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Volumn 13, Issue 4, 2002, Pages 376-384

Enzyme activation for nonaqueous media

Author keywords

[No Author keywords available]

Indexed keywords

BETA CYCLODEXTRIN DERIVATIVE; ETHER DERIVATIVE; EXCIPIENT; HORSERADISH PEROXIDASE; MACROGOL; SUBTILISIN; SURFACTANT; TRIACYLGLYCEROL LIPASE;

EID: 0036669618     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(02)00337-3     Document Type: Review
Times cited : (195)

References (47)
  • 1
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov A.M. Improving enzymes by using them in organic solvents. Nature. 409:2001;241-246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 2
    • 0031047280 scopus 로고    scopus 로고
    • Structure and function of subtilisin BPN′ solubilized in organic solvents
    • Wangikar P.P., Michels P.C., Clark D.S., Dordick J.S. Structure and function of subtilisin BPN′ solubilized in organic solvents. J Am Chem Soc. 119:1997;70-76.
    • (1997) J Am Chem Soc , vol.119 , pp. 70-76
    • Wangikar, P.P.1    Michels, P.C.2    Clark, D.S.3    Dordick, J.S.4
  • 3
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • Carrea G., Riva S. Properties and synthetic applications of enzymes in organic solvents. Angew Chem Int Ed. 39:2000;2226-2254.
    • (2000) Angew Chem Int Ed , vol.39 , pp. 2226-2254
    • Carrea, G.1    Riva, S.2
  • 4
    • 0027909093 scopus 로고
    • Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectants
    • Dabulis K., Klibanov A.M. Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectants. Biotechnol Bioeng. 41:1993;566-571.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 566-571
    • Dabulis, K.1    Klibanov, A.M.2
  • 5
    • 0029636230 scopus 로고
    • Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media
    • Triantafyllou A.O., Wehtje E., Adlercreutz P., Mattiasson B. Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media. Biotechnol Bioeng. 45:1995;406-414.
    • (1995) Biotechnol Bioeng , vol.45 , pp. 406-414
    • Triantafyllou, A.O.1    Wehtje, E.2    Adlercreutz, P.3    Mattiasson, B.4
  • 7
    • 0027962938 scopus 로고
    • Salts dramatically enhance activity of enzymes suspended in organic solvents
    • Khmelnitsky Y.L., Welch S.H., Clark D.S., Dordick J.S. Salts dramatically enhance activity of enzymes suspended in organic solvents. J Am Chem Soc. 116:1994;2647-2648.
    • (1994) J Am Chem Soc , vol.116 , pp. 2647-2648
    • Khmelnitsky, Y.L.1    Welch, S.H.2    Clark, D.S.3    Dordick, J.S.4
  • 8
    • 0032551298 scopus 로고    scopus 로고
    • Testing for diffusion limitations in salt-activated enzyme catalysts operating in organic solvents
    • Bedell B.A., Mozhaev V.V., Clark D.S., Dordick J.S. Testing for diffusion limitations in salt-activated enzyme catalysts operating in organic solvents. Biotechnol Bioeng. 58:1998;654-657.
    • (1998) Biotechnol Bioeng , vol.58 , pp. 654-657
    • Bedell, B.A.1    Mozhaev, V.V.2    Clark, D.S.3    Dordick, J.S.4
  • 9
    • 0033586738 scopus 로고    scopus 로고
    • Optimizing the salt-induced activation of enzymes in organic solvents: Effects of lyophilization time and water content
    • Ru M.T., Dordick J.S., Reimer J.A., Clark D.S. Optimizing the salt-induced activation of enzymes in organic solvents: effects of lyophilization time and water content. Biotechnol Bioeng. 63:1999;233-241.
    • (1999) Biotechnol Bioeng , vol.63 , pp. 233-241
    • Ru, M.T.1    Dordick, J.S.2    Reimer, J.A.3    Clark, D.S.4
  • 10
    • 0034058387 scopus 로고    scopus 로고
    • On the salt-induced activation of lyophilized enzymes in organic solvents: Effect of salt kosmotropicity on enzyme activity
    • Ru M.T., Hirokane S.Y., Lo A.S., Dordick J.S., Reimer J.A., Clark D.S. On the salt-induced activation of lyophilized enzymes in organic solvents: effect of salt kosmotropicity on enzyme activity. J Am Chem Soc. 122:2000;1565-1571. The mechanism of the dramatic activation of enzymes by nonbuffer salts is partially elucidated in this work. Significant correlation of enzyme activity and the kosmotropicity of the salt (as reflected in its Jones-Dole B coefficient) indicates that salt-activation is a physicochemical phenomenon that may partly relate to the stabilization of the native enzyme structure in the organic media by a preferential hydration-type mechanism.
    • (2000) J Am Chem Soc , vol.122 , pp. 1565-1571
    • Ru, M.T.1    Hirokane, S.Y.2    Lo, A.S.3    Dordick, J.S.4    Reimer, J.A.5    Clark, D.S.6
  • 11
    • 0035922876 scopus 로고    scopus 로고
    • Towards more active biocatalysts in organic media: Increasing the activity of salt activated enzymes
    • Ru M.T., Wu K.C., Dordick J.S., Reimer J.A., Clark D.S. Towards more active biocatalysts in organic media: increasing the activity of salt activated enzymes. Biotechnol Bioeng. 75:2001;187-196.
    • (2001) Biotechnol Bioeng , vol.75 , pp. 187-196
    • Ru, M.T.1    Wu, K.C.2    Dordick, J.S.3    Reimer, J.A.4    Clark, D.S.5
  • 12
    • 33947352893 scopus 로고
    • Viscosity of aqueous solutions of strong electrolytes with special reference to barium chloride
    • Jones G., Dole M. Viscosity of aqueous solutions of strong electrolytes with special reference to barium chloride. J Am Chem Soc. 51:1929;2950-2964.
    • (1929) J Am Chem Soc , vol.51 , pp. 2950-2964
    • Jones, G.1    Dole, M.2
  • 13
    • 0028999046 scopus 로고
    • Sticky ions in biological systems
    • Collins K.D. Sticky ions in biological systems. Proc Natl Acad Sci USA. 92:1995;5553-5557.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5553-5557
    • Collins, K.D.1
  • 14
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T., Timasheff S.N. Stabilization of protein structure by sugars. Biochemistry. 21:1982;6536-6544.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 16
    • 0037028984 scopus 로고    scopus 로고
    • Nonaqueous biocatalytic synthesis of new cytotoxic doxorubicin derivatives: Exploiting unexpected differences in the regioselectivity of salt-activated and solubilized subtilisin
    • Altreuter D.H., Dordick J.S., Clark D.S. Nonaqueous biocatalytic synthesis of new cytotoxic doxorubicin derivatives: exploiting unexpected differences in the regioselectivity of salt-activated and solubilized subtilisin. J Am Chem Soc. 124:2002;1871-1876. Lipase from Mucor miehei and subtilisin Carlsberg were shown to catalyze the selective acylation of DOX in toluene to yield several novel derivatives with greater potency than native DOX against MCF7 and MCF7-ADR multidrug-resistant breast cancer cell lines. Acylation of DOX was greatly facilitated by salt-activation of both enzymes. Interestingly, the salt-activated subtilisin was more promiscuous in its regioselectivity than the lipase or ion-paired lipase and ion-paired subtilisin, and catalyzed the formation of acylated DOX derivatives at the 14, 3′, and 4′ sites. This result indicates that enzymic regioselectivity can be tailored by enzyme activation methods.
    • (2002) J Am Chem Soc , vol.124 , pp. 1871-1876
    • Altreuter, D.H.1    Dordick, J.S.2    Clark, D.S.3
  • 17
    • 0037008370 scopus 로고    scopus 로고
    • Penicillin amidase is activated for use in nonaqueous media by lyophilizing in the presence of potassium chloride
    • in press
    • Lindsay JP, Clark DS, Dordick JS: Penicillin amidase is activated for use in nonaqueous media by lyophilizing in the presence of potassium chloride. Enzyme Microb Technol 2002, in press.
    • (2002) Enzyme Microb Technol
    • Lindsay, J.P.1    Clark, D.S.2    Dordick, J.S.3
  • 18
    • 85031371598 scopus 로고    scopus 로고
    • Biocatalytic methods for synthesizing and identifying biologically active compounds. US Patent 6,136,961, 2001.
    • Dordick JS, Clark DS, Michels PC, Khmelnitsky YL: Biocatalytic methods for synthesizing and identifying biologically active compounds. US Patent 6,136,961, 2001.
    • Dordick, J.S.1    Clark, D.S.2    Michels, P.C.3    Khmelnitsky, Y.L.4
  • 20
    • 0032487140 scopus 로고    scopus 로고
    • Large acceleration of α-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents
    • van Unen D.-J., Engbersen J.F.J., Reinhoudt D.N. Large acceleration of α-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents. Biotechnol Bioeng. 59:1998;553-556.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 553-556
    • Van Unen, D.-J.1    Engbersen, J.F.J.2    Reinhoudt, D.N.3
  • 21
    • 0000074941 scopus 로고    scopus 로고
    • Effects of crown ethers and small amounts of cosolvent on the activity and enantioselectivity of α-chymotrypsin in organic solvents
    • Engbersen J.F.J., Broos J., Verboom W., Reinhoudt D.N. Effects of crown ethers and small amounts of cosolvent on the activity and enantioselectivity of α-chymotrypsin in organic solvents. Pure Appl Chem. 68:1996;2171-2178.
    • (1996) Pure Appl Chem , vol.68 , pp. 2171-2178
    • Engbersen, J.F.J.1    Broos, J.2    Verboom, W.3    Reinhoudt, D.N.4
  • 22
    • 0035931572 scopus 로고    scopus 로고
    • Studies on the mechanism of crown-ether-induced activation of enzymes in non-aqueous media
    • van Unen D.-J., Engbersen J.F.J., Reinhoudt D.N. Studies on the mechanism of crown-ether-induced activation of enzymes in non-aqueous media. J Mol Catal B Enzymat. 11:2001;877-882.
    • (2001) J Mol Catal B Enzymat , vol.11 , pp. 877-882
    • Van Unen, D.-J.1    Engbersen, J.F.J.2    Reinhoudt, D.N.3
  • 23
    • 0034801424 scopus 로고    scopus 로고
    • Native-like enzyme properties are important for optimum activity in neat organic solvents
    • Griebenow K., Vidal M., Baez C., Santos A.M., Barletta G. Native-like enzyme properties are important for optimum activity in neat organic solvents. J Am Chem Soc. 123:2001;5380-5381. The authors have used FTIR spectroscopy to probe the secondary structure of subtilisin Carlsberg in different solvents following lyophilization in the presence of 18-crown-6. The crown ether appears to promote enzyme activation in organic media by increasing the flexibility of the enzyme.
    • (2001) J Am Chem Soc , vol.123 , pp. 5380-5381
    • Griebenow, K.1    Vidal, M.2    Baez, C.3    Santos, A.M.4    Barletta, G.5
  • 24
    • 0035921170 scopus 로고    scopus 로고
    • Effect of crown ethers on structure, stability, activity, and enantioselectivity of subtilisin Carlsberg in organic solvents
    • Santos A.M., Vidal M., Pacheco Y., Frontera J., Báez C., Ornellas O., Barletta G., Griebenow K. Effect of crown ethers on structure, stability, activity, and enantioselectivity of subtilisin Carlsberg in organic solvents. Biotechnol Bioeng. 74:2001;295-308.
    • (2001) Biotechnol Bioeng , vol.74 , pp. 295-308
    • Santos, A.M.1    Vidal, M.2    Pacheco, Y.3    Frontera, J.4    Báez, C.5    Ornellas, O.6    Barletta, G.7    Griebenow, K.8
  • 25
    • 11644249583 scopus 로고
    • Cyclodextrins and their applications in analytical chemistry
    • Li S., Purdy W.C. Cyclodextrins and their applications in analytical chemistry. Chem Rev. 92:1992;1457-1470.
    • (1992) Chem Rev , vol.92 , pp. 1457-1470
    • Li, S.1    Purdy, W.C.2
  • 26
    • 0026459045 scopus 로고
    • Effect of cyclodextrins on the thermal stability of globular proteins
    • Cooper A. Effect of cyclodextrins on the thermal stability of globular proteins. J Am Chem Soc. 114:1992;9208-9209.
    • (1992) J Am Chem Soc , vol.114 , pp. 9208-9209
    • Cooper, A.1
  • 27
    • 0035958487 scopus 로고    scopus 로고
    • Tuning lipase enantioselectivity in organic media using solid-state buffers
    • Quiros M., Parker M.-C., Turner N.J. Tuning lipase enantioselectivity in organic media using solid-state buffers. J Org Chem. 66:2001;5074-5079. By adding various acids, bases and buffers to an organic solvent, the activity and enantioselectivity of C. antarctica and M. miehei lipases on ionic substrates can be modulated.
    • (2001) J Org Chem , vol.66 , pp. 5074-5079
    • Quiros, M.1    Parker, M.-C.2    Turner, N.J.3
  • 28
    • 0033553149 scopus 로고    scopus 로고
    • Markedly enhancing enzymatic enantioselectivity in organic solvents by forming substrate salts
    • Ke T., Klibanov A.M. Markedly enhancing enzymatic enantioselectivity in organic solvents by forming substrate salts. J Am Chem Soc. 121:1999;3334-3340.
    • (1999) J Am Chem Soc , vol.121 , pp. 3334-3340
    • Ke, T.1    Klibanov, A.M.2
  • 29
    • 0034609593 scopus 로고    scopus 로고
    • Improving lipase enantioselectivity in organic solvents by forming substrate salts with chiral agents
    • Shin J.-S., Luque S., Klibanov A.M. Improving lipase enantioselectivity in organic solvents by forming substrate salts with chiral agents. Biotechnol Bioeng. 69:2000;577-583. A simple technique of forming a salt between a racemic ionic substrate and a bulky organic chiral counterion results in the dramatic improvement in the enantioselectivity of P. cepacia-catalyzed transesterification reactions. Structure-based molecular modeling of this effect was performed to show that the results can be explained by the formation of specific diasteriomers.
    • (2000) Biotechnol Bioeng , vol.69 , pp. 577-583
    • Shin, J.-S.1    Luque, S.2    Klibanov, A.M.3
  • 30
    • 0037028543 scopus 로고    scopus 로고
    • Binding of hydrophobic hydroxamic acids enhances peroxidase's stereoselectivity in nonaqueous sulfoxidations
    • Das P.K., Caaveiro J.M.M., Luque S., Klibanov A.M. Binding of hydrophobic hydroxamic acids enhances peroxidase's stereoselectivity in nonaqueous sulfoxidations. J Am Chem Soc. 124:2002;782-787. This interesting paper describes the simple transformation of an inherently non-stereoselective enzyme, HRP, into one with respectable enantioselectivity. By performing the sulfoxidation reaction in the presence of hydroxamic acids the formation of one enantiomer is inhibited more effectively than another, resulting in enhanced observed enantioselectivity.
    • (2002) J Am Chem Soc , vol.124 , pp. 782-787
    • Das, P.K.1    Caaveiro, J.M.M.2    Luque, S.3    Klibanov, A.M.4
  • 31
    • 0033578312 scopus 로고    scopus 로고
    • Striking activation of oxidative enzymes suspended in nonaqueous media
    • Dai L., Klibanov A.M. Striking activation of oxidative enzymes suspended in nonaqueous media. Proc Natl Acad Sci USA. 96:1999;9475-9478.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9475-9478
    • Dai, L.1    Klibanov, A.M.2
  • 32
    • 0033835404 scopus 로고    scopus 로고
    • Myoglobin-catalyzed epoxidation of styrene in organic solvents accelerated by bioimprinting
    • Ozawa S., Klibanov A.M. Myoglobin-catalyzed epoxidation of styrene in organic solvents accelerated by bioimprinting. Biotechnol Lett. 22:2000;1269-1272.
    • (2000) Biotechnol Lett , vol.22 , pp. 1269-1272
    • Ozawa, S.1    Klibanov, A.M.2
  • 33
    • 0034632430 scopus 로고    scopus 로고
    • Enhancing the enantioselectivity of lipase in transesterification by substrate matching: An enzyme memory based approach
    • Lee D., Choi Y.K., Kim M.J. Enhancing the enantioselectivity of lipase in transesterification by substrate matching: an enzyme memory based approach. Org Lett. 2:2000;2553-2555. By combining the principles of molecular imprinting with transesterification, the authors demonstrate that acyl donors and acceptors that are structurally similar are more selective than structurally dissimilar donor-acceptor pairs. This effect was rationalized by assuming that a lipase follows ping-pong kinetics and that the acyl donor assists in the formation of a cavity in the binding pocket of the enzyme that is structurally similar to the acyl acceptor. The result is better acyl acceptor binding, giving increased activity and enantioselectivity.
    • (2000) Org Lett , vol.2 , pp. 2553-2555
    • Lee, D.1    Choi, Y.K.2    Kim, M.J.3
  • 34
    • 0037094133 scopus 로고    scopus 로고
    • Molecular imprinting of enzymes with water-insoluble ligands for nonaqueous biocatalysis
    • Rich J.O., Mozhaev V.V., Dordick J.S., Clark D.S., Khmelnitsky Y.L. Molecular imprinting of enzymes with water-insoluble ligands for nonaqueous biocatalysis. J Am Chem Soc. 124:2002;5244-5245.
    • (2002) J Am Chem Soc , vol.124 , pp. 5244-5245
    • Rich, J.O.1    Mozhaev, V.V.2    Dordick, J.S.3    Clark, D.S.4    Khmelnitsky, Y.L.5
  • 35
    • 0035820418 scopus 로고    scopus 로고
    • Activation of enzymes for nonaqueous biocatalysis by denaturing concentrations of urea
    • Guo Y., Clark D.S. Activation of enzymes for nonaqueous biocatalysis by denaturing concentrations of urea. Biochim Biophys Acta. 1546:2001;406-411. Enzymes lyophilized from denaturing concentrations of urea are substantially more reactive in organic media than their untreated counterparts. HRP was up to 350-fold more reactive after lyophilization from an 8 M urea solution, and this was hypothesized to be due to a slight unfolding of the protein enabling it to be less rigid in the organic solvent, ultimately leading to higher catalytic activity.
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 406-411
    • Guo, Y.1    Clark, D.S.2
  • 36
    • 0027962947 scopus 로고
    • Aqueous-like activity of α-chymotrypsin dissolved in nearly anhydrous organic solvents
    • Paradkar V.M., Dordick J.S. Aqueous-like activity of α-chymotrypsin dissolved in nearly anhydrous organic solvents. J Am Chem Soc. 116:1994;5009-5010.
    • (1994) J Am Chem Soc , vol.116 , pp. 5009-5010
    • Paradkar, V.M.1    Dordick, J.S.2
  • 37
    • 0031081342 scopus 로고    scopus 로고
    • Lipid-coated enzymes as efficient catalysts in organic media
    • Okahata Y., Mori T. Lipid-coated enzymes as efficient catalysts in organic media. Trends Biotechnol. 15:1997;50-54.
    • (1997) Trends Biotechnol , vol.15 , pp. 50-54
    • Okahata, Y.1    Mori, T.2
  • 38
    • 0036129497 scopus 로고    scopus 로고
    • Protein-containing hydrophobic coatings and films
    • Novick S.J., Dordick J.S. Protein-containing hydrophobic coatings and films. Biomaterials. 23:2002;441-448.
    • (2002) Biomaterials , vol.23 , pp. 441-448
    • Novick, S.J.1    Dordick, J.S.2
  • 39
    • 0035648023 scopus 로고    scopus 로고
    • A dramatic improvement of enantioselectivity of lipase in organic solvents by addition of aqueous SDS: A close correlation between enantioselectivity and conformational flexibility of lipase
    • Ueji S, Nishimura M, Kudo R, Matsumi R, Watanabe K, Ebara Y: A dramatic improvement of enantioselectivity of lipase in organic solvents by addition of aqueous SDS: a close correlation between enantioselectivity and conformational flexibility of lipase. Chem Lett 2001, 912-913.
    • (2001) Chem Lett , pp. 912-913
    • Ueji, S.1    Nishimura, M.2    Kudo, R.3    Matsumi, R.4    Watanabe, K.5    Ebara, Y.6
  • 40
    • 0034727946 scopus 로고    scopus 로고
    • Lipase-catalyzed reactions in ionic liquids
    • Lau R.M., van Rantwijk F., Seddon K.R., Sheldon R.A. Lipase-catalyzed reactions in ionic liquids. Org Lett. 2:2000;4189-4191. A series of C. antarctica lipase-catalyzed reactions were performed in different ionic media, including transesterification and aminolysis of fatty acid esters.
    • (2000) Org Lett , vol.2 , pp. 4189-4191
    • Lau, R.M.1    Van Rantwijk, F.2    Seddon, K.R.3    Sheldon, R.A.4
  • 41
    • 0035819970 scopus 로고    scopus 로고
    • Enzyme catalysis in ionic liquids: Lipase catalyzed kinetic resolution of 1-phenylethanol with improved enantioselectivity
    • Schofer SH, Kaftzik N, Wasserscheid P, Kragl U: Enzyme catalysis in ionic liquids: lipase catalyzed kinetic resolution of 1-phenylethanol with improved enantioselectivity. Chem Commun 2001: 425-426. A total of 11 lipases and esterases were screened for their reactivity in ten ionic liquids for the enantioselective transesterification of 1-phenylethanol with vinyl acetate. High reaction conversions and enantioselectivity were obtained with lipase from C. antarctica and porcine pancreas.
    • (2001) Chem Commun , pp. 425-426
    • Schofer, S.H.1    Kaftzik, N.2    Wasserscheid, P.3    Kragl, U.4
  • 42
    • 0034524760 scopus 로고    scopus 로고
    • Enzymatic catalysis of formation of Z-aspartame in ionic liquid: An alternative to enzymatic catalysis in organic solvents
    • Erbeldinger M., Mesiano A.J., Russell A.J. Enzymatic catalysis of formation of Z-aspartame in ionic liquid: an alternative to enzymatic catalysis in organic solvents. Biotechnol Prog. 16:2001;1129-1131.
    • (2001) Biotechnol Prog , vol.16 , pp. 1129-1131
    • Erbeldinger, M.1    Mesiano, A.J.2    Russell, A.J.3
  • 43
    • 0035861716 scopus 로고    scopus 로고
    • Improved preparation and use of room temperature ionic liquids in lipase-catalyzed enantio- and regioselective acylations
    • 4 were formed in 99% yield, of which 93% was the desired 6-O-acetyl glucose. This is far more regioselective for the 6-ester than that found in more conventional organic solvents. Furthermore, using the Reichardt's polarity index, the authors demonstrated that the ionic liquids support catalytic activity at polarity levels far higher than organic solvents. Hence, reactions that require highly polar media (e.g. sugar acylation) are more effective in ionic liquids than organic solvents.
    • (2001) J Org Chem , vol.66 , pp. 8395-8401
    • Park, S.S.1    Kazlauskas, R.J.2
  • 44
    • 0036525716 scopus 로고    scopus 로고
    • Lipases as practical biocatalysts
    • Reetz M. Lipases as practical biocatalysts. Curr Opin Chem Biol. 6:2002;145-150.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 145-150
    • Reetz, M.1
  • 45
    • 0035927926 scopus 로고    scopus 로고
    • Enzyme-coated micro-crystals: A 1-step method for high activity biocatalyst preparation
    • 4) into a polar organic solvent that is heavily agitated results in the formation of enzyme particles as small as 100 nm, which are highly active in organic media for transesterification reactions. These micro-crystals are extremely stable, with storage stability of greater than 14 months.
    • (2001) Chem Commun , pp. 1096-1097
    • Kreiner, M.1    Moore, B.D.2    Parker, M.C.3
  • 46
    • 0036525713 scopus 로고    scopus 로고
    • Protein engineering of oxygenases for biocatalysis
    • Cirino P.C., Arnold F.H. Protein engineering of oxygenases for biocatalysis. Curr Opin Chem Biol. 6:2002;130-135.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 130-135
    • Cirino, P.C.1    Arnold, F.H.2


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