α-d-Galactosidase immobilized on a soluble polymer

Kuo, Jong-Yuan; Goldstein, Jack

doi:10.1016/0141-0229(83)90079-0

Cited by 16 publications

(8 citation statements)

References 20 publications

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“…Enzymes can be modified with CNBr-activated water-soluble carbohydrates through chemistry similar to that involved on immobilization on CNBr-activated polysaccharide supports. − ,− It is strongly recommended to perform a previous activation step, followed by purification of the resulting reactive carbohydrate before coupling to the enzyme molecule to avoid CNBr-mediated protein cleavage.…”

Section: Strategies For Preparing Artificial Glycoenzymesmentioning

confidence: 99%

Neoglycoenzymes

et al. 2014

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Section: Strategies For Preparing Artificial Glycoenzymesmentioning

confidence: 99%

Neoglycoenzymes

et al. 2014

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“…Enzyme from coffee beans was covalently bound to dextran activated with cyanogen bromide (Kuo & Goldstein, 1983). α-D-galactosidase from Pycnoporus cinnabarinus was immobilized on chitin dispersions with glutaric dialdehyde (Ohtakara & Mitsutomi, 1987).…”

Section: Immobilization Of α-D-galactosidasesmentioning

confidence: 99%

Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

Bakunina

Balabanova

Pennacchio

et al. 2015

Critical Reviews in Biotechnology

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α-d-Galactosidases (EC 3.2.1.22) are enzymes employed in a number of useful bio-based applications. We have depicted a comprehensive general survey of α-d-galactosidases from different origin with special emphasis on marine example(s). The structures of natural α-galactosyl containing compounds are described. In addition to 3D structures and mechanisms of action of α-d-galactosidases, different sources, natural function and genetic regulation are also covered. Finally, hydrolytic and synthetic exploitations as free or immobilized biocatalysts are reviewed. Interest in the synthetic aspects during the next years is anticipated for access to important small molecules by green technology with an emphasis on alternative selectivity of this class of enzymes from different sources.

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“…General stability information Mn 2 + (stabilizes du ring enzyme assay) [1]; Reducing agents (stabilize du ring enzyme assay) [1]; Thawing (loss of activity) [5]; lmmobilization [7,8]; Lyophilized (-20 °C, enzyme I stable enzyme, II not stable) [21]; Freezedrying (60% loss of activity [25], stable [35]) [25,35]; Freezing and thawing (stable) [35]; Dilute solutions (very unstable even at D-5°C) [55] Storage 4°C, 30 days (36% loss of activity) [20]; -20°C, 20% glycerol (indefinitely stable) [20]; -20°C, pH 6.5, 6 months [22]; 4°C, several months [25]; -20°C, 30% glycerol, 10% sucrose, 3 months [35]; -20°C, 0.02 M sodium acetate buffer, pH 5.2 [54] Enzyme Handbook ©Springer-Verlag Berlin Heidelberg 1991 Duplication, reproduction and storage in data banks are only allowed with the prior permission of the publishers…”

Section: Organic Solventmentioning

confidence: 99%

Alpha-galactosidase

Schomburg¹,

Salzmann²

1991

Enzyme Handbook 4

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Synonymes Melibiase Galactosidase, .alpha . . alpha.-0-Galactosidase .alpha.-Galactosidase .alpha.-Galactosidase A .alpha.-0-Galactoside galactohydrolase . alpha.-Galactoside galactohydrolase CASReg. No. 9025-35-8 REACTION AND SPECIFICITY Catalysed reactionAlpha-0-galactoside (galactose-ROH} + H 2 0 ---> 3.2.1.22---> galactose + R (mechanism [1], hydro Iysis of terminal, non-reducing alpha-0-galactose residues in alpha-0-galactosides, including galactose oligosaccharides, galactomannans and galactolipids} Reaction type 0-Giycosyl band hydrolysis, 57] 3 Melibiose + H 2 0 [1, 15, 33, 53] 4 Raffinose + H 2 0 [1, 2, 4, 15, 20, 29, 33, 44, 53) 5 Stachyose + H 2 0 [2, 15, 20, 29, 33) Enzyme Handbock ©Springer-Verlag Berlin Heldeiberg 1991 Duplication, reproduction and storage in data banks are only allowed with the prior permission of the publishers Alpha-galactosidase 3.2.1.22 6 Glycolipids + H 2 0 [40] 7 Galabiosylceramide + H20 [40]8 Globotriglycosylceramide + H 2 0 [40] 9 Disaccharides (and derivatives) + H 2 0 (overview) [5] 10 Trisaccharides (reducing and nonreducing) + H 2 0 (overview) [5] 11 Oligosaccharides + H 2 0 (overview) [5] 12 Polysaccharides+ H 2 0 (overview) [5] 13 More (galactosyl transferase activity [1,5,24,37,49,55], alphafucosidase activity [33], hydrolysis of alpha-D-galactopyranosidic linkages in glycosides of methanol, phenol and p-nitrophenol [5], Ieetin activity [33], not: substances with beta-galactosidic linkages [2], not: arabinosides [57]) [1, 2, 5, 24, 33, 37, 49, 55] Product spectrum 1 Galactose + ? (e.g. p-nitrophenol + D-galactose) 2 Fucose + ? (e.g. p-nitrophenol + D-fucose) 3 D-Galactose + D-glucose 4 Galactose + sucrose [2] 5 Galactose [2]

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α-d-Galactosidase immobilized on a soluble polymer

Cited by 16 publications

References 20 publications

Neoglycoenzymes

Neoglycoenzymes

Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

Alpha-galactosidase

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