GH36 α-galactosidase from Lactobacillus plantarum WCFS1 synthesize Gal-α-1,6 linked prebiotic α-galactooligosaccharide by transglycosylation

Panwar, Deepesh; Shubhashini, A.; Chaudhari, Sachin Rama; Prashanth, K. V. Harish; Kapoor, M.

doi:10.1016/j.ijbiomac.2019.12.032

Cited by 16 publications

(8 citation statements)

References 42 publications

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“…24,25 A recent study has addressed the biochemical characterization and carbohydrate specificity of MelA, a cold-active α-galactosidase from L. plantarum WCFS1 belonging to the glycoside hydrolase (GH) family 36, demonstrating a unique preference for the transfer of galactosyl residues from melibiose, RFOS, or nonfructosylated α-GOS to the C6-hydroxyl group of galactose units to elongate the chain of the acceptor substrates. 17 Despite this great diversity in accommodating specific α-GOS compounds acting both as donor and acceptor substrates, studies about acceptor specificity of MelA from L. plantarum WCFS1 using melibiose as a galactosyl donor and a variety of potentially suitable acceptors are scarce 18 and their resistance to intestinal digestion and potential prebiotic effect have never been studied. This approach could be a promising strategy for obtaining novel tailored HOS of high interest and added value for potential applications in the food and/or nutraceutical sectors.…”

Section: Introductionmentioning

confidence: 99%

“…α- d -Galactosidases are widely distributed among fungi, , plants, , animals, and bacteria strains. , Some studies have addressed the use of these α- d -galactosidases to hydrolyze the raffinose family of oligosaccharides (RFOS), such as raffinose, stachyose, or verbascose, to mitigate flatulence, while others have been focused on the synthesis of α-GOS. ,,, Remarkably, α-galactosidases have also been employed, using a variety of acceptors and donors, to produce hetero-oligosaccharides (HOS) with potentially extended functionality as compared to conventional α-GOS. Several authors reported the use of melibiose, raffinose, or p -nitrophenyl-α- d -galactopyranoside (acting as donors) along with different monosaccharides (galactose, glucose, and fructose), disaccharides (lactose, maltose, isomaltose, and cellobiose), or sugar alcohols (sorbitol and mannitol) to investigate the acceptor specificity of different α- d -galactosidases.…”

Section: Introductionmentioning

confidence: 99%

“…Despite this great diversity in accommodating specific α-GOS compounds acting both as donor and acceptor substrates, studies about acceptor specificity of MelA from L. plantarum WCFS1 using melibiose as a galactosyl donor and a variety of potentially suitable acceptors are scarce and their resistance to intestinal digestion and potential prebiotic effect have never been studied. This approach could be a promising strategy for obtaining novel tailored HOS of high interest and added value for potential applications in the food and/or nutraceutical sectors.…”

Section: Introductionmentioning

confidence: 99%

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Biosynthesis of Nondigestible Galactose-Containing Hetero-oligosaccharides by Lactobacillus plantarum WCFS1 MelA α-Galactosidase

Delgado-Fernández

Rivas

Múñoz

et al. 2021

J. Agric. Food Chem.

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This work describes the high capacity of MelA α-galactosidase from Lactobacillus plantarum WCFS1 to transfer galactosyl residues from melibiose to the C6-hydroxyl group of disaccharideacceptors with β-linkages (lactulose, lactose and cellobiose) or α-linkages (isomaltulose and isomaltose) to produce novel galactose-containing hetero-oligosaccharides (HOS). A comprehensive NMR characterization of the transfer products derived from melibiose:lactulose reaction mixtures revealed the biosynthesis of αD-galactopyranosyl-(1→6)-β-D-galactopyranosyl-(1→4)-β-D-fructose as the main component, as well as the presence of α-D-galactopyranosyl-(1→3)-β-D-galactopyranosyl-(1→4)-β-D-fructose and αD-galactopyranosyl-(1→6)-αDgalactopyranosyl-(1→6)-β-D-galactopyranosyl-(1→4)-β-D-fructose. Melibiose-derived αgalactooligosaccharides (α-GOS), manninotriose and verbascotetraose, were also simultaneously synthesized. An in vitro assessment of the intestinal digestibility of the novel biosynthesized HOS revealed a high resistance of α-galactosides derived from lactulose, lactose, cellobiose and isomaltulose. According to the evidence gathered for conventional α-GOS and certain disaccharides used as acceptors in this work, these novel non-digestible α-galactosides could be potential candidates to selectively modulate the gut microbiota composition, among other applications, such as low-calorie food ingredients.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Biosynthesis of Nondigestible Galactose-Containing Hetero-oligosaccharides by Lactobacillus plantarum WCFS1 MelA α-Galactosidase

Delgado-Fernández

Rivas

Múñoz

et al. 2021

J. Agric. Food Chem.

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“…Additionally, α-galactosidases, which act as hydrolases in nature, can be used in the food industry, such as the hydrolysis of galactosyl residues from raffinose to improve the crystallization of sucrose [ 5 ]. Studies conducted over the years have shown that α-galactosidases can mediate transglycosylation to produce a series of important compounds [ 6 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of a Thermostable GH36 α-Galactosidase from Anoxybacillus vitaminiphilus WMF1 and Its Application in Synthesizing Isofloridoside by Reverse Hydrolysis

Wang

Cao

Chen

et al. 2021

IJMS

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An α-galactosidase-producing strain named Anoxybacillus vitaminiphilus WMF1, which catalyzed the reverse hydrolysis of d-galactose and glycerol to produce isofloridoside, was isolated from soil. The α-galactosidase (galV) gene was cloned and expressed in Escherichia coli. The galV was classified into the GH36 family with a molecular mass of 80 kDa. The optimum pH and temperature of galV was pH 7.5 and 60 °C, respectively, and it was highly stable at alkaline pH (6.0–9.0) and temperature below 65 °C. The specificity for p-nitrophenyl α-d-galactopyranoside was 70 U/mg, much higher than that for raffinose and stachyose. Among the metals and reagents tested, galV showed tolerance in the presence of various organic solvents. The kinetic parameters of the enzyme towards p-nitrophenyl α-d-galactopyranoside were obtained as Km (0.12 mM), Vmax (1.10 × 10−3 mM s−1), and Kcat/Km (763.92 mM−1 s−1). During the reaction of reverse hydrolysis, the enzyme exhibited high specificity towards the glycosyl donor galactose and acceptors glycerol, ethanol and ethylene glycol. Finally, the isofloridoside was synthesized using galactose as the donor and glycerol as the acceptor with a 26.6% conversion rate of galactose. This study indicated that galV might provide a potential enzyme source in producing isofloridoside because of its high thermal stability and activity.

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“…However, α -galactosidase with transglycosylation activity from lactobacilli was rarely reported. The recently reported α -galactosidase with transglycosylation activity was from Lactobacillus plantarum WCFS1 [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Cloning and expression of a novel α-galactosidase from Lactobacillus amylolyticus L6 with hydrolytic and transgalactosyl properties

et al. 2020

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Lactobacillus amylolyticus L6, a gram-positive amylolytic bacterium isolated from naturally fermented tofu whey (NFTW), was able to hydrolyze raffinose and stachyose for the production of α -galactosidase. The cell-free extract of L . amylolyticus L6 was found to exhibit glycosyltransferase activity to synthesize α-galacto-oligosaccharides (GOS) with melibiose as substrate. The coding genes of α -galactosidase were identified in the genome of L . amylolyticus L6. The α-galactosidase (AglB) was placed into GH36 family by amino acid sequence alignments with other α-galactosidases from lactobacilli. The optimal reaction conditions of pH and temperature for AglB were pH 6.0 and 37°C, respectively. Besides, potassium ion was found to improve the activity of AglB while divalent mercury ion, copper ion and zinc ion displayed different degrees of inhibition effect. Under the optimum reaction condition, AglB could catalyze the synthesis of GOS with degree of polymerization (DP) ≥5 by using 300 mM melibiose concentration as substrate. The maximum yield of GOS with (DP) ≥3 could reach 31.56% (w/w). Transgalactosyl properties made AglB a potential candidate for application in the production of GOS.

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GH36 α-galactosidase from Lactobacillus plantarum WCFS1 synthesize Gal-α-1,6 linked prebiotic α-galactooligosaccharide by transglycosylation

Cited by 16 publications

References 42 publications

Biosynthesis of Nondigestible Galactose-Containing Hetero-oligosaccharides by Lactobacillus plantarum WCFS1 MelA α-Galactosidase

Biosynthesis of Nondigestible Galactose-Containing Hetero-oligosaccharides by Lactobacillus plantarum WCFS1 MelA α-Galactosidase

Identification and Characterization of a Thermostable GH36 α-Galactosidase from Anoxybacillus vitaminiphilus WMF1 and Its Application in Synthesizing Isofloridoside by Reverse Hydrolysis

Cloning and expression of a novel α-galactosidase from Lactobacillus amylolyticus L6 with hydrolytic and transgalactosyl properties

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