Raffinose family oligosaccharide utilisation by probiotic bacteria: insight into substrate recognition, molecular architecture and diversity of GH36 α-galactosidases

Hachem, Maher Abou; Fredslund, Folmer; Andersen, Joakim Mark; Larsen, R. Jonsgaard; Majumder, Arun Lahiri; Ejby, Morten; Zanten, Gabriella Christina van; Lahtinen, Sampo J.; Barrangou, Rodolphe; Klaenhammer, Todd R.; Jacobsen, Susanne; Coutinho, Pedro M.; Leggio, Leila Lo; Svensson, Birte

doi:10.3109/10242422.2012.674717

Cited by 15 publications

(15 citation statements)

References 47 publications

(62 reference statements)

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“…cazy.org) [1]. GH27 and GH36 a-galactosidases belong to clan D and share a common (a/b) 8 fold [2]. These families contain cloned and some structurally characterized a-galactosidases from various prokaryotic and eukaryotic organisms isolated from soil [3][4][5], thermal springs [6,7] and the mammalian gut [8][9][10].…”

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confidence: 99%

“…These families contain cloned and some structurally characterized α‐galactosidases from various prokaryotic and eukaryotic organisms isolated from soil , thermal springs and the mammalian gut . GH27 α‐galactosidases are active on both terminal and/or internal galactosidic linkages from polysaccharides like galactomannan and galactosylated oligosaccharides , while GH36 α‐galactosidases are mainly active on terminal α‐galactosidic linkages in raffinose family oligosaccharides (RFOS) such as raffinose and melibiose . Previous studies suggest that unique structural/sequence motifs and the oligomeric state of the enzymes impart the substrate preferences (terminal versus internal galactose linkages) in GH27 and GH36 α‐galactosidases.…”

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confidence: 99%

“…Tetrameric α‐galactosidases from both the families have a narrow active site cleft and preferably hydrolyse only terminal α‐galactosidic linkages present in RFOS . Recent phylogenetic analysis of GH36 enzymes clusters these sequences into four distinct subgroups . The GH36 subgroup I is by far the largest group of the family and contains mainly tetrameric α‐galactosidases active on terminal α‐galactosidic linkages.…”

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confidence: 99%

“…The GH36 subgroup I is by far the largest group of the family and contains mainly tetrameric α‐galactosidases active on terminal α‐galactosidic linkages. The majority of biochemically and structurally characterized subgroup I α‐galactosidases are from gut bacteria, such as Bifidobacterium and Lactobacillus species, and are involved in RFOS utilization .…”

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A β‐mannan utilization locus in Bacteroides ovatus involves a GH36 α‐galactosidase active on galactomannans

et al. 2016

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The Bacova_02091 gene in the β‐mannan utilization locus of Bacteroides ovatus encodes a family GH36 α‐galactosidase (BoGal36A), transcriptionally upregulated during growth on galactomannan. Characterization of recombinant BoGal36A reveals unique properties compared to other GH36 α‐galactosidases, which preferentially hydrolyse terminal α‐galactose in raffinose family oligosaccharides. BoGal36A prefers hydrolysing internal galactose substitutions from intact and depolymerized galactomannan. BoGal36A efficiently releases (> 90%) galactose from guar and locust bean galactomannans, resulting in precipitation of the polysaccharides. As compared to other GH36 structures, the BoGal36A 3D model displays a loop deletion, resulting in a wider active site cleft which likely can accommodate a galactose‐substituted polymannose backbone.

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confidence: 99%

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confidence: 99%

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confidence: 99%

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A β‐mannan utilization locus in Bacteroides ovatus involves a GH36 α‐galactosidase active on galactomannans

et al. 2016

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“…(Astronomo and Burton 2010). Furthermore, α-1,6 linked galactooligosaccharides have been recognized for their prebiotic properties (Andersen et al 2013;Cervera-Tison et al 2012;Hachem et al 2012;Nakai et al 2010;Wang et al 2014). However, their use is hindered by their poor availability: unlike for proteins and nucleic acids, there is no general synthetic route for oligosaccharides and, despite the considerable development of efficient methods in this field (Wang et al 2007;Zhu and Schmidt 2009), the assembly of oligosaccharides remains a substantial challenge.…”

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Semi-rational approach for converting a GH36 α-glycosidase into an α-transglycosidase

et al. 2014

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A large number of retaining glycosidases catalyze both hydrolysis and transglycosylation reactions. In order to use them as catalysts for oligosaccharide synthesis, the balance between these two competing reactions has to be shifted toward transglycosylation. We previously designed a semi-rational approach to convert the Thermus thermophilus β-glycosidases into transglycosidases by mutating highly conserved residues located around the -1 subsite. In an attempt to verify that this strategy could be a generic approach to turn glycosidases into transglycosidases, Geobacillus stearothermophilus α-galactosidase (AgaB) was selected in order to obtain α-transgalactosidases. This is of particular interest as, to date, there are no efficient α-galactosynthases, despite the considerable importance of α-galactooligosaccharides. Thus, by site-directed mutagenesis on 14 AgaB residues, 26 single mutants and 22 double mutants were created and screened, of which 11 single mutants and 6 double mutants exhibited improved synthetic activity, producing 4-nitrophenyl α-d-galactopyranosyl-(1,6)-α-d-galactopyranoside in 26-57% yields against only 22% when native AgaB was used. It is interesting to note that the best variant was obtained by mutating a second-shell residue, with no direct interaction with the substrate or a catalytic amino acid. As this approach has proved to be efficient with both α- and β-glycosidases, it is a promising route to convert retaining glycosidases into transglycosidases.

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Current studies on physiological functions and biological production of lactosucrose

Chen

Wang

et al. 2013

Appl Microbiol Biotechnol

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Lactosucrose (O-β-D-galactopyranosyl-(1,4)-O-α-D-glucopyranosyl-(1,2)-β-D-fructofuranoside) is a trisaccharide formed from lactose and sucrose by enzymatic transglycosylation. This rare trisaccharide is a kind of indigestible carbohydrate, has good prebiotic effect, and promotes intestinal mineral absorption. It has been used as a functional ingredient in a range of food products which are approved as foods for specified health uses in Japan. Using lactose and sucrose as substrates, lactosucrose can be produced through transfructosylation by β-fructofuranosidase from Arthrobacter sp. K-1 or a range of levansucrases, or through transgalactosylation by β-galactosidase from Bacillus circulans. This article presented a review of recent studies on the physiological functions of lactosucrose and the biological production from lactose and sucrose by different enzymes.

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Raffinose family oligosaccharide utilisation by probiotic bacteria: insight into substrate recognition, molecular architecture and diversity of GH36 α-galactosidases

Cited by 15 publications

References 47 publications

A β‐mannan utilization locus in Bacteroides ovatus involves a GH36 α‐galactosidase active on galactomannans

A β‐mannan utilization locus in Bacteroides ovatus involves a GH36 α‐galactosidase active on galactomannans

Semi-rational approach for converting a GH36 α-glycosidase into an α-transglycosidase

Current studies on physiological functions and biological production of lactosucrose

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