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Volumn 176, Issue 4, 2015, Pages 999-1011

Stabilization of Phenylalanine Ammonia Lyase from Rhodotorula glutinis by Encapsulation in Polyethyleneimine-Mediated Biomimetic Silica

Author keywords

Biomimetic silica; Immobilization enzyme; Phenylalanine ammonia lyase; Rhodotorula glutinis; Stability

Indexed keywords

AMINO ACIDS; AMMONIA; BIOMIMETICS; CONVERGENCE OF NUMERICAL METHODS; ENZYME IMMOBILIZATION; ENZYMES; MASS TRANSFER; PH EFFECTS; SILICA; STABILITY; THERMODYNAMIC STABILITY;

EID: 84937815921     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-015-1624-0     Document Type: Article
Times cited : (17)

References (35)
  • 1
    • 0030297793 scopus 로고    scopus 로고
    • Stabilization of phenylalanine ammonia lyase containing Rhodotorula glutinis cells for the continuous synthesis of L-phenylalanine methyl ester
    • D’ Cunha, G. B., Satyanarayan, V., & Nair, P. M. (1996). Stabilization of phenylalanine ammonia lyase containing Rhodotorula glutinis cells for the continuous synthesis of L-phenylalanine methyl ester. Enzyme and Microbial Technology, 19, 421–427.
    • (1996) Enzyme and Microbial Technology , vol.19 , pp. 421-427
    • D’ Cunha, G.B.1    Satyanarayan, V.2    Nair, P.M.3
  • 2
    • 0036019046 scopus 로고    scopus 로고
    • Optimization of reaction conditions and stabilization of phenylalanine ammonia lyase-containing Rhodotorula glutinis cells during bioconversion of trans-cinnamic acid to L-phenylalanine
    • EI-Batal, A. I. (2002). Optimization of reaction conditions and stabilization of phenylalanine ammonia lyase-containing Rhodotorula glutinis cells during bioconversion of trans-cinnamic acid to L-phenylalanine. Acta Microbiologica Polonica, 51, 139–145.
    • (2002) Acta Microbiologica Polonica , vol.51 , pp. 139-145
    • EI-Batal, A.I.1
  • 3
    • 62349088919 scopus 로고    scopus 로고
    • Optimal culture condition for the production of phenyalanine ammonia lyase from E. coli
    • COI: 1:CAS:528:DC%2BD1MXnslCqt7k%3D
    • Cui, J. D., & Li, Y. (2009). Optimal culture condition for the production of phenyalanine ammonia lyase from E. coli. Korean Journal Chemical Engineering, 26, 444–449.
    • (2009) Korean Journal Chemical Engineering , vol.26 , pp. 444-449
    • Cui, J.D.1    Li, Y.2
  • 4
    • 84904904266 scopus 로고    scopus 로고
    • Mechanism-based site-directed mutagenesis to shift the optimum pH of the phenylalanine ammonia-lyase from Rhodotorula glutinis JN-1
    • Zhu, L. B., Zhou, L., Cui, W. J., Liu, Z. M., & Zhou, Z. M. (2014). Mechanism-based site-directed mutagenesis to shift the optimum pH of the phenylalanine ammonia-lyase from Rhodotorula glutinis JN-1. Biotechnology Reports, 3, 21–26.
    • (2014) Biotechnology Reports , vol.3 , pp. 21-26
    • Zhu, L.B.1    Zhou, L.2    Cui, W.J.3    Liu, Z.M.4    Zhou, Z.M.5
  • 5
    • 0011926954 scopus 로고
    • Phenylalanine ammonia lyase from Sporidiobolus pararoseus and Rhodosporidium toruloides: application for phenylalanine and tyrosine deamination
    • COI: 1:CAS:528:DyaK3sXjslGjsg%3D%3D
    • Watanabe, S. K., Hemandez-Velazco, G., Iturbe-Chinas, F., & Lopez-Mungia, A. (1992). Phenylalanine ammonia lyase from Sporidiobolus pararoseus and Rhodosporidium toruloides: application for phenylalanine and tyrosine deamination. World Journal Microbiology Biotechnology, 8, 406–411.
    • (1992) World Journal Microbiology Biotechnology , vol.8 , pp. 406-411
    • Watanabe, S.K.1    Hemandez-Velazco, G.2    Iturbe-Chinas, F.3    Lopez-Mungia, A.4
  • 6
    • 84903759443 scopus 로고    scopus 로고
    • Single-dose, subcutaneous recombinant phenylalanine ammonia lyase conjugated with polyethylene glycol in adult patients with phenylketonuria: an open-label, multicentre, phase 1 dose-escalation trial
    • COI: 1:CAS:528:DC%2BC2cXmtlWhsrs%3D
    • Longo, N., Harding, C. O., Burton, B. K., Grange, D. K., Vockey, J., Wasserstein, M., Rice, G. M., Dorenbaun, A., Neuenburg, J. K., Musson, D. M., Gu, Z. H., & Sile, S. (2014). Single-dose, subcutaneous recombinant phenylalanine ammonia lyase conjugated with polyethylene glycol in adult patients with phenylketonuria: an open-label, multicentre, phase 1 dose-escalation trial. Lancet, 384(9937), 37–44.
    • (2014) Lancet , vol.384 , Issue.9937 , pp. 37-44
    • Longo, N.1    Harding, C.O.2    Burton, B.K.3    Grange, D.K.4    Vockey, J.5    Wasserstein, M.6    Rice, G.M.7    Dorenbaun, A.8    Neuenburg, J.K.9    Musson, D.M.10    Gu, Z.H.11    Sile, S.12
  • 8
    • 35148882050 scopus 로고    scopus 로고
    • Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase enzyme
    • COI: 1:CAS:528:DC%2BD2sXhtFGrtb3O
    • Xue, Z. X., McCluskey, M., Cantera, K., Ren-Bassat, A., Sariaslani, F. S., & Huang, L. X. (2007). Improved production of p-hydroxycinnamic acid from tyrosine using a novel thermostable phenylalanine/tyrosine ammonia lyase enzyme. Enzyme and Microbial Technology, 42, 58–64.
    • (2007) Enzyme and Microbial Technology , vol.42 , pp. 58-64
    • Xue, Z.X.1    McCluskey, M.2    Cantera, K.3    Ren-Bassat, A.4    Sariaslani, F.S.5    Huang, L.X.6
  • 9
    • 43949141783 scopus 로고    scopus 로고
    • Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia. coli
    • COI: 1:CAS:528:DC%2BD1cXotFeiu7w%3D
    • Cui, J. D., Jia, S. R., & Sun, A. Y. (2008). Influence of amino acids, organic solvents and surfactants for phenylalanine ammonia lyase activity in recombinant Escherichia. coli. Letters in Applied Microbiology, 46, 631–635.
    • (2008) Letters in Applied Microbiology , vol.46 , pp. 631-635
    • Cui, J.D.1    Jia, S.R.2    Sun, A.Y.3
  • 10
    • 0030249793 scopus 로고    scopus 로고
    • Stability of L-phenylalanine ammonia lyase in aqueous solution and as the solid state in air and organic solvents
    • COI: 1:CAS:528:DyaK28XltVOju7Y%3D
    • Rees, D. G., & Jones, D. H. (1996). Stability of L-phenylalanine ammonia lyase in aqueous solution and as the solid state in air and organic solvents. Enzyme and Microbial Technology, 19, 282–288.
    • (1996) Enzyme and Microbial Technology , vol.19 , pp. 282-288
    • Rees, D.G.1    Jones, D.H.2
  • 11
    • 0011998872 scopus 로고
    • Strain improvement of Rhodotorula graminis for production of a novel L-phenylalanine ammonia-lyase
    • COI: 1:CAS:528:DyaL1cXit1Shu7g%3D
    • Orndorff, S. A., Costantino, N., & Stewart, D. (1988). Strain improvement of Rhodotorula graminis for production of a novel L-phenylalanine ammonia-lyase. Applied and Environment Microbiology, 54, 996–1002.
    • (1988) Applied and Environment Microbiology , vol.54 , pp. 996-1002
    • Orndorff, S.A.1    Costantino, N.2    Stewart, D.3
  • 12
    • 84870783601 scopus 로고    scopus 로고
    • Chemical amination of lipase B from Candida antarctica is an efficient solution for the preparation of crosslinked enzyme aggregates
    • COI: 1:CAS:528:DC%2BC38XhsFCnsrbM
    • Galvis, M., Barbosa, C. J., Ortiz, C., Torres, R., & Fernandez-Lafuente, R. (2012). Chemical amination of lipase B from Candida antarctica is an efficient solution for the preparation of crosslinked enzyme aggregates. Process Biochemistry, 47, 2373–2378.
    • (2012) Process Biochemistry , vol.47 , pp. 2373-2378
    • Galvis, M.1    Barbosa, C.J.2    Ortiz, C.3    Torres, R.4    Fernandez-Lafuente, R.5
  • 13
    • 84906234873 scopus 로고    scopus 로고
    • Biotechnological production and applications of microbial phenylalanine ammonia lyase: a recent review
    • COI: 1:CAS:528:DC%2BC2cXhsVWru7vI
    • Cui, J. D., Qiu, J. Q., Fan, X. W., Jia, S. R., & Tan, Z. L. (2014). Biotechnological production and applications of microbial phenylalanine ammonia lyase: a recent review. Critical Reviews in Biotechnology, 34(3), 258–268.
    • (2014) Critical Reviews in Biotechnology , vol.34 , Issue.3 , pp. 258-268
    • Cui, J.D.1    Qiu, J.Q.2    Fan, X.W.3    Jia, S.R.4    Tan, Z.L.5
  • 14
    • 80051787511 scopus 로고    scopus 로고
    • Coupling chemical modification and immobilization to improve the catalytic performance of enzymes
    • COI: 1:CAS:528:DC%2BC3MXovVCrsbc%3D
    • Rodrigues, R. C., Berenguer-Murcia, Á., & Fernandez-Lafuente, R. (2011). Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Advanced Synthesis & Catalysis, 353, 2216–2238.
    • (2011) Advanced Synthesis & Catalysis , vol.353 , pp. 2216-2238
    • Rodrigues, R.C.1    Berenguer-Murcia, Á.2    Fernandez-Lafuente, R.3
  • 16
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: strategies to prevent subunit dissociation
    • COI: 1:CAS:528:DC%2BD1MXht1GksL3F
    • Fernandez-Lafuente, R. (2009). Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme and Microbial Technology, 45, 405–418.
    • (2009) Enzyme and Microbial Technology , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 18
    • 77949671915 scopus 로고    scopus 로고
    • Properties of immobilized phenylalanine ammonia lyase and Investigation of its use for the prediagnosis of phenylketonuria
    • Ateş, S., & Doğan, N. S. (2010). Properties of immobilized phenylalanine ammonia lyase and Investigation of its use for the prediagnosis of phenylketonuria. Turkish Journal of Biochemistry, 35, 58–62.
    • (2010) Turkish Journal of Biochemistry , vol.35 , pp. 58-62
    • Ateş, S.1    Doğan, N.S.2
  • 19
    • 84863720938 scopus 로고    scopus 로고
    • Cross-linked enzyme aggregates of phenylalanine ammonia lyase: novel biocatalysts for synthesis of L-phenylalanine
    • COI: 1:CAS:528:DC%2BC38XotVOgu7k%3D
    • Cui, J. D., Zhang, S., & Sun, L. M. (2012). Cross-linked enzyme aggregates of phenylalanine ammonia lyase: novel biocatalysts for synthesis of L-phenylalanine. Applied Biochemistry and Biotechology, 167, 835–840.
    • (2012) Applied Biochemistry and Biotechology , vol.167 , pp. 835-840
    • Cui, J.D.1    Zhang, S.2    Sun, L.M.3
  • 20
    • 84901250046 scopus 로고    scopus 로고
    • Hybrid magnetic cross-linked enzyme aggregates of phenylalanine ammonia lyase from Rhodotorula glutinis
    • Cui, J. D., Cui, L. L., Zhang, S. P., Zhang, Y. F., Su, Z. G., & Ma, G. H. (2014). Hybrid magnetic cross-linked enzyme aggregates of phenylalanine ammonia lyase from Rhodotorula glutinis. PLoS ONE, 9(5), e97221.
    • (2014) PLoS ONE , vol.9 , Issue.5
    • Cui, J.D.1    Cui, L.L.2    Zhang, S.P.3    Zhang, Y.F.4    Su, Z.G.5    Ma, G.H.6
  • 21
    • 79959778503 scopus 로고    scopus 로고
    • Biomimetic and bioinspired silica: recent developments and applications
    • COI: 1:CAS:528:DC%2BC3MXotVGitr0%3D
    • Patwardhan, S. V. (2011). Biomimetic and bioinspired silica: recent developments and applications. Chemical Communication, 47, 7567–7582.
    • (2011) Chemical Communication , vol.47 , pp. 7567-7582
    • Patwardhan, S.V.1
  • 22
    • 84927174332 scopus 로고    scopus 로고
    • Chitosan-mediated formation of biomimetic silica nanoparticles: an effective method for manganese peroxidase immobilization and stabilization
    • COI: 1:CAS:528:DC%2BC2cXpslClsbk%3D
    • Luan, P. P., Jiang, Y. J., Zhang, S. P., Gao, J., Su, Z. G., Ma, G. H., & Zhang, Y. F. (2014). Chitosan-mediated formation of biomimetic silica nanoparticles: an effective method for manganese peroxidase immobilization and stabilization. Journal of Bioscience and Bioengineering, 118, 575–582.
    • (2014) Journal of Bioscience and Bioengineering , vol.118 , pp. 575-582
    • Luan, P.P.1    Jiang, Y.J.2    Zhang, S.P.3    Gao, J.4    Su, Z.G.5    Ma, G.H.6    Zhang, Y.F.7
  • 23
    • 77949411233 scopus 로고    scopus 로고
    • Biomimetic silica encapsulation of enzymes for replacement of biocides in antifouling coatings
    • COI: 1:CAS:528:DC%2BC3cXjtVSqs74%3D
    • Kristensen, J. B., Meyer, R. L., Poulsen, C. H., Kragh, K. M., Besenbacher, F., & Laursen, B. S. (2010). Biomimetic silica encapsulation of enzymes for replacement of biocides in antifouling coatings. Green Chemistry, 12, 387–394.
    • (2010) Green Chemistry , vol.12 , pp. 387-394
    • Kristensen, J.B.1    Meyer, R.L.2    Poulsen, C.H.3    Kragh, K.M.4    Besenbacher, F.5    Laursen, B.S.6
  • 24
    • 84875410601 scopus 로고    scopus 로고
    • 2 sequestration by enzyme immobilized onto bioinspired silica
    • COI: 1:CAS:528:DC%2BC3sXktlKjtrw%3D
    • 2 sequestration by enzyme immobilized onto bioinspired silica. Chemical Communication, 49, 3191–3193.
    • (2013) Chemical Communication , vol.49 , pp. 3191-3193
    • Forsyth, C.1    Yip, T.W.S.2    Patwardhan, S.V.3
  • 25
    • 84910674439 scopus 로고    scopus 로고
    • Polymer–inorganic microcapsules fabricated by combining biomimetic adhesion and bioinspired mineralization and their use for catalase immobilization
    • COI: 1:CAS:528:DC%2BC2cXhvFWgsLnK
    • Zhang, S. H., Jiang, Z. Y., Zhang, W. Y., Wang, X. L., & Shi, J. F. (2015). Polymer–inorganic microcapsules fabricated by combining biomimetic adhesion and bioinspired mineralization and their use for catalase immobilization. Biochemical Engineering Journal, 93, 281–288.
    • (2015) Biochemical Engineering Journal , vol.93 , pp. 281-288
    • Zhang, S.H.1    Jiang, Z.Y.2    Zhang, W.Y.3    Wang, X.L.4    Shi, J.F.5
  • 27
    • 84906872022 scopus 로고    scopus 로고
    • Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools
    • COI: 1:CAS:528:DC%2BC2cXht1yltbjL
    • Rodrigues, R. C., Barbosa, O., Ortiz, C., Berenguer-Murcia, Á., Torres, R., & Fernandez-Lafuente, R. (2014). Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools. RSC Advances, 4, 38350–38374.
    • (2014) RSC Advances , vol.4 , pp. 38350-38374
    • Rodrigues, R.C.1    Barbosa, O.2    Ortiz, C.3    Berenguer-Murcia, Á.4    Torres, R.5    Fernandez-Lafuente, R.6
  • 28
    • 84910118178 scopus 로고    scopus 로고
    • Preparation of cross-linked enzyme aggregates of trehalose synthase via co-aggregation with polyethyleneimine
    • COI: 1:CAS:528:DC%2BC2cXhsVehsLrP
    • Zheng, J., Chen, Y., Yang, L., Li, M., & Zhang, J. (2014). Preparation of cross-linked enzyme aggregates of trehalose synthase via co-aggregation with polyethyleneimine. Applied Biochemistry and Biotechnology, 174, 2067–2078.
    • (2014) Applied Biochemistry and Biotechnology , vol.174 , pp. 2067-2078
    • Zheng, J.1    Chen, Y.2    Yang, L.3    Li, M.4    Zhang, J.5
  • 29
    • 84871790816 scopus 로고    scopus 로고
    • Enhancement of phenylalanine ammonia lyase production from Rhodotorula mucilaginosa by optimization of culture conditions in batch and fed-batch
    • COI: 1:CAS:528:DC%2BC3sXjtlWqtr0%3D
    • Zhang, S., & Cui, J. D. (2012). Enhancement of phenylalanine ammonia lyase production from Rhodotorula mucilaginosa by optimization of culture conditions in batch and fed-batch. Biotechnology and Biotechnological Equipment, 26, 3418–3423.
    • (2012) Biotechnology and Biotechnological Equipment , vol.26 , pp. 3418-3423
    • Zhang, S.1    Cui, J.D.2
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • COI: 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0742323370 scopus 로고    scopus 로고
    • Enzyme immobilization in a biomimetic silica support
    • COI: 1:CAS:528:DC%2BD2cXnvFeitA%3D%3D
    • Luckarift, H. R., Spain, J. C., Naik, R. R., & Stone, M. O. (2004). Enzyme immobilization in a biomimetic silica support. Nature Biotechnology, 22, 211–213.
    • (2004) Nature Biotechnology , vol.22 , pp. 211-213
    • Luckarift, H.R.1    Spain, J.C.2    Naik, R.R.3    Stone, M.O.4
  • 32
    • 77954217658 scopus 로고    scopus 로고
    • Efficient and stable enzyme immobilization in a block copolypeptide vesicle-templated biomimetic silica support
    • COI: 1:CAS:528:DC%2BC3cXosVyksL8%3D
    • Lai, J. K., Chuang, T. H., Jan, J. S., & Wang, S. S. (2010). Efficient and stable enzyme immobilization in a block copolypeptide vesicle-templated biomimetic silica support. Colloids and Surfaces B-Biointerfaces, 80, 51–58.
    • (2010) Colloids and Surfaces B-Biointerfaces , vol.80 , pp. 51-58
    • Lai, J.K.1    Chuang, T.H.2    Jan, J.S.3    Wang, S.S.4
  • 33
    • 84894101439 scopus 로고    scopus 로고
    • Immobilization of cross-linked phenylalanine ammonia lyase aggregates in microporous silica gel
    • Cui, J. D., Li, L. L., & Bian, H. J. (2013). Immobilization of cross-linked phenylalanine ammonia lyase aggregates in microporous silica gel. PLOS ONE, 8(11), e80581.
    • (2013) PLOS ONE , vol.8 , Issue.11
    • Cui, J.D.1    Li, L.L.2    Bian, H.J.3
  • 34
    • 84881318376 scopus 로고    scopus 로고
    • A simple technique of preparing stable CLEAs of phenylalanine ammonia lyase using co-aggregation with starch and bovine serum albumin
    • Cui, J. D., Sun, L. M., & Zhang, S. (2013). A simple technique of preparing stable CLEAs of phenylalanine ammonia lyase using co-aggregation with starch and bovine serum albumin. Applied Biochemistry and Biotechnology, 2013(170), 1827–1837.
    • (2013) Applied Biochemistry and Biotechnology , vol.2013 , Issue.170 , pp. 1827-1837
    • Cui, J.D.1    Sun, L.M.2    Zhang, S.3


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