2019
DOI: 10.1016/j.jsb.2018.12.002
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Structural and functional characterization of a family GH53 β-1,4-galactanase from Bacteroides thetaiotaomicron that facilitates degradation of prebiotic galactooligosaccharides

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Cited by 30 publications
(19 citation statements)
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“…In B. breve UCC2003 (and in Bacteroides thetaiotaomicron ), it was demonstrated that efficient GOS utilization, particularly of higher DP compounds, correlated with the expression of a membrane-associated GH53 endo-galactanase (GalA). 38,39 The gene encoding this enzyme was part of a galactan utilization operon encoding also an ABC transporter (GalCDE) and an intracellular GH42 β-galactosidase (GalG). Another GOS utilization system was identified in B. lactis Bl-04 which employs the LacS/LacZ pathway and in addition the GosDEC (ABC transporter) with GosG (intracellular GH42 β-galactosidase).…”
Section: Resultsmentioning
confidence: 99%
“…In B. breve UCC2003 (and in Bacteroides thetaiotaomicron ), it was demonstrated that efficient GOS utilization, particularly of higher DP compounds, correlated with the expression of a membrane-associated GH53 endo-galactanase (GalA). 38,39 The gene encoding this enzyme was part of a galactan utilization operon encoding also an ABC transporter (GalCDE) and an intracellular GH42 β-galactosidase (GalG). Another GOS utilization system was identified in B. lactis Bl-04 which employs the LacS/LacZ pathway and in addition the GosDEC (ABC transporter) with GosG (intracellular GH42 β-galactosidase).…”
Section: Resultsmentioning
confidence: 99%
“…Another bacterial galactanase from Geobacillus stearothermophilus produces mostly galactotetraose from galactan, and was also shown not to degrade galactotriose to smaller oligosaccharides (Tabachnikov & Shoham, 2013), while the galactanase from Bifidobacterium longum was reported to produce galactotriose by a processive mechanism (Hinz et al, 2005). However, in a more recent study a bacterial galactanase from Bacteroides thetaiotaomicron showed the ability to degrade potato galactan to galactobiose (77%) and galactose (23%) (van Bueren et al, 2017;Bö ger et al, 2019), thus showing that bacteria possess galactanases with diverse degradation patterns. Structural comparison suggests that the differences in product profile between the fungal and BlGal galactanases and the inability of the latter to degrade galatotriose is owing to the fact that BlGal has a more extended glycone substrate-binding site and thus can bind small oligosaccharides nonproductively (Ryttersgaard et al, 2004;Torpenholt et al, 2011).…”
Section: Issn 2053-230xmentioning
confidence: 99%
“…In recent years, galactanases have increasingly been characterized as part of the galactan/galactose-utilization systems of human gut bacteria (see, for example, Hinz et al, 2005;van Bueren et al, 2017;Bö ger et al, 2019), the pivotal role of which in human health is increasingly being recognized. Simultaneously, galactose-containing oligosaccharides are increasingly being recognized as prebiotic agents that are able to promote the 'good' bacteria in the gut.…”
Section: Subsite à2mentioning
confidence: 99%
“…To date, four fungal endo-β-1,4-galactanases from the following sources have been structurally and biochemically characterized: Thermothelomyces thermophila (also known as Myceliophthora thermophila ) (MtGal, GenBank ID AAE73520.1, PDB IDs: 1HJS, 1HJU) [ 16 ], Humicola insolens (HiGal, GenBank ID AAN99815.1, PDB ID: 1HJQ) [ 16 ], Aspergillus aculeatus KSM 510 (AaGal, GenBank ID AAA32692.1, PDB IDs: 1FHL, 1FOB) [ 17 ] and the highly related Aspergillus nidulans FGSC A4 (EnGal, GenBank ID ABF50874.1, PDB ID: 4BF7) [ 18 ]. Two bacterial endo-β-1,4-galactanase have also been structurally characterized, one from Bacillus licheniformis (BlGal, GenBank ID AAO31370.1, PDB IDs: 1R8L, 1UR0, 1UR4, 2CCR, 2GFT, 2J74) [ 19 , 20 ], and one from Bacteroides thetaiotaomicron (BtGal, GenBank ID AAO79773.1, PDB IDs: 6GP5, 6GPA) [ 21 ]. The fungal galactanases mentioned above as well as BtGal can degrade the galactan substrate down to galactobiose [ 15 , 20 , 21 ].…”
Section: Introductionmentioning
confidence: 99%
“…Two bacterial endo-β-1,4-galactanase have also been structurally characterized, one from Bacillus licheniformis (BlGal, GenBank ID AAO31370.1, PDB IDs: 1R8L, 1UR0, 1UR4, 2CCR, 2GFT, 2J74) [ 19 , 20 ], and one from Bacteroides thetaiotaomicron (BtGal, GenBank ID AAO79773.1, PDB IDs: 6GP5, 6GPA) [ 21 ]. The fungal galactanases mentioned above as well as BtGal can degrade the galactan substrate down to galactobiose [ 15 , 20 , 21 ]. In addition, some fungal galactanases can carry out trans-glycosylation, unlike BlGal which neither degrades galactotriose nor performs trans-glycosylation [ 20 , 22 ].…”
Section: Introductionmentioning
confidence: 99%