Enzymatic Production and Characterization of Konjac Glucomannan Oligosaccharides

Albrecht, Simone; Muiswinkel, G.C.J. van; Xu, Jiqiang; Schols, Henk A.; Voragen, A.G.J.; Gruppen, Harry

doi:10.1021/jf203091h

Cited by 52 publications

(23 citation statements)

References 29 publications

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“…Moreover, KPM contains high amount of cKGM and the amine contents of cKGM may act as a buffer region in acidic environment and delay the hydrolysis of nucleic acid drug by gastric acid. Besides this, the existence of enzyme form the colon flora may degrade cKGM and may lead to the destabilization of cKGM&ASO complex which is existed in the colon lumen [27,28]. But we observed that the degradation percentage of cKGM was much lower than that of KGM with cellulase and mannase digestion and cKGM&ASO complex could still strand in the well after long term digestion.…”

Section: Discussionmentioning

confidence: 74%

An orally administrated nucleotide-delivery vehicle targeting colonic macrophages for the treatment of inflammatory bowel disease

et al. 2015

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Section: Discussionmentioning

confidence: 74%

An orally administrated nucleotide-delivery vehicle targeting colonic macrophages for the treatment of inflammatory bowel disease

et al. 2015

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“…3). The main hydrolysis products of locust bean gum and konjac flour have been reported as galactose-branched mannooligosaccharides (17) and glucose-linked mannooligosaccharides (18). In the case of Man113A, a larger amount of shorter sugars was detected in the hydrolysis products of locust bean gum while higher hydrolytic activities (defined by the total reduced sugar equivalents) were detected when using konjac flour as the substrate.…”

Section: Resultsmentioning

confidence: 99%

A Novel Glycoside Hydrolase Family 113 Endo-β-1,4-Mannanase from Alicyclobacillus sp. Strain A4 and Insight into the Substrate Recognition and Catalytic Mechanism of This Family

Xia

et al. 2016

Appl Environ Microbiol

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c Few members of glycoside hydrolase (GH) family 113 have been characterized, and information on substrate recognition by and the catalytic mechanism of this family is extremely limited. In the present study, a novel endo-␤-1,4-mannanase of GH 113, Man113A, was identified in thermoacidophilic Alicyclobacillus sp. strain A4 and found to exhibit both hydrolytic and transglycosylation activities. The enzyme had a broad substrate spectrum, showed higher activities on glucomannan than on galactomannan, and released mannobiose and mannotriose as the main hydrolysis products after an extended incubation. Compared to the only functionally characterized and structure-resolved counterpart Alicyclobacillus acidocaldarius ManA (AaManA) of GH 113, Man113A showed much higher catalytic efficiency on mannooligosaccharides, in the order mannohexaose Ϸ mannopentaose > mannotetraose > mannotriose, and required at least four sugar units for efficient catalysis. Homology modeling, molecular docking analysis, and site-directed mutagenesis revealed the vital roles of eight residues (Trp13, Asn90, Trp96, Arg97, Tyr196, Trp274, Tyr292, and Cys143) related to substrate recognition by and catalytic mechanism of GH 113. Comparison of the binding pockets and key residues of ␤-mannanases of different families indicated that members of GH 113 and GH 5 have more residues serving as stacking platforms to support ؊4 to ؊1 subsites than those of GH 26 and that the residues preceding the acid/base catalyst are quite different. Taken as a whole, this study elucidates substrate recognition by and the catalytic mechanism of GH 113 ␤-mannanases and distinguishes them from counterparts of other families.A major component of hemicellulose in the plant cell walls of softwood, plant seeds, and beans is ␤-1,4-mannan, including mannan polysaccharides, glucomannan, galactomannan, and galactoglucomannan. It is composed of a backbone of ␤-1,4-linked mannose or a combination of glucose and mannose with side chains of ␣-1,6-linked galactose residues (1). The mannan-degrading enzymes have biotechnological applications in various areas, such as feed manufacturing (2), paper processing (3), and coffee extract treatment (4). Mannooligosaccharides, the major hydrolysis products of mannan, are beneficial as animal nutrition additives due to their potential prebiotic properties (5). The complete degradation of mannan polysaccharides into monomers requires an enzyme system including ␤-mannanase (EC 3.2.1.78), ␤-mannosidase (EC 3.2.1.25), ␤-glucosidase (EC 3.2.1.21), and ␣-galactosidase (EC 3.2.1.22). Of these, ␤-mannanase randomly hydrolyzes the ␤-D-1,4-mannopyranoside linkages and plays the major role in mannan degradation.␤-Mannanases are widely distributed in various organisms, including bacteria, yeasts, filamentous fungi, and plants. Based on the amino acid sequence and structural similarities of catalytic domains, ␤-mannanases are grouped into three glycoside hydrolase (GH) families in the Carbohydrate-Active enZYmes (CAZy) database (6), i.e., 5, 26, and 113. GH 1...

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“…Thus, the potential ␤-mannosidase and ␣-galactosidase activities of B. adolescentis necessary for monosaccharide release from the BaMan26A products remain to be identified. In addition, there is a possibility that bacterial consortia, rather than individual organisms, contribute to the complete degradation of complex heteromannan substrates in the colon (26).…”

Section: Discussionmentioning

confidence: 99%

“…Not only can ␤-mannans be metabolized in terrestrial and marine environments, but also guar gum galactomannan can be fermented in the human digestive tract (24), and mixed cultures from human feces are able to hydrolyze guar gum galactomannan (25) and glucomannan oligosaccharides (26,27). The processing and utilization of nondigestible diet polysaccharides by the human gut bacteria are highly important for the health of the host (28,29).…”

mentioning

confidence: 99%

Expression and Characterization of a Bifidobacterium adolescentis Beta-Mannanase Carrying Mannan-Binding and Cell Association Motifs

Kulcinskaja

Rosengren

Ibrahim

et al. 2013

Appl Environ Microbiol

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The gene encoding ␤-mannanase (EC 3.2.1.78) BaMan26A from the bacterium Bifidobacterium adolescentis (living in the human gut) was cloned and the gene product characterized. The enzyme was found to be modular and to contain a putative signal peptide. It possesses a catalytic module of the glycoside hydrolase family 26, a predicted immunoglobulin-like module, and two putative carbohydrate-binding modules (CBMs) of family 23. The enzyme is likely cell attached either by the sortase mechanism (LPXTG motif) or via a C-terminal transmembrane helix. The gene was expressed in Escherichia coli without the native signal peptide or the cell anchor. Two variants were made: one containing all four modules, designated BaMan26A-101K, and one truncated before the CBMs, designated BaMan26A-53K. BaMan26A-101K, which contains the CBMs, showed an affinity to carob galactomannan having a dissociation constant of 0.34 M (8.8 mg/liter), whereas BaMan26A-53K did not bind, showing that at least one of the putative CBMs of family 23 is mannan binding. For BaMan26A-53K, k cat was determined to be 444 s ؊1 and K m 21.3 g/liter using carob galactomannan as the substrate at the optimal pH of 5.3. Both of the enzyme variants hydrolyzed konjac glucomannan, as well as carob and guar gum galactomannans to a mixture of oligosaccharides. The dominant product from ivory nut mannan was found to be mannotriose. Mannobiose and mannotetraose were produced to a lesser extent, as shown by high-performance anion-exchange chromatography. Mannobiose was not hydrolyzed, and mannotriose was hydrolyzed at a significantly lower rate than the longer oligosaccharides.

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Enzymatic Production and Characterization of Konjac Glucomannan Oligosaccharides

Cited by 52 publications

References 29 publications

An orally administrated nucleotide-delivery vehicle targeting colonic macrophages for the treatment of inflammatory bowel disease

An orally administrated nucleotide-delivery vehicle targeting colonic macrophages for the treatment of inflammatory bowel disease

A Novel Glycoside Hydrolase Family 113 Endo-β-1,4-Mannanase from Alicyclobacillus sp. Strain A4 and Insight into the Substrate Recognition and Catalytic Mechanism of This Family

Expression and Characterization of a Bifidobacterium adolescentis Beta-Mannanase Carrying Mannan-Binding and Cell Association Motifs

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