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Volumn 13, Issue 9, 2012, Pages 11333-11342

An imprinted cross-linked enzyme aggregate (iCLEA) of sucrose phosphorylase: Combining improved stability with altered specificity

Author keywords

CLEA; Glucosyl glycerol; Immobilization; Imprinting; Sucrose phosphorylase

Indexed keywords

ENZYME; GLYCOSYLTRANSFERASE; IMPRINTED CROSS LINKED ENZYME AGGREGATE; SUCROSE PHOSPHORYLASE; UNCLASSIFIED DRUG; GLUCOSYLTRANSFERASE; GLUTARALDEHYDE; GLYCEROL; IMMOBILIZED ENZYME;

EID: 84866900049     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms130911333     Document Type: Article
Times cited : (35)

References (30)
  • 1
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino-acid sequence similarities
    • Henrissat, B. A classification of glycosyl hydrolases based on amino-acid sequence similarities. Biochem. J. 1991, 280, 309-316.
    • (1991) Biochem. J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 45049088085 scopus 로고    scopus 로고
    • Mechanistic differences among retaining disaccharide phosphorylases: Insights from kinetic analysis of active site mutants of sucrose phosphorylase and alpha,alpha-trehalose phosphorylase
    • Goedl, C.; Schwarz, A.; Mueller, M.; Brecker, L.; Nidetzky, B. Mechanistic differences among retaining disaccharide phosphorylases: Insights from kinetic analysis of active site mutants of sucrose phosphorylase and alpha,alpha-trehalose phosphorylase. Carbohydr. Res. 2008, 343, 2032-2040.
    • (2008) Carbohydr. Res , vol.343 , pp. 2032-2040
    • Goedl, C.1    Schwarz, A.2    Mueller, M.3    Brecker, L.4    Nidetzky, B.5
  • 4
    • 74549196321 scopus 로고    scopus 로고
    • Sucrose phosphorylase: A powerful transglucosylation catalyst for the synthesis of alpha-D-glucosides as industrial fine chemicals
    • Goedl, C.; Sawangwan, T.; Wildberger, P.; Nidetzky, B. Sucrose phosphorylase: A powerful transglucosylation catalyst for the synthesis of alpha-D-glucosides as industrial fine chemicals. Biocatal. Biotransform. 2010, 28, 10-21.
    • (2010) Biocatal. Biotransform , vol.28 , pp. 10-21
    • Goedl, C.1    Sawangwan, T.2    Wildberger, P.3    Nidetzky, B.4
  • 5
    • 57749102704 scopus 로고    scopus 로고
    • A high-yielding biocatalytic process for the production of 2-O-(α-D-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient
    • Goedl, C.; Sawangwan, T.; Mueller, M.; Schwarz, A.; Nidetzky, B. A high-yielding biocatalytic process for the production of 2-O-(α-D-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient. Angew. Chem. Int. Ed. Engl. 2008, 47, 10086-10089.
    • (2008) Angew. Chem. Int. Ed. Engl , vol.47 , pp. 10086-10089
    • Goedl, C.1    Sawangwan, T.2    Mueller, M.3    Schwarz, A.4    Nidetzky, B.5
  • 6
    • 70349808079 scopus 로고    scopus 로고
    • Single-step enzymatic synthesis of (R)-2-O-α-D-glucopyranosyl glycerate, a compatible solute from micro-organisms that functions as a protein stabiliser
    • Sawangwan, T.; Goedl, C.; Nidetzky, B. Single-step enzymatic synthesis of (R)-2-O-α-D-glucopyranosyl glycerate, a compatible solute from micro-organisms that functions as a protein stabiliser. Org. Biomol. Chem. 2009, 7, 4267-4270.
    • (2009) Org. Biomol. Chem , vol.7 , pp. 4267-4270
    • Sawangwan, T.1    Goedl, C.2    Nidetzky, B.3
  • 7
    • 0041528514 scopus 로고    scopus 로고
    • Immobilizing enzymes: How to create more suitable biocatalysts
    • Bornscheuer, U.T. Immobilizing enzymes: How to create more suitable biocatalysts. Angew. Chem.-Int. Ed. 2003, 42, 3336-3337.
    • (2003) Angew. Chem.-Int. Ed , vol.42 , pp. 3336-3337
    • Bornscheuer, U.T.1
  • 8
    • 80053576308 scopus 로고    scopus 로고
    • Transglucosylation potential of six sucrose phosphorylases toward different classes of acceptors
    • Aerts, D.; Verhaeghe, T.F.; Roman, B.I.; Stevens, C.V.; Desmet, T.; Soetaert, W. Transglucosylation potential of six sucrose phosphorylases toward different classes of acceptors. Carbohydr. Res. 2011, 346, 1860-1867.
    • (2011) Carbohydr. Res , vol.346 , pp. 1860-1867
    • Aerts, D.1    Verhaeghe, T.F.2    Roman, B.I.3    Stevens, C.V.4    Desmet, T.5    Soetaert, W.6
  • 9
    • 77957367702 scopus 로고    scopus 로고
    • Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization
    • Cerdobbel, A.; Desmet, T.; de Winter, K.; Maertens, J.; Soetaert, W. Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization. J. Biotechnol. 2010a, 150, 125-130.
    • (2010) J. Biotechnol , vol.150 , pp. 125-130
    • Cerdobbel, A.1    Desmet, T.2    de Winter, K.3    Maertens, J.4    Soetaert, W.5
  • 10
    • 78349258236 scopus 로고    scopus 로고
    • Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial applications
    • Cerdobbel, A.; de Winter, K.; Desmet, T.; Soetaert, W. Sucrose phosphorylase as cross-linked enzyme aggregate: Improved thermal stability for industrial applications. Biotechnol. J. 2010b, 5, 1192-1197.
    • (2010) Biotechnol. J , vol.5 , pp. 1192-1197
    • Cerdobbel, A.1    de Winter, K.2    Desmet, T.3    Soetaert, W.4
  • 11
    • 79251469073 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates as industrial biocatalysts
    • Sheldon, R.A. Cross-linked enzyme aggregates as industrial biocatalysts. Org. Process Res. Dev. 2011, 15, 213-223.
    • (2011) Org. Process Res. Dev , vol.15 , pp. 213-223
    • Sheldon, R.A.1
  • 12
    • 80054902432 scopus 로고    scopus 로고
    • Increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis
    • Cerdobbel, A.; de Winter, K.; Aerts, D.; Kuipers, R.; Joosten, H.-J.; Soetaert, W.; Desmet, T. Increasing the thermostability of sucrose phosphorylase by a combination of sequence- and structure-based mutagenesis. Protein Eng. Des. Sel. 2011, 24, 829-834.
    • (2011) Protein Eng. Des. Sel , vol.24 , pp. 829-834
    • Cerdobbel, A.1    de Winter, K.2    Aerts, D.3    Kuipers, R.4    Joosten, H.-J.5    Soetaert, W.6    Desmet, T.7
  • 13
    • 79551502426 scopus 로고    scopus 로고
    • Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe(52)→Ala and Phe(52)→Asn mutants
    • Wildberger, P.; Luley-Goedl, C.; Nidetzky, B. Aromatic interactions at the catalytic subsite of sucrose phosphorylase: Their roles in enzymatic glucosyl transfer probed with Phe(52)→Ala and Phe(52)→Asn mutants. FEBS Lett. 2011, 585, 499-504.
    • (2011) FEBS Lett , vol.585 , pp. 499-504
    • Wildberger, P.1    Luley-Goedl, C.2    Nidetzky, B.3
  • 14
    • 77952581756 scopus 로고    scopus 로고
    • Substitution of the catalytic acid-base glu237 by gln suppresses hydrolysis during glucosylation of phenolic acceptors catalyzed by leuconostoc mesenteroides sucrose phosphorylase
    • Wiesbauer, J.; Goedl, C.; Schwarz, A.; Brecker, L.; Nidetzky, B. Substitution of the catalytic acid-base glu237 by gln suppresses hydrolysis during glucosylation of phenolic acceptors catalyzed by leuconostoc mesenteroides sucrose phosphorylase J. Mol. Catal. B Enzym. 2009, 65, 24-29.
    • (2009) J. Mol. Catal. B Enzym , vol.65 , pp. 24-29
    • Wiesbauer, J.1    Goedl, C.2    Schwarz, A.3    Brecker, L.4    Nidetzky, B.5
  • 15
    • 0000983403 scopus 로고
    • Induced stereo- and substrate selectivity of bioimprinted alpha-chymotrypsin in anhydrous organic media
    • Stahl, M.; Jeppssonwistrand, U.; Mansson, M.O.; Mosbach, K. Induced stereo- and substrate selectivity of bioimprinted alpha-chymotrypsin in anhydrous organic media. J. Am. Chem. Soc. 1991, 113, 9366-9368.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 9366-9368
    • Stahl, M.1    Jeppssonwistrand, U.2    Mansson, M.O.3    Mosbach, K.4
  • 18
    • 0033549571 scopus 로고    scopus 로고
    • Template-mediated synthesis of a polymeric receptor specific to amino acid sequences
    • Klein, J.U.; Whitcombe, M.J.; Mulholland, F.; Vulfson, E.N. Template-mediated synthesis of a polymeric receptor specific to amino acid sequences. Angew. Chem.-Int. Ed. 1999, 38, 2057-2060.
    • (1999) Angew. Chem.-Int. Ed , vol.38 , pp. 2057-2060
    • Klein, J.U.1    Whitcombe, M.J.2    Mulholland, F.3    Vulfson, E.N.4
  • 19
    • 0006644240 scopus 로고    scopus 로고
    • Crosslinking of imprinted proteases to maintain a tailor-made substrate selectivity in aqueous solutions
    • Peissker, F.; Fischer, L. Crosslinking of imprinted proteases to maintain a tailor-made substrate selectivity in aqueous solutions. Bioorgan. Med. Chem. 1999, 7, 2231-2237.
    • (1999) Bioorgan. Med. Chem , vol.7 , pp. 2231-2237
    • Peissker, F.1    Fischer, L.2
  • 20
    • 33846842389 scopus 로고    scopus 로고
    • Molecular imprinting of cyclodextrin glycosyltransferases from paenibacillus sp a11 and bacillus macerans with γ-cyclodextrin
    • Kaulpiboon, J.; Pongsawasdi, P.; Zimmermann, W. Molecular imprinting of cyclodextrin glycosyltransferases from paenibacillus sp a11 and bacillus macerans with γ-cyclodextrin. FEBS J. 2007, 274, 1001-1010.
    • (2007) FEBS J , vol.274 , pp. 1001-1010
    • Kaulpiboon, J.1    Pongsawasdi, P.2    Zimmermann, W.3
  • 21
    • 0347717661 scopus 로고    scopus 로고
    • Altering glucose oxidase to oxidize D-galactose through crosslinking of imprinted protein
    • Vaidya, A.; Borck, A.; Manns, A.; Fischer, L. Altering glucose oxidase to oxidize D-galactose through crosslinking of imprinted protein. Chembiochem 2004, 5, 132-135.
    • (2004) Chembiochem , vol.5 , pp. 132-135
    • Vaidya, A.1    Borck, A.2    Manns, A.3    Fischer, L.4
  • 22
    • 80052891175 scopus 로고    scopus 로고
    • Enhancement of activity of cross-linked enzyme aggregates by a sugar-assisted precipitation strategy: Technical development and molecular mechanism
    • Wang, M.; Qi, W.; Jia, C.; Ren, Y.; Su, R.; He, Z. Enhancement of activity of cross-linked enzyme aggregates by a sugar-assisted precipitation strategy: Technical development and molecular mechanism. J. Biotechnol. 2011, 156, 30-38.
    • (2011) J. Biotechnol , vol.156 , pp. 30-38
    • Wang, M.1    Qi, W.2    Jia, C.3    Ren, Y.4    Su, R.5    He, Z.6
  • 23
    • 79551509765 scopus 로고    scopus 로고
    • Enzymatic glycosyl transfer: Mechanisms and applications
    • doi:10.3109/10242422.2010.548557
    • Desmet, T.; Soetaert, W. Enzymatic glycosyl transfer: Mechanisms and applications. Biocatal. Biotransform. 2011, 29, doi:10.3109/10242422.2010.548557.
    • (2011) Biocatal. Biotransform , vol.29
    • Desmet, T.1    Soetaert, W.2
  • 25
  • 26
    • 0014216416 scopus 로고
    • Purification and mechanism of action of sucrose phosphorylase
    • Silverstein, R.; Voet, J.; Reed, D.; Abeles, R.H. Purification and mechanism of action of sucrose phosphorylase. J. Biol. Chem. 1967, 242, 1338-1346.
    • (1967) J. Biol. Chem , vol.242 , pp. 1338-1346
    • Silverstein, R.1    Voet, J.2    Reed, D.3    Abeles, R.H.4
  • 27
    • 0023406022 scopus 로고
    • Assay of reducing sugars in the nanomole range with 2,2'-bicinchoninate
    • Waffenschmidt, S.; Jaenicke, L. Assay of reducing sugars in the nanomole range with 2,2'-bicinchoninate. Anal. Biochem. 1987, 165, 337-340.
    • (1987) Anal. Biochem , vol.165 , pp. 337-340
    • Waffenschmidt, S.1    Jaenicke, L.2
  • 28
    • 34250489053 scopus 로고
    • Properties of a new chromogen for determination of glucose in blood according to god/pod-method
    • Werner, W.; Rey, H.G.; Wielinge, H. Properties of a new chromogen for determination of glucose in blood according to god/pod-method. Z. Anal. Chem. 1970, 252, 224-228.
    • (1970) Z. Anal. Chem , vol.252 , pp. 224-228
    • Werner, W.1    Rey, H.G.2    Wielinge, H.3
  • 30
    • 55049131930 scopus 로고    scopus 로고
    • Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: A recyclable enantioselective catalyst
    • Cabirol, F.L.; Tan, P.L.; Tay, B.; Cheng, S.; Hanefeld, U.; Sheldon, R.A. Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: A recyclable enantioselective catalyst. Adv. Synth. Catal. 2008, 350, 2329-2338.
    • (2008) Adv. Synth. Catal , vol.350 , pp. 2329-2338
    • Cabirol, F.L.1    Tan, P.L.2    Tay, B.3    Cheng, S.4    Hanefeld, U.5    Sheldon, R.A.6


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