Transglucosylation of a Fungal α‐Glucosidase

Duan, Kow‐Jen; Sheu, Dey-Chyi; Lin, Chi‐Tsai

doi:10.1111/j.1749-6632.1995.tb19974.x

Cited by 30 publications

(25 citation statements)

References 5 publications

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“…Furthermore, the results were different from the α- glucosidases originated from other strains (Table 3). With 300 g/L maltose as substrate, the main transglycosylation product of Aspergillus niger α-glucosidase was 30% (w/v) isomaltose (Duan et al 1995). The α-glucosidase from Bacillus stearothermophilus produced α-1, 3-, α-1,4-, and α-1,6-glucosidic linkages to produce prebiotic oligosaccharides (Mala et al 1999).…”

Section: Biochemical Characterization Of the Recombinant α-Glucosidasementioning

confidence: 99%

“…Many α-glucosidases also catalyze the transglycosylation reaction besides hydrolysis activity. For example, the α-glucosidase from Aspergillus niger converted maltose into isomaltose and panose (Duan et al 1995) and that from Xantophyllomyces dendrorhous yielded a final product enriched in trisaccharides and tetrasaccharides (Lucia et al 2007). This transglycosylation activity has been applied in the industrial production of isomaltooligodaccharides (Crittenden & Playne 1996) and in improving the chemical properties by conjugating sugar residues (Murase et al 1997;Prodanovic et al 2005).…”

Section: Introductionmentioning

confidence: 99%

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Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application

et al. 2009

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In this study, a new α-glucosidase gene from Thermoanaerobacter ethanolicus JW200 was cloned and expressed in Escherichia coli by a novel heat-shock vector pHsh. The recombinant α-glucosidase exhibited its maximum hydrolytic activity at 70• C and pH 5.0∼5.5. With p-nitrophenyl-α-D-glucoside as a substrate and under the optimal condition (70 • C, pH 5.5), Km and Vmax of the enzyme was 1.72 mM and 39 U/mg, respectively. The purified α-glucosidase could hydrolyze oligosaccharides with both α-1,4 and α-1,6 linkages. The enzyme also had strong transglycosylation activity when maltose was used as sugar donor. The transglucosylation products towards maltose are isomaltose, maltotriose, panose, isomaltotriose and tetrasaccharides. The enzyme could convert 400 g/L maltose to oligosaccharides with a conversion rate of 52%, and 83% of the oligosaccharides formed were prebiotic isomaltooligosaccharides (containing isomaltose, panose and isomaltotriose).

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Section: Biochemical Characterization Of the Recombinant α-Glucosidasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application

et al. 2009

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“…Theoretically ␣-glucosidase is capable of catalyzing transglycosylation, since it is a retaining glycosyl hydrolase (GH) (2), and some ␣-glucosidases indeed exhibit clear transglycosylation activity. For example, Aspergillus niger ␣-glucosidase catalyzes formation of ␣-1,6 glucosidic linkages in addition to hydrolysis, resulting in production of isomaltose (6-O-␣-D-glucopyranosyl-D-glucopyranose) and panose (6-O-␣-glucopyranosyl-maltose) from maltose (3,15,21). Buckwheat ␣-glucosidase produces kojibiose (2-O-␣-glucosyl-glucose), nigerose (3-O-␣-glucosyl-glucose), maltose, and isomaltose from soluble starch (1), and ␣-glucosidases from Bacillus stearothermophilus and brewer's yeast produce oligosaccharides consisting of ␣-1,3, ␣-1,4, and ␣-1,6 linkages (13).…”

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confidence: 99%

“…At 6 h of the reaction, approximately 50% of maltose was converted to transglycosylation products, 60% of which was found to be isomaltose. Formation of isomaltose and panose from maltose by the action of ␣-glucosidase has been demonstrated in A. niger and A. oryzae (3,15,(20)(21)(22). The A. niger enzyme possesses strong transglycosylation activity, however, a maltose concentration of 30% is used for A. niger ␣-glucosidase to achieve an isomaltose content of 30% in the final reaction products (3,21).…”

mentioning

confidence: 99%

“…6B). A. niger ␣-glucosidase, which has been shown to exhibit strong transglycosylation activity (3,15,21), was located in the fungal cluster with close genetic distances to ␣-glucosidases (AgdAs) from A. oryzae and A. nidulans. However, AgdB was phylogenetically distant from those Aspergillus ␣-glucosidases, and surprisingly, it was located outside of the fungal cluster.…”

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Novel α-Glucosidase from Aspergillus nidulans with Strong Transglycosylation Activity

Kato

Suyama

Shirokane

et al. 2002

Appl Environ Microbiol

128

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Aspergillus nidulans possessed an ␣-glucosidase with strong transglycosylation activity. The enzyme, designated ␣-glucosidase B (AgdB), was purified and characterized. AgdB was a heterodimeric protein comprising 74-and 55-kDa subunits and catalyzed hydrolysis of maltose along with formation of isomaltose and panose. Approximately 50% of maltose was converted to isomaltose, panose, and other minor transglycosylation products by AgdB, even at low maltose concentrations. The agdB gene was cloned and sequenced. The gene comprised 3,055 bp, interrupted by three short introns, and encoded a polypeptide of 955 amino acids. The deduced amino acid sequence contained the chemically determined N-terminal and internal amino acid sequences of the 74-and 55-kDa subunits. This implies that AgdB is synthesized as a single polypeptide precursor. AgdB showed low but overall sequence homology to ␣-glucosidases of glycosyl hydrolase family 31. However, AgdB was phylogenetically distinct from any other ␣-glucosidases. We propose here that AgdB is a novel ␣-glucosidase with unusually strong transglycosylation activity.␣-Glucosidases (EC 3.2.1.20) catalyze liberation of glucose from nonreducing ends of ␣-glucosides, ␣-linked oligosaccharides, and ␣-glucans. They show diverse substrate specificities; some prefer ␣-linked di-, oligo-, and/or polyglucans, while others preferentially hydrolyze heterogeneous substrates such as aryl glucosides and sucrose (1, 5). Theoretically ␣-glucosidase is capable of catalyzing transglycosylation, since it is a retaining glycosyl hydrolase (GH) (2), and some ␣-glucosidases indeed exhibit clear transglycosylation activity. For example, Aspergillus niger ␣-glucosidase catalyzes formation of ␣-1,6 glucosidic linkages in addition to hydrolysis, resulting in production of isomaltose (6-O-␣-D-glucopyranosyl-D-glucopyranose) and panose (6-O-␣-glucopyranosyl-maltose) from maltose (3,15,21). Buckwheat ␣-glucosidase produces kojibiose (2-O-␣-glucosyl-glucose), nigerose (3-O-␣-glucosyl-glucose), maltose, and isomaltose from soluble starch (1), and ␣-glucosidases from Bacillus stearothermophilus and brewer's yeast produce oligosaccharides consisting of ␣-1,3, ␣-1,4, and ␣-1,6 linkages (13). Transglycosylation activity of the ␣-glucosidases has been applied in industries to produce isomaltooligosaccharides and also to conjugate sugars to biologically useful materials, aiming to improve their chemical properties and physiological functions (18, 33).The main physiological role of most exo-type glycosidases such as ␣-glucosidase is to produce monosaccharides that are utilized as carbon and energy sources. However, transglycosylation activities of exo-type glycosidases sometimes play physiologically important roles in gene regulation involved in carbohydrate utilization. A well-known example is induction of the lac operon in Escherichia coli. The physiological inducer of the operon, allolactose (6-O-␤-D-galactopyranosyl-D-glucose), is synthesized from lactose by transglycosylation activity of ␤-galactosidase encoded by ...

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