para-nitrophenyl b-rutinoside -is described.

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“…[15] It is an important phytochemical contained in various plants and fruits (buckwheat, tobacco, apples, tomatoes, citrus, and grapes), whichw as nameda fter one of its primary natural sources, the common rue Ruta graveolens. [16] Rutin is now produced as am ultiton commodityc hemical from the Brazilian treeF avad 'anta (Dimorphandra mollis); it also accumulates as aw aste byproduct in different manufacturing processes (e.g.,t he productiono ff ruit juices). Rutin has GRAS status (www.hc-sc.gc.ca)a nd it is used in plethora of nutraceuticals and pharmaceutical preparation as ac apillary/blood vessel protectanta nd as an antiviral agent.…”

Section: Introductionmentioning

confidence: 99%

A Sustainable One‐Pot, Two‐Enzyme Synthesis of Naturally Occurring Arylalkyl Glucosides

et al. 2017

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A sustainable, convenient, scalable, one-pot, two-enzyme method for the glucosylation of arylalkyl alcohols was developed. The reaction scheme is based on a transrutinosylation catalyzed by a rutinosidase from A. niger using the cheap commercially available natural flavonoid rutin as glycosyl donor, followed by selective "trimming" of the rutinoside unit catalyzed by a rhamnosidase from A. terreus. The process was validated with the syntheses of several natural bioactive glucosides, which could be isolated in up to 75 % yield without silica-gel chromatography.

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Functional and biotechnological insights into diglycosidases*

Cited by 31 publications

References 51 publications

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)

α‐L‐Rhamnosyl‐β‐D‐glucosidase (Rutinosidase) from Aspergillus niger: Characterization and Synthetic Potential of a Novel Diglycosidase

A Sustainable One‐Pot, Two‐Enzyme Synthesis of Naturally Occurring Arylalkyl Glucosides

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