메뉴 건너뛰기




Volumn 3, Issue 7, 2015, Pages 1589-1599

Papain@Magnetic Nanocrystalline Cellulose Nanobiocatalyst: A Highly Efficient Biocatalyst for Dipeptide Biosynthesis in Deep Eutectic Solvents

Author keywords

Deep eutectic solvent; Dipiptide; Green chemistry; Magnetic nanoparticle; Nanocrystalline cellulose; Protease; Sustainable chemistry

Indexed keywords

AMINO ACIDS; BIOCATALYSTS; BIOCHEMISTRY; BIOSYNTHESIS; CELLULOSE; CELLULOSE DERIVATIVES; CHLORINE COMPOUNDS; ENZYME ACTIVITY; ENZYMES; EUTECTICS; IONIC LIQUIDS; MAGNETISM; NANOPARTICLES; PAPAIN; PEPTIDES; SOLVENTS; UREA;

EID: 84936776924     PISSN: None     EISSN: 21680485     Source Type: Journal    
DOI: 10.1021/acssuschemeng.5b00290     Document Type: Article
Times cited : (94)

References (59)
  • 1
    • 84864415350 scopus 로고    scopus 로고
    • A novel approach for efficient immobilization and stabilization of papain on magnetic gold nanocomposites
    • Sahoo, B.; Sahu, S. K.; Bhattacharya, D.; Dhara, D.; Pramanik, P. A novel approach for efficient immobilization and stabilization of papain on magnetic gold nanocomposites Colloids Surf., B. Biointerfaces 2013, 101, 280-289
    • (2013) Colloids Surf., B. Biointerfaces , vol.101 , pp. 280-289
    • Sahoo, B.1    Sahu, S.K.2    Bhattacharya, D.3    Dhara, D.4    Pramanik, P.5
  • 2
    • 33747311893 scopus 로고    scopus 로고
    • Catalytic conversion of cellulose into sugar alcohols
    • Fukuoka, A.; Dhepe, P. L. Catalytic conversion of cellulose into sugar alcohols Angew. Chem., Int. Ed. 2006, 45, 5161-5163
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 5161-5163
    • Fukuoka, A.1    Dhepe, P.L.2
  • 3
    • 84858081092 scopus 로고    scopus 로고
    • Direct conversion of cellulose and lignocellulosic biomass into chemicals and biofuel with metal chloride catalysts
    • Dutta, S.; De, S.; Alam, M. I.; Abu-Omar, M. M.; Saha, B. Direct conversion of cellulose and lignocellulosic biomass into chemicals and biofuel with metal chloride catalysts J. Catal. 2012, 288, 8-15
    • (2012) J. Catal. , vol.288 , pp. 8-15
    • Dutta, S.1    De, S.2    Alam, M.I.3    Abu-Omar, M.M.4    Saha, B.5
  • 4
    • 68949093960 scopus 로고    scopus 로고
    • Cellulose modification by polymer grafting: A review
    • Roy, D.; Semsarilar, M.; Guthrie, J. T.; Perrier, S. Cellulose modification by polymer grafting: A review Chem. Soc. Rev. 2009, 38, 2046-2064
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2046-2064
    • Roy, D.1    Semsarilar, M.2    Guthrie, J.T.3    Perrier, S.4
  • 5
    • 84862256427 scopus 로고    scopus 로고
    • Comparing microcrystalline with spherical nanocrystalline cellulose from waste cotton fabrics
    • Xiong, R.; Zhang, X. X.; Tian, D.; Zhou, Z. H.; Lu, C. H. Comparing microcrystalline with spherical nanocrystalline cellulose from waste cotton fabrics Cellulose 2012, 19, 1189-1198
    • (2012) Cellulose , vol.19 , pp. 1189-1198
    • Xiong, R.1    Zhang, X.X.2    Tian, D.3    Zhou, Z.H.4    Lu, C.H.5
  • 6
    • 77953296073 scopus 로고    scopus 로고
    • Cellulose nanocrystals: Chemistry, self-assembly, and applications
    • Habibi, Y.; Lucia, L. A.; Rojas, O. J. Cellulose nanocrystals: Chemistry, self-assembly, and applications Chem. Rev. 2010, 110, 3479
    • (2010) Chem. Rev. , vol.110 , pp. 3479
    • Habibi, Y.1    Lucia, L.A.2    Rojas, O.J.3
  • 7
    • 84872337879 scopus 로고    scopus 로고
    • Nanocomposites of nanocrystalline cellulose for enzyme immobilization
    • Incani, V.; Danumah, C.; Boluk, Y. Nanocomposites of nanocrystalline cellulose for enzyme immobilization Cellulose 2013, 20, 191-200
    • (2013) Cellulose , vol.20 , pp. 191-200
    • Incani, V.1    Danumah, C.2    Boluk, Y.3
  • 8
    • 45949097954 scopus 로고    scopus 로고
    • Peroxidase conjugate of cellulose nanocrystals for the removal of chlorinated phenolic compounds in aqueous solution
    • Yang, R.; Tan, H.; Wei, F.; Wang, S. Peroxidase conjugate of cellulose nanocrystals for the removal of chlorinated phenolic compounds in aqueous solution Biotechnology 2008, 7, 233-241
    • (2008) Biotechnology , vol.7 , pp. 233-241
    • Yang, R.1    Tan, H.2    Wei, F.3    Wang, S.4
  • 9
    • 84857356498 scopus 로고    scopus 로고
    • Immobilization of lysozyme-cellulose amide-linked conjugates on cellulose i and II cotton nanocrystalline preparations
    • Edwards, J. V.; Prevost, N. T.; Condon, B.; French, A.; Wu, Q. Immobilization of lysozyme-cellulose amide-linked conjugates on cellulose I and II cotton nanocrystalline preparations Cellulose 2012, 19, 495-506
    • (2012) Cellulose , vol.19 , pp. 495-506
    • Edwards, J.V.1    Prevost, N.T.2    Condon, B.3    French, A.4    Wu, Q.5
  • 10
    • 84905728355 scopus 로고    scopus 로고
    • Preparation of a novel magnetic cellulose nanocrystal and its efficient use for enzyme immobilization
    • Cao, S.-L.; Li, X.-H.; Lou, W.-Y.; Zong, M.-H. Preparation of a novel magnetic cellulose nanocrystal and its efficient use for enzyme immobilization J. Mater. Chem. B 2014, 2, 5522-5530
    • (2014) J. Mater. Chem. B , vol.2 , pp. 5522-5530
    • Cao, S.-L.1    Li, X.-H.2    Lou, W.-Y.3    Zong, M.-H.4
  • 11
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: From research to food applications
    • Hartmann, R.; Meisel, H. Food-derived peptides with biological activity: From research to food applications Curr. Opin. Biotechnol. 2007, 18, 163-169
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 12
    • 0038050529 scopus 로고    scopus 로고
    • Interorgan amino acid transport and its regulation
    • Brosnan, J. T. Interorgan amino acid transport and its regulation J. Nutr. 2003, 133, 2068S-2072S
    • (2003) J. Nutr. , vol.133 , pp. 2068S-2072S
    • Brosnan, J.T.1
  • 13
    • 83755228545 scopus 로고    scopus 로고
    • Kinetically controlled enzymatic synthesis of dipeptide precursor of l -alanyl- l -glutamine
    • Wang, M.; Qi, W.; Yu, Q.; Su, R.; He, Z. Kinetically controlled enzymatic synthesis of dipeptide precursor of l -alanyl- l -glutamine Biotechnol. Appl. Biochem. 2011, 58, 449-455
    • (2011) Biotechnol. Appl. Biochem. , vol.58 , pp. 449-455
    • Wang, M.1    Qi, W.2    Yu, Q.3    Su, R.4    He, Z.5
  • 14
    • 54349118620 scopus 로고    scopus 로고
    • Synthesis and application of dipeptides; Current status and perspectives
    • Yagasaki, M.; Hashimoto, S. Synthesis and application of dipeptides; Current status and perspectives Appl. Microbiol. Biotechnol. 2008, 81, 13-22
    • (2008) Appl. Microbiol. Biotechnol. , vol.81 , pp. 13-22
    • Yagasaki, M.1    Hashimoto, S.2
  • 15
    • 0033822104 scopus 로고    scopus 로고
    • A thirty-year odyssey in nitrogen metabolism: From ammonium to dipeptides
    • Furst, P. A thirty-year odyssey in nitrogen metabolism: From ammonium to dipeptides J. Parenter. Enteral Nutr. 2000, 24, 197-209
    • (2000) J. Parenter. Enteral Nutr. , vol.24 , pp. 197-209
    • Furst, P.1
  • 17
    • 84907104280 scopus 로고    scopus 로고
    • Recent advances in chemoenzymatic peptide syntheses
    • Yazawa, K.; Numata, K. Recent advances in chemoenzymatic peptide syntheses Molecules 2014, 19, 13755-13774
    • (2014) Molecules , vol.19 , pp. 13755-13774
    • Yazawa, K.1    Numata, K.2
  • 19
    • 69349091133 scopus 로고    scopus 로고
    • Catalytic activity of A-chymotrypsin in enzymatic peptide synthesis in ionic liquids
    • Noritomi, H.; Suzuki, K.; Kikuta, M.; Kato, S. Catalytic activity of A-chymotrypsin in enzymatic peptide synthesis in ionic liquids Biochem. Eng. J. 2009, 47, 27-30
    • (2009) Biochem. Eng. J. , vol.47 , pp. 27-30
    • Noritomi, H.1    Suzuki, K.2    Kikuta, M.3    Kato, S.4
  • 20
    • 55949096748 scopus 로고    scopus 로고
    • Protease-catalyzed dipeptide synthesis from N-protected amino acid carbamoylmethyl esters and free amino acids in frozen aqueous solutions
    • Salam, S. M. A.; Kagawa, K.-i.; Matsubara, T.; Kawashiro, K. Protease-catalyzed dipeptide synthesis from N-protected amino acid carbamoylmethyl esters and free amino acids in frozen aqueous solutions Enzyme Microb. Technol. 2008, 43, 537-543
    • (2008) Enzyme Microb. Technol. , vol.43 , pp. 537-543
    • Salam, S.M.A.1    Kagawa, K.-I.2    Matsubara, T.3    Kawashiro, K.4
  • 23
    • 84876088474 scopus 로고    scopus 로고
    • Deep eutectic solvents: Synthesis, application, and focus on lipase-catalyzed reactions
    • Durand, E.; Lecomte, J.; Villeneuve, P. Deep eutectic solvents: Synthesis, application, and focus on lipase-catalyzed reactions Eur. J. Lipid Sci. Technol. 2013, 115, 379-385
    • (2013) Eur. J. Lipid Sci. Technol. , vol.115 , pp. 379-385
    • Durand, E.1    Lecomte, J.2    Villeneuve, P.3
  • 24
    • 33645891642 scopus 로고    scopus 로고
    • Optimization of the isolation of nanocrystals from microcrystalline cellulose by acid hydrolysis
    • Bondeson, D.; Mathew, A.; Oksman, K. Optimization of the isolation of nanocrystals from microcrystalline cellulose by acid hydrolysis Cellulose 2006, 13, 171-180
    • (2006) Cellulose , vol.13 , pp. 171-180
    • Bondeson, D.1    Mathew, A.2    Oksman, K.3
  • 25
    • 84905728355 scopus 로고    scopus 로고
    • Preparation of novel magnetic cellulose nanocrystals via in-situ co-precipitation-electrostatic self-assembly technique and its efficient use for enzyme immobilization
    • Cao, S. L.; Lou, W. Y.; Zong, M. H. Preparation of novel magnetic cellulose nanocrystals via in-situ co-precipitation-electrostatic self-assembly technique and its efficient use for enzyme immobilization J. Mater. Chem. B 2014, 2, 5522-5530
    • (2014) J. Mater. Chem. B , vol.2 , pp. 5522-5530
    • Cao, S.L.1    Lou, W.Y.2    Zong, M.H.3
  • 26
    • 84863921269 scopus 로고    scopus 로고
    • A facile synthesis of cysteine-ferrite magnetic nanoparticles for application in multicomponent reactions - A sustainable protocol
    • Gawande, M. B.; Velhinho, A.; Nogueira, I. D.; Ghumman, C.; Teodoro, O.; Branco, P. S. A facile synthesis of cysteine-ferrite magnetic nanoparticles for application in multicomponent reactions-A sustainable protocol RSC Adv. 2012, 2, 6144-6149
    • (2012) RSC Adv. , vol.2 , pp. 6144-6149
    • Gawande, M.B.1    Velhinho, A.2    Nogueira, I.D.3    Ghumman, C.4    Teodoro, O.5    Branco, P.S.6
  • 27
    • 66449110019 scopus 로고    scopus 로고
    • Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins
    • Nissen, M. S.; Kumar, G. M.; Youn, B.; Knowles, D. B.; Lam, K. S.; Ballinger, W. J.; Knowles, N. R.; Kang, C. Characterization of Solanum tuberosum multicystatin and its structural comparison with other cystatins Plant Cell 2009, 21, 861-875
    • (2009) Plant Cell , vol.21 , pp. 861-875
    • Nissen, M.S.1    Kumar, G.M.2    Youn, B.3    Knowles, D.B.4    Lam, K.S.5    Ballinger, W.J.6    Knowles, N.R.7    Kang, C.8
  • 29
    • 79751517209 scopus 로고    scopus 로고
    • Characteristics and properties of carboxylated cellulose nanocrystals prepared from a novel one-step procedure
    • Leung, A. C.; Hrapovic, S.; Lam, E.; Liu, Y.; Male, K. B.; Mahmoud, K. A.; Luong, J. H. Characteristics and properties of carboxylated cellulose nanocrystals prepared from a novel one-step procedure Small 2011, 7, 302-305
    • (2011) Small , vol.7 , pp. 302-305
    • Leung, A.C.1    Hrapovic, S.2    Lam, E.3    Liu, Y.4    Male, K.B.5    Mahmoud, K.A.6    Luong, J.H.7
  • 30
    • 84863886392 scopus 로고    scopus 로고
    • Biocompatible magnetic cellulose-chitosan hybrid gel microspheres reconstituted from ionic liquids for enzyme immobilization
    • Liu, Z.; Wang, H.; Li, B.; Liu, C.; Jiang, Y.; Yu, G.; Mu, X. Biocompatible magnetic cellulose-chitosan hybrid gel microspheres reconstituted from ionic liquids for enzyme immobilization J. Mater. Chem. 2012, 22, 15085-15091
    • (2012) J. Mater. Chem. , vol.22 , pp. 15085-15091
    • Liu, Z.1    Wang, H.2    Li, B.3    Liu, C.4    Jiang, Y.5    Yu, G.6    Mu, X.7
  • 32
    • 0033885445 scopus 로고    scopus 로고
    • X-ray diffractometric study of microcrystallite size of naturally colored cottons
    • Chen, H.-L.; Yokochi, A. X-ray diffractometric study of microcrystallite size of naturally colored cottons J. Appl. Polym. Sci. 2000, 76, 1466-1471
    • (2000) J. Appl. Polym. Sci. , vol.76 , pp. 1466-1471
    • Chen, H.-L.1    Yokochi, A.2
  • 33
    • 7044229930 scopus 로고    scopus 로고
    • Preparation and antibacterial activity of chitosan nanoparticles
    • Qi, L.; Xu, Z.; Jiang, X.; Hu, C.; Zou, X. Preparation and antibacterial activity of chitosan nanoparticles Carbohydr. Res. 2004, 339, 2693-2700
    • (2004) Carbohydr. Res. , vol.339 , pp. 2693-2700
    • Qi, L.1    Xu, Z.2    Jiang, X.3    Hu, C.4    Zou, X.5
  • 34
    • 33947177073 scopus 로고    scopus 로고
    • Preparation of hydrophilic magnetic nanospheres with high saturation magnetization
    • Xu, H.; Tong, N.; Cui, L.; Lu, Y.; Gu, H. Preparation of hydrophilic magnetic nanospheres with high saturation magnetization J. Magn. Magn. Mater. 2007, 311, 125-130
    • (2007) J. Magn. Magn. Mater. , vol.311 , pp. 125-130
    • Xu, H.1    Tong, N.2    Cui, L.3    Lu, Y.4    Gu, H.5
  • 35
    • 52949087492 scopus 로고    scopus 로고
    • Chitosan-induced synthesis of magnetite nanoparticles via iron ions assembly
    • Wang, Y.; Li, B.; Zhou, Y.; Jia, D. Chitosan-induced synthesis of magnetite nanoparticles via iron ions assembly Polym. Adv. Technol. 2008, 19, 1256-1261
    • (2008) Polym. Adv. Technol. , vol.19 , pp. 1256-1261
    • Wang, Y.1    Li, B.2    Zhou, Y.3    Jia, D.4
  • 36
    • 76249107786 scopus 로고    scopus 로고
    • Biobased nanocomposites from layer-by-layer assembly of cellulose nanowhiskers with chitosan
    • de Mesquita, J. P.; Donnici, C. L.; Pereira, F. V. Biobased nanocomposites from layer-by-layer assembly of cellulose nanowhiskers with chitosan Biomacromolecules 2010, 11, 473-480
    • (2010) Biomacromolecules , vol.11 , pp. 473-480
    • De Mesquita, J.P.1    Donnici, C.L.2    Pereira, F.V.3
  • 37
    • 84879095331 scopus 로고    scopus 로고
    • Preparation of well-dispersed gold/magnetite nanoparticles embedded on cellulose nanocrystals for efficient immobilization of papain enzyme
    • Mahmoud, K. A.; Lam, E.; Hrapovic, S.; Luong, J. H. Preparation of well-dispersed gold/magnetite nanoparticles embedded on cellulose nanocrystals for efficient immobilization of papain enzyme ACS Appl. Mater. Interfaces 2013, 5, 4978-4985
    • (2013) ACS Appl. Mater. Interfaces , vol.5 , pp. 4978-4985
    • Mahmoud, K.A.1    Lam, E.2    Hrapovic, S.3    Luong, J.H.4
  • 38
    • 38049085641 scopus 로고    scopus 로고
    • Preparation of cross-linked tyrosinase aggregates
    • Aytar, B. S.; Bakir, U. Preparation of cross-linked tyrosinase aggregates Process Biochem. 2008, 43, 125-131
    • (2008) Process Biochem. , vol.43 , pp. 125-131
    • Aytar, B.S.1    Bakir, U.2
  • 39
    • 78649906228 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis
    • Kumar, S.; Mohan, U.; Kamble, A. L.; Pawar, S.; Banerjee, U. C. Cross-linked enzyme aggregates of recombinant Pseudomonas putida nitrilase for enantioselective nitrile hydrolysis Bioresour. Technol. 2010, 101, 6856-6858
    • (2010) Bioresour. Technol. , vol.101 , pp. 6856-6858
    • Kumar, S.1    Mohan, U.2    Kamble, A.L.3    Pawar, S.4    Banerjee, U.C.5
  • 42
    • 77957958242 scopus 로고    scopus 로고
    • Cross-linking enzyme aggregates in the macropores of silica gel: A practical and efficient method for enzyme stabilization
    • Wang, M.; Qi, W.; Yu, Q.; Su, R.; He, Z. Cross-linking enzyme aggregates in the macropores of silica gel: A practical and efficient method for enzyme stabilization Biochem. Eng. J. 2010, 52, 168-174
    • (2010) Biochem. Eng. J. , vol.52 , pp. 168-174
    • Wang, M.1    Qi, W.2    Yu, Q.3    Su, R.4    He, Z.5
  • 43
    • 2942541288 scopus 로고    scopus 로고
    • The preparation and catalytically active characterization of papain immobilized on magnetic composite microspheres
    • Lei, H.; Wang, W.; Chen, L. L.; Li, X. C.; Yi, B.; Deng, L. The preparation and catalytically active characterization of papain immobilized on magnetic composite microspheres Enzyme Microb. Technol. 2004, 35, 15-21
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 15-21
    • Lei, H.1    Wang, W.2    Chen, L.L.3    Li, X.C.4    Yi, B.5    Deng, L.6
  • 44
    • 0142258126 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups
    • Chiou, S.-H.; Wu, W.-T. Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups Biomaterials 2004, 25, 197-204
    • (2004) Biomaterials , vol.25 , pp. 197-204
    • Chiou, S.-H.1    Wu, W.-T.2
  • 45
    • 50049088751 scopus 로고    scopus 로고
    • Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications
    • Sangeetha, K.; Emilia Abraham, T. Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications Int. J. Biol. Macromol. 2008, 43, 314-319
    • (2008) Int. J. Biol. Macromol. , vol.43 , pp. 314-319
    • Sangeetha, K.1    Emilia Abraham, T.2
  • 46
    • 84878200842 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of mung bean epoxide hydrolases: A highly active, stable and recyclable biocatalyst for asymmetric hydrolysis of epoxides
    • Yu, C.-Y.; Li, X.-F.; Lou, W.-Y.; Zong, M.-H. Cross-linked enzyme aggregates of mung bean epoxide hydrolases: A highly active, stable and recyclable biocatalyst for asymmetric hydrolysis of epoxides J. Biotechnol. 2013, 166, 12-19
    • (2013) J. Biotechnol. , vol.166 , pp. 12-19
    • Yu, C.-Y.1    Li, X.-F.2    Lou, W.-Y.3    Zong, M.-H.4
  • 47
    • 84907879493 scopus 로고    scopus 로고
    • One-pot synthesis of protein-embedded metal-organic frameworks with enhanced biological activities
    • Lyu, F.; Zhang, Y.; Zare, R. N.; Ge, J.; Liu, Z. One-pot synthesis of protein-embedded metal-organic frameworks with enhanced biological activities Nano Lett. 2014, 14, 5761-5765
    • (2014) Nano Lett. , vol.14 , pp. 5761-5765
    • Lyu, F.1    Zhang, Y.2    Zare, R.N.3    Ge, J.4    Liu, Z.5
  • 48
    • 84857509026 scopus 로고    scopus 로고
    • Immobilization of α-amylase from locale bacteria isolate Bacillus subtilis ITBCCB148 with carboxymethyl cellulose (CM-cellulose)
    • Susanti, D.; Suhartati, T.; Hadi, S. Immobilization of α-amylase from locale bacteria isolate Bacillus subtilis ITBCCB148 with carboxymethyl cellulose (CM-cellulose). Modern Appl. Sci., 2012, 6.
    • (2012) Modern Appl. Sci. , vol.6
    • Susanti, D.1    Suhartati, T.2    Hadi, S.3
  • 50
    • 0028944301 scopus 로고
    • Second derivative infrared spectroscopy as a non-destructive tool to assess the purity and structural integrity of proteins
    • Byler, D. M.; Wilson, R. M.; Randall, C. S.; Sokoloski, T. D. Second derivative infrared spectroscopy as a non-destructive tool to assess the purity and structural integrity of proteins Pharm. Res. 1995, 12, 446-450
    • (1995) Pharm. Res. , vol.12 , pp. 446-450
    • Byler, D.M.1    Wilson, R.M.2    Randall, C.S.3    Sokoloski, T.D.4
  • 51
    • 12844274977 scopus 로고    scopus 로고
    • Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy
    • Natalello, A.; Ami, D.; Brocca, S.; Lotti, M.; Doglia, S. Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy Biochem. J. 2005, 385, 511-517
    • (2005) Biochem. J. , vol.385 , pp. 511-517
    • Natalello, A.1    Ami, D.2    Brocca, S.3    Lotti, M.4    Doglia, S.5
  • 52
    • 33744959273 scopus 로고    scopus 로고
    • Impact of ionic liquids on papain: An investigation of structure-function relationships
    • Lou, W.-Y.; Zong, M.-H.; Smith, T. J.; Wu, H.; Wang, J.-F. Impact of ionic liquids on papain: An investigation of structure-function relationships Green Chem. 2006, 8, 509-512
    • (2006) Green Chem. , vol.8 , pp. 509-512
    • Lou, W.-Y.1    Zong, M.-H.2    Smith, T.J.3    Wu, H.4    Wang, J.-F.5
  • 53
    • 0345085739 scopus 로고    scopus 로고
    • Fourier-transform infrared spectroscopy study of dehydrated lipases from Candida antarctica B and Pseudomonas cepacia
    • Vecchio, G.; Zambianchi, F.; Zacchetti, P.; Secundo, F.; Carrea, G. Fourier-transform infrared spectroscopy study of dehydrated lipases from Candida antarctica B and Pseudomonas cepacia Biotechnol. Bioeng. 1999, 64, 545-551
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 545-551
    • Vecchio, G.1    Zambianchi, F.2    Zacchetti, P.3    Secundo, F.4    Carrea, G.5
  • 54
    • 33847308554 scopus 로고    scopus 로고
    • Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography
    • Collins, M. D.; Quillin, M. L.; Hummer, G.; Matthews, B. W.; Gruner, S. M. Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography J. Mol. Biol. 2007, 367, 752-763
    • (2007) J. Mol. Biol. , vol.367 , pp. 752-763
    • Collins, M.D.1    Quillin, M.L.2    Hummer, G.3    Matthews, B.W.4    Gruner, S.M.5
  • 55
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks, A.; Klibanov, A. M. Enzymatic catalysis in nonaqueous solvents J. Biol. Chem. 1988, 263, 3194-3201
    • (1988) J. Biol. Chem. , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 56
    • 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 2001, 409, 241-246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 57
    • 0031662567 scopus 로고    scopus 로고
    • Structure, function and stability of enzymes from the archaea
    • Danson, M. J.; Hough, D. W. Structure, function and stability of enzymes from the archaea Trends Microbiol. 1998, 6, 307-314
    • (1998) Trends Microbiol. , vol.6 , pp. 307-314
    • Danson, M.J.1    Hough, D.W.2
  • 58
    • 84879881396 scopus 로고    scopus 로고
    • Chymotrypsin-catalyzed peptide synthesis in deep eutectic solvents
    • Maugeri, Z.; Leitner, W.; de Maria, P. D. Chymotrypsin-catalyzed peptide synthesis in deep eutectic solvents Eur. J. Org. Chem. 2013, 2013, 4223-4228
    • (2013) Eur. J. Org. Chem. , vol.2013 , pp. 4223-4228
    • Maugeri, Z.1    Leitner, W.2    De Maria, P.D.3
  • 59
    • 0036787578 scopus 로고    scopus 로고
    • Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature
    • Otzen, D. E. Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature Biophys. J. 2002, 83, 2219-2230
    • (2002) Biophys. J. , vol.83 , pp. 2219-2230
    • Otzen, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.