Glycosidase-catalysed synthesis of alkyl glycosides

Rantwijk, Fred van; Oosterom, Marjolein Woudenberg-van; Sheldon, Roger A.

doi:10.1016/s1381-1177(99)00042-9

Cited by 274 publications

(181 citation statements)

References 117 publications

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“…To overcome this limitation, several protein engineering strategies, based on site directed mutagenesis (Mackensie et al 1998) or molecular directed evolution (Feng et al 2005), have been proposed to reduce and even eliminate the hydrolytic activities of glycosidases while keeping the transglycosylation activities. Other alternatives suggested to prevent the undesirable hydrolysis reaction were reducing the water activity by using organic solvents (van Rantwijk et al 1999) or using frozen buffer (ChiffoleauGiraud et al 1997). However, most of the water-immiscible solvents do not dissolve carbohydrate substrates while water-miscible solvents, such as DMSO and DMF, although dissolving carbohydrates, generally inactivate glycosidases at concentrations above 20%.…”

Section: Introductionmentioning

confidence: 99%

Correlation between thermostability and stability of glycosidases in ionic liquid

et al. 2011

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Section: Introductionmentioning

confidence: 99%

Correlation between thermostability and stability of glycosidases in ionic liquid

et al. 2011

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“…The enzymatic approach can be followed through either the thermodynamically controlled reverse hydrolysis reaction or the kinetically controlled transglycosylation reaction (4). The latter has the possibility to overshoot the thermodynamic equilibrium and is more influenced by the properties of the enzyme (5); therefore, it is the focus of this study.…”

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confidence: 99%

Improved Transferase/Hydrolase Ratio through Rational Design of a Family 1 β-Glucosidase from Thermotoga neapolitana

Lundemo

Adlercreutz

Karlsson

2013

Appl Environ Microbiol

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Alkyl glycosides are attractive surfactants because of their high surface activity and good biodegradability and can be produced from renewable resources. Through enzymatic catalysis, one can obtain well-defined alkyl glycosides, something that is very difficult to do using conventional chemistry. However, there is a need for better enzymes to get a commercially feasible process. A thermostable ␤-glucosidase from the well-studied glycoside hydrolase family 1 from Thermotoga neapolitana, TnBgl1A, was mutated in an attempt to improve its value for synthesis of alkyl glycosides. This was done by rational design using prior knowledge from structural homologues together with a recently generated model of the enzyme in question. Three out of four studied mutations increased the hydrolytic reaction rate in an aqueous environment, while none displayed this property in the presence of an alcohol acceptor. This shows that even if the enzyme resides in a separate aqueous phase, the presence of an organic solvent has a great influence. We could also show that a single amino acid replacement in a less studied part of the aglycone subsite, N220F, improves the specificity for transglycosylation 7-fold and thereby increases the potential yield of alkyl glycoside from 17% to 58%.

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“…1,2) On the other hand, thermostable glycosidases have been recently isolated from hyperthermophilic microorganisms [3][4][5][6][7][8][9] and utilized for synthesis of alkyl glucosides and oligosaccharides. 2,[10][11][12][13][14][15] Glycosylation using thermostable glycosidases was performed at an elevated temperature to compensate for the low solubility of glycosyl acceptor and/or donor. 2) The -glucosidase form Pyrococcus furiosus (Pfu--glucosidase) is one of the most thermostable glycosidases and has respectable -galactosidase and -mannosidase activity.…”

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confidence: 99%

“…2,[10][11][12][13][14][15] Glycosylation using thermostable glycosidases was performed at an elevated temperature to compensate for the low solubility of glycosyl acceptor and/or donor. 2) The -glucosidase form Pyrococcus furiosus (Pfu--glucosidase) is one of the most thermostable glycosidases and has respectable -galactosidase and -mannosidase activity. [5][6][7][8] Only two methods for immobilization of Pfu--glucosidase have been reported.…”

mentioning

confidence: 99%

Preparation and Properties of Gelatin-Immobilized β-Glucosidase fromPyrococcus furiosus

Nagatomo

Matsushita

Sugamoto

et al. 2005

Bioscience, Biotechnology, and Biochemistry

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Hyperthermostable -glucosidase from Pyrococcus furiosus was enclosed in gelatin gel by cross-linking with transglutaminase. Gelatin-immobilized -glucosidase was considerably more thermostable than the native enzyme. Lyophilized immobilisate was stored at 90 C for 1 month without loss of activity. The immobilized -glucosidase catalyzed transglucosylation of 5-phenylpentanol with 10.0 equivalent of cellobiose at pH 5.0 and 70 C for 12 h to afford 5-phenylpentyl -Dglucopyranoside in 41% yield. The immobilized enzyme was more effective than the native one in transglucosylation. The gelatin-immobilized Pfu--glucosidase recovered from the first run of the reaction was reusable on successive runs.

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Glycosidase-catalysed synthesis of alkyl glycosides

Cited by 274 publications

References 117 publications

Correlation between thermostability and stability of glycosidases in ionic liquid

Correlation between thermostability and stability of glycosidases in ionic liquid

Improved Transferase/Hydrolase Ratio through Rational Design of a Family 1 β-Glucosidase from Thermotoga neapolitana

Preparation and Properties of Gelatin-Immobilized β-Glucosidase fromPyrococcus furiosus

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