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Volumn 46, Issue 4, 2011, Pages 1029-1034

Performance improvement of araujiain, a cystein phytoprotease, by immobilization within calcium alginate beads

Author keywords

Alginate beads; Araujiain; Cystein phytoprotease; Enzymatic peptide synthesis; Immobilization

Indexed keywords

ALGINATE BEADS; ARAUJIAIN; CYSTEIN PHYTOPROTEASE; ENZYMATIC PEPTIDE SYNTHESIS; IMMOBILIZATION;

EID: 79952283769     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.01.012     Document Type: Article
Times cited : (50)

References (35)
  • 1
    • 0036882398 scopus 로고    scopus 로고
    • Proteases in organic synthesis
    • F. Bordusa Proteases in organic synthesis Chem Rev 102 2002 4817 4867
    • (2002) Chem Rev , vol.102 , pp. 4817-4867
    • Bordusa, F.1
  • 5
    • 33947602594 scopus 로고    scopus 로고
    • Improvement of enzyme activity, stability and selectivity via immobilization techniques
    • DOI 10.1016/j.enzmictec.2007.01.018, PII S0141022907000506
    • C. Mateo, J.M. Palomo, G. Fernandez-Lafuente, J.M. Guisan, and R. Fernandez-Lafuente Improvement of enzyme activity, stability and selectivity via immobilization techniques Enzyme Microb Technol 40 2007 1451 1463 (Pubitemid 46482654)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.6 , pp. 1451-1463
    • Mateo, C.1    Palomo, J.M.2    Fernandez-Lorente, G.3    Guisan, J.M.4    Fernandez-Lafuente, R.5
  • 6
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilisation: The quest for optimum performance
    • R.A. Sheldon Enzyme immobilisation: The quest for optimum performance Adv Synth Catal 349 2007 1289 1307
    • (2007) Adv Synth Catal , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 7
    • 0034993188 scopus 로고    scopus 로고
    • Immobilization of invertase within calcium alginate gel capsules
    • DOI 10.1016/S0032-9592(01)00146-7, PII S0032959201001467
    • A. Tanriseven, and. Dogan Immobilization of invertase within calcium alginate gel capsules Process Biochem 36 2001 1081 1083 (Pubitemid 32506306)
    • (2001) Process Biochemistry , vol.36 , Issue.11 , pp. 1081-1083
    • Tanriseven, A.1    Doan, E.2
  • 8
    • 0035119130 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase within calcium alginate gel capsules
    • DOI 10.1016/S0032-9592(00)00240-5, PII S0032959200002405
    • A. Blandino, M. Macías, and D. Cantero Immobilization of glucose oxidase within calcium alginate gel capsules Process Biochem 36 2001 601 606 (Pubitemid 32179010)
    • (2001) Process Biochemistry , vol.36 , Issue.7 , pp. 601-606
    • Blandino, A.1    Macias, M.2    Cantero, D.3
  • 9
    • 33751167596 scopus 로고    scopus 로고
    • Improved stabilization of microencapsulated Cathepsin B in harsh conditions
    • DOI 10.1016/j.enzmictec.2006.04.024, PII S014102290600216X
    • S. Sharma, A. Mittal, V.K. Gupta, and H. Singh Improved stabilization of microencapsulated cathepsin B in harsh conditions Enzyme Microb Technol 40 2007 337 342 (Pubitemid 44779791)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.2 , pp. 337-342
    • Sharma, S.1    Mittal, A.2    Gupta, V.K.3    Singh, H.4
  • 10
    • 13844320182 scopus 로고    scopus 로고
    • Optimization of lipase entrapment in Ca-alginate gel beads
    • DOI 10.1016/j.procbio.2004.08.014, PII S0032959204003693
    • K. Won, S. Kima, and K.J. Kim Optimization of lipase entrapment in Ca-alginate gel beads Process Biochem 40 2005 2149 2154 (Pubitemid 40257041)
    • (2005) Process Biochemistry , vol.40 , Issue.6 , pp. 2149-2154
    • Won, K.1    Kim, S.2    Kim, K.-J.3    Park, H.W.4    Moon, S.-J.5
  • 11
    • 27744601951 scopus 로고    scopus 로고
    • Papain entrapment in alginate beads for stability improvement and site specific delivery: Physicochemical characterization and factorial optimization using neural network modeling
    • M.G. Sankalia, R.C. Mashru, J.M. Sankalia, and V.B. Sutariya Papain entrapment in alginate beads for stability improvement and site specific delivery: physicochemical characterization and factorial optimization using neural network modeling AAPS Pharm Sci Technol 6 2005 391 397
    • (2005) AAPS Pharm Sci Technol , vol.6 , pp. 391-397
    • Sankalia, M.G.1    Mashru, R.C.2    Sankalia, J.M.3    Sutariya, V.B.4
  • 12
    • 70350502117 scopus 로고    scopus 로고
    • Immobilization of Bacillus licheniformis l-arabinose isomerase for semi-continuous l-ribulose production
    • Y.-W. Zhang, and P. Prabhu Lee J-K. Immobilization of Bacillus licheniformis l-arabinose isomerase for semi-continuous l-ribulose production Biosci Biotechnol Biochem 73 2009 2234 2239
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 2234-2239
    • Zhang, Y.-W.1    Prabhu, P.2    Lee, J-K.3
  • 13
    • 67349182377 scopus 로고    scopus 로고
    • Immobilization of Escherichia coli novablue γ- glutamyltranspeptidase in Ca-alginate-k-carrageenan beads
    • C.-P. Hung, H.-F. Lo, W.-H. Hsu, Chen S-Ch, and L.-L. Lin Immobilization of Escherichia coli novablue γ-glutamyltranspeptidase in Ca-alginate-k-carrageenan beads Appl Biochem Biotechnol 150 2008 157 170
    • (2008) Appl Biochem Biotechnol , vol.150 , pp. 157-170
    • Hung, C.-P.1    Lo, H.-F.2    Hsu, W.-H.3    S-Ch, C.4    Lin, L.-L.5
  • 14
    • 33746474818 scopus 로고    scopus 로고
    • Polyionic hydrocolloids for the intestinal delivery of protein drugs: Alginate and chitosan - A review
    • DOI 10.1016/j.jconrel.2006.04.017, PII S016836590600201X
    • M. George, and T.E. Abraham Polyionic hydrocolloids for the intestinal delivery of protein drugs: alginate and chitosan - a review J Controlled Release 114 2006 1 14 (Pubitemid 44131680)
    • (2006) Journal of Controlled Release , vol.114 , Issue.1 , pp. 1-14
    • George, M.1    Abraham, T.E.2
  • 15
    • 38349122721 scopus 로고    scopus 로고
    • Sodium lauryl sulfate impedes drug release from zinc-crosslinked alginate beads: Switching from enteric coating release into biphasic profiles
    • M.O. Taha, W. Nasser, A. Ardakani, and H.S. Al Khatib Sodium lauryl sulfate impedes drug release from zinc-crosslinked alginate beads: switching from enteric coating release into biphasic profiles Int J Pharm 350 2008 291 300
    • (2008) Int J Pharm , vol.350 , pp. 291-300
    • Taha, M.O.1    Nasser, W.2    Ardakani, A.3    Al Khatib, H.S.4
  • 16
    • 52849101977 scopus 로고    scopus 로고
    • Isolation and characterization of a cysteine protease from the latex of Araujia hortorum fruits
    • DOI 10.1023/A:1007042825783
    • N. Priolo, S. Morcelle del Valle, M. Arribére, L. López, and N. Caffini Isolation and characterization of cysteine protease from the latex of Araujia hortorum fruits J Protein Chem 19 2000 39 49 (Pubitemid 30471013)
    • (2000) Journal of Protein Chemistry , vol.19 , Issue.1 , pp. 39-49
    • Priolo, N.1    Del Valle, S.M.2    Arribere, M.C.3    Lopez, L.4    Caffini, N.5
  • 18
    • 43049093022 scopus 로고    scopus 로고
    • Peptide synthesis in aqueous-organic media catalyzed by proteases from latex of Araujia hortorum (Asclepiadaceae) fruits
    • DOI 10.1016/j.bej.2007.08.020, PII S1369703X07003087
    • E. Quiroga, N. Priolo, D. Obregón, J. Marchese, and S. Barberis Peptide synthesis in aqueous-organic media catalyzed by proteases from latex of Araujia hortorum (Asclepiadaceae) fruits Biochem Eng J 39 2008 115 120 (Pubitemid 351625643)
    • (2008) Biochemical Engineering Journal , vol.39 , Issue.1 , pp. 115-120
    • Quiroga, E.1    Priolo, N.2    Obregon, D.3    Marchese, J.4    Barberis, S.5
  • 19
    • 0035501540 scopus 로고    scopus 로고
    • Isolation and purification of cysteine peptidases from the latex of Araujia hortorum fruits. Study of their esterase activities using partial least-squares (PLS) modeling
    • N. Priolo, M.C. Arribére, N. Caffini, S. Barberis, R.N. Vázquez, and J.M. Luco Isolation and purification of cysteine peptidases from the latex of Araujia hortorum fruits. Study of their esterase activities using partial least-squares (PLS) modeling J Mol Catal B: Enzym 635 2001 1 13
    • (2001) J Mol Catal B: Enzym , vol.635 , pp. 1-13
    • Priolo, N.1    Arribére, M.C.2    Caffini, N.3    Barberis, S.4    Vázquez, R.N.5    Luco, J.M.6
  • 20
    • 31044445942 scopus 로고    scopus 로고
    • Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
    • DOI 10.1016/j.molcatb.2005.11.011, PII S1381117705002018
    • S. Barberis, E. Quiroga, S. Morcelle, N. Priolo, and J.M. Luco Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships J Mol Catal B: Enzym 38 2006 95 103 (Pubitemid 43121430)
    • (2006) Journal of Molecular Catalysis B: Enzymatic , vol.38 , Issue.2 , pp. 95-103
    • Barberis, S.1    Quiroga, E.2    Morcelle, S.3    Priolo, N.4    Luco, J.M.5
  • 21
    • 23044488255 scopus 로고    scopus 로고
    • Stability of araujiain, a novel plant protease, in different organic systems
    • E. Quiroga, N. Priolo, J. Marchese, and S. Barberis Stability of araujiain, a novel plant protease, on different organic systems Acta Farmacéutica Bonaerense 24 2005 204 208 (Pubitemid 41076209)
    • (2005) Acta Farmaceutica Bonaerense , vol.24 , Issue.2 , pp. 204-208
    • Quiroga, E.1    Priolo, N.2    Marchese, J.3    Barberis, S.4
  • 22
    • 32044473288 scopus 로고    scopus 로고
    • Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
    • DOI 10.2225/vol9-issue1-fulltext-6
    • E. Quiroga, N. Priolo, J. Marchese, and S. Barberis Behaviour of araujiain, a cystein phytoprotease, in organic media with low water content Electron J Biotechnol 9 2006 18 25 (Pubitemid 43200922)
    • (2006) Electronic Journal of Biotechnology , vol.9 , Issue.1 , pp. 18-25
    • Quiroga, E.1    Priolo, N.2    Marchese, J.3    Barberis, S.4
  • 23
    • 0015937127 scopus 로고
    • Kinetic of papain-catalyzed hydrolysis of α-N-Benzoyl-l-arginine-p- anilide
    • J.E. Mole, and R. Horton Kinetic of papain-catalyzed hydrolysis of α-N-Benzoyl-l-arginine-p-anilide Biochemistry 12 1973 816 822
    • (1973) Biochemistry , vol.12 , pp. 816-822
    • Mole, J.E.1    Horton, R.2
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • DOI 10.1006/abio.2001.5337
    • M. Van der Weert, P.I. Haris, W.E. Hennink, and D.J.A. Crommelin Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling methods and stress factors Anal Biochem 297 2001 160 169 (Pubitemid 32989346)
    • (2001) Analytical Biochemistry , vol.297 , Issue.2 , pp. 160-169
    • Van De Weert, M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.A.4
  • 26
    • 34247862192 scopus 로고    scopus 로고
    • Organic solvent effect on the secondary structure of araujiain hI, in different media
    • E. Quiroga, G. Camí, J. Marchese, and S. Barberis Organic solvent effect on the secondary structure of araujiain hI, in different media Biochem Eng J 35 2007 202 1985
    • (2007) Biochem Eng J , vol.35 , pp. 202-1985
    • Quiroga, E.1    Camí, G.2    Marchese, J.3    Barberis, S.4
  • 27
    • 21644449995 scopus 로고    scopus 로고
    • Characterization of dipeptidyl peptidase IV (DPP IV) in Ca-alginate beads
    • A. Mittal, S. Khurana, H. Singh, and R.C. Kamboj Characterization of dipeptidyl peptidase IV (DPP IV) in Ca-alginate beads Enzyme Microb Technol 37 2005 318 323
    • (2005) Enzyme Microb Technol , vol.37 , pp. 318-323
    • Mittal, A.1    Khurana, S.2    Singh, H.3    Kamboj, R.C.4
  • 29
    • 67549099873 scopus 로고    scopus 로고
    • Optimization, immobilization of extracellular alkaline protease and characterization of its enzymatic properties
    • S.A. Ahmed, R.A. Al-domany, N.M.A. El-Shayeb, H.H. Radwan, and S.A. Saleh Optimization, immobilization of extracellular alkaline protease and characterization of its enzymatic properties Res J Agr Biol Sci 4 2008 434 446
    • (2008) Res J Agr Biol Sci , vol.4 , pp. 434-446
    • Ahmed, S.A.1    Al-Domany, R.A.2    El-Shayeb, N.M.A.3    Radwan, H.H.4    Saleh, S.A.5
  • 30
    • 27744447201 scopus 로고    scopus 로고
    • A novel matrix for the immobilization of acetylcholinesterase
    • DOI 10.1016/j.ijbiomac.2005.10.003, PII S0141813005002096
    • F. ahin, G. Demirel, and H. Tümtürk A novel matrix for the immobilization of acetylcholinesterase Int J Biol Macromol 37 2005 148 153 (Pubitemid 41607708)
    • (2005) International Journal of Biological Macromolecules , vol.37 , Issue.3 , pp. 148-153
    • Sahin, F.1    Demirel, G.2    Tumturk, H.3
  • 31
    • 34249052181 scopus 로고    scopus 로고
    • Optimization of α-amylase immobilization in calcium alginate beads
    • DOI 10.1080/10826060701386679, PII 778919120
    • F. Ertan, H. Yagar, and B. Balkan Optimization of alpha-amylase immobilization in calcium alginate beads Prep Biochem Biotechnol 37 2007 195 204 (Pubitemid 46791633)
    • (2007) Preparative Biochemistry and Biotechnology , vol.37 , Issue.3 , pp. 195-204
    • Ertan, F.1    Yagar, H.2    Balkan, B.3
  • 32
    • 33748855376 scopus 로고    scopus 로고
    • Immobilization of urease by using chitosan-alginate and poly(acrylamide-co-acrylic acid)/κ-carrageenan supports
    • DOI 10.1007/s00449-006-0073-0
    • F. Kara, G. Demirel, and H. Tümtürk Immobilization of urease by using chitosan-alginate and poly(acrylamide-co-acrylic acid)/κ- carrageenan supports Bioprocess Biosyst Eng 29 2006 207 211 (Pubitemid 44421535)
    • (2006) Bioprocess and Biosystems Engineering , vol.29 , Issue.3 , pp. 207-211
    • Kara, F.1    Demirel, G.2    Tumturk, H.3
  • 33
    • 23944492122 scopus 로고    scopus 로고
    • Binary immobilization of tyrosinase by using alginate gel beads and poly(acrylamide-co-acrylic acid) hydrogels
    • DOI 10.1016/j.ijbiomac.2005.06.011, PII S0141813005000905
    • A. Yahi, F. ahin, G. Demirel, and H. Tümtürk Binary immobilization of tyrosinase by using alginate gel beads and poly(acrylamide-co-acrylic acid) hydrogels Int J Biol Macromol 36 2005 253 258 (Pubitemid 41196746)
    • (2005) International Journal of Biological Macromolecules , vol.36 , Issue.4 , pp. 253-258
    • Yahsi, A.1    Sahin, F.2    Demirel, G.3    Tumturk, H.4
  • 34
    • 0037007546 scopus 로고    scopus 로고
    • Stability and properties of mushroom tyrosinase entrapped in alginate, polyacrylamide and gelatin gels
    • DOI 10.1016/S0141-0229(02)00019-4, PII S0141022902000194
    • N. Munjal, and S.V. Sawhney Stability and properties of mushroom tyrosinase entrapped in alginate and polyacrylamide and gelatin gels Enzyme Microb Technol 30 2002 613 619 (Pubitemid 34327695)
    • (2002) Enzyme and Microbial Technology , vol.30 , Issue.5 , pp. 613-619
    • Munjal, N.1    Sawhney, S.K.2
  • 35
    • 0037028008 scopus 로고    scopus 로고
    • Design of controlled-release solid dosage forms of alginate and chitosan using microwave
    • DOI 10.1016/S0168-3659(02)00237-7, PII S0168365902002377
    • T.W. Wong, L.W. Chan, S.B. Kho, and P.W.S. Heng Design of controlled-release solid dosage forms of alginate and chitosan using microwave J Controlled Release 84 2002 99 114 (Pubitemid 35439141)
    • (2002) Journal of Controlled Release , vol.84 , Issue.3 , pp. 99-114
    • Wong, T.W.1    Chan, L.W.2    Kho, S.B.3    Sia Heng, P.W.4


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