메뉴 건너뛰기




Volumn 9, Issue 9, 2014, Pages

Efficient preparation of enantiopure D-phenylalanine through asymmetric resolution using immobilized phenylalanine ammonia-lyase from rhodotorula glutinis JN-1 in a recirculating packed-bed reactor

Author keywords

[No Author keywords available]

Indexed keywords

MESOPOROUS SILICA; PHENYLALANINE; PHENYLALANINE AMMONIA LYASE; SILICON DIOXIDE; UNCLASSIFIED DRUG; FUNGAL PROTEIN; IMMOBILIZED ENZYME;

EID: 84907485593     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0108586     Document Type: Article
Times cited : (31)

References (36)
  • 3
    • 0037413411 scopus 로고    scopus 로고
    • New thermostable d-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for d-phenylalanine production
    • Back DH, Song JJ, Lee SG, Kwon SJ, Asano Y, et al. (2003) New thermostable d-methionine amidase from Brevibacillus borstelensis BCS-1 and its application for d-phenylalanine production. Enzyme Microb Technol 32: 131-139.
    • (2003) Enzyme Microb Technol , vol.32 , pp. 131-139
    • Back, D.H.1    Song, J.J.2    Lee, S.G.3    Kwon, S.J.4    Asano, Y.5
  • 4
    • 79959755723 scopus 로고    scopus 로고
    • Racemic resolution of some DL-amino acids using Aspergillus fumigatus L-amino acid oxidase
    • Singh S, Gogoi BK, Bezbaruah RL (2011) Racemic resolution of some DL-amino acids using Aspergillus fumigatus L-amino acid oxidase. Curr Microbiol 63: 94-99.
    • (2011) Curr Microbiol , vol.63 , pp. 94-99
    • Singh, S.1    Gogoi, B.K.2    Bezbaruah, R.L.3
  • 6
    • 42749097788 scopus 로고    scopus 로고
    • Construction and co-expression of polycistronic plasmid encoding d-hydantoinase and d-carbamoylase for the production of d-amino acids
    • Liu Y, Li Q, Hu X, Yang J (2008) Construction and co-expression of polycistronic plasmid encoding d-hydantoinase and d-carbamoylase for the production of d-amino acids. Enzyme Microb Technol 42: 589-593.
    • (2008) Enzyme Microb Technol , vol.42 , pp. 589-593
    • Liu, Y.1    Li, Q.2    Hu, X.3    Yang, J.4
  • 7
    • 0037269569 scopus 로고    scopus 로고
    • Enhanced hydantoinase and N-carbamoylase activity on immobilisation of Agrobacterium tumefaciens
    • Foster IM, Dorrington RD, Burton SG (2003) Enhanced hydantoinase and N-carbamoylase activity on immobilisation of Agrobacterium tumefaciens. Biotechnol Lett 25: 67-72.
    • (2003) Biotechnol Lett , vol.25 , pp. 67-72
    • Foster, I.M.1    Dorrington, R.D.2    Burton, S.G.3
  • 8
    • 0033960556 scopus 로고    scopus 로고
    • Optimum ratio of d-carbamoylase to d-hydantoinase for maximizing d-p-hydroxyphenylglycine productivity
    • Chao YP, Chiang CJ, Chen PT (2000) Optimum ratio of d-carbamoylase to d-hydantoinase for maximizing d-p-hydroxyphenylglycine productivity. Biotechnol Lett 22: 99-103.
    • (2000) Biotechnol Lett , vol.22 , pp. 99-103
    • Chao, Y.P.1    Chiang, C.J.2    Chen, P.T.3
  • 9
    • 13844299133 scopus 로고    scopus 로고
    • D-Amino acid production by E. Coli co-expressed three genes encoding hydantoin racemase, d-hydantoinase and N-carbamoyl-d-amino acid amidohydrolase
    • Nozaki H, Takenaka Y, Kira I, Watanabe K, Yokozeki K (2005) d-Amino acid production by E. coli co-expressed three genes encoding hydantoin racemase, d-hydantoinase and N-carbamoyl-d-amino acid amidohydrolase. J MoL Catal B Enzym 32: 213-218.
    • (2005) J MoL Catal B Enzym , vol.32 , pp. 213-218
    • Nozaki, H.1    Takenaka, Y.2    Kira, I.3    Watanabe, K.4    Yokozeki, K.5
  • 11
    • 33751505449 scopus 로고    scopus 로고
    • Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti
    • Martinez-Rodriguez S, Andujar-Sanchez M, Neira JL, Clemente-Jimenez JM, Jara-Perez V, et al. (2006) Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti. Protein Sci 15: 2729-2738.
    • (2006) Protein Sci , vol.15 , pp. 2729-2738
    • Martinez-Rodriguez, S.1    Andujar-Sanchez, M.2    Neira, J.L.3    Clemente-Jimenez, J.M.4    Jara-Perez, V.5
  • 12
    • 0031457941 scopus 로고    scopus 로고
    • D-Amino acid production from racemic amino acids by a microbial asymmetric degradation
    • Takahashi E, Furui M, Shibatan T (1997) D-Amino acid production from racemic amino acids by a microbial asymmetric degradation. Biotechnol Tech 11: 913-916.
    • (1997) Biotechnol Tech , vol.11 , pp. 913-916
    • Takahashi, E.1    Furui, M.2    Shibatan, T.3
  • 13
    • 84860135513 scopus 로고    scopus 로고
    • A Simple Enzymatic Method for Production of a Wide Variety of D-Amino Acids Using L-Amino Acid Oxidase from Rhodococcus sp. AIU Z-35-1
    • Isobe K, Tamauchi H, Fuhshuku K, Nagasawa S, Asano Y (2010) A Simple Enzymatic Method for Production of a Wide Variety of D-Amino Acids Using L-Amino Acid Oxidase from Rhodococcus sp. AIU Z-35-1. Enzyme Res 2010: 567210. doi: 10.4061/2010/567210.
    • (2010) Enzyme Res , vol.2010 , pp. 567210
    • Isobe, K.1    Tamauchi, H.2    Fuhshuku, K.3    Nagasawa, S.4    Asano, Y.5
  • 14
    • 84880973674 scopus 로고    scopus 로고
    • Engineering the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum by site saturation mutagenesis for D-phenylalanine synthesis
    • Gao X, Huang F, Feng J, Chen X, Zhang H, et al. (2013) Engineering the meso-diaminopimelate dehydrogenase from Symbiobacterium thermophilum by site saturation mutagenesis for D-phenylalanine synthesis. Appl Environ Microbiol 79: 5078-5081.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 5078-5081
    • Gao, X.1    Huang, F.2    Feng, J.3    Chen, X.4    Zhang, H.5
  • 15
    • 0141763460 scopus 로고    scopus 로고
    • Recent developments in the treatment of type 2 diabetes mellitus
    • Ruilope LM (2003) Recent developments in the treatment of type 2 diabetes mellitus. Cardiovas Druqs Ther 17: 151-158.
    • (2003) Cardiovas Druqs Ther , vol.17 , pp. 151-158
    • Ruilope, L.M.1
  • 16
    • 84876969482 scopus 로고    scopus 로고
    • Cloning, expression and characterization of phenylalanine ammonia-lyase from Rhodotorula glutinis
    • Zhu L, Cui W, Fang Y, Liu Y, Gao X, et al. (2013) Cloning, expression and characterization of phenylalanine ammonia-lyase from Rhodotorula glutinis. Biotechnol Lett 35: 751-756.
    • (2013) Biotechnol Lett , vol.35 , pp. 751-756
    • Zhu, L.1    Cui, W.2    Fang, Y.3    Liu, Y.4    Gao, X.5
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 77649225940 scopus 로고    scopus 로고
    • Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve SBA-15
    • Jung D, Streb C, Hartmann M (2010) Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve SBA-15. Int J Mol Sci 11: 762-778.
    • (2010) Int J Mol Sci , vol.11 , pp. 762-778
    • Jung, D.1    Streb, C.2    Hartmann, M.3
  • 19
    • 56049111888 scopus 로고    scopus 로고
    • Immobilization of alkaline serine endopeptidase from Bacillus licheniformis on SBA-15 and MCF by surface covalent binding
    • Kannan K, Jasra RV (2009) Immobilization of alkaline serine endopeptidase from Bacillus licheniformis on SBA-15 and MCF by surface covalent binding. J Mol Catal B Enzym 56: 34-40.
    • (2009) J Mol Catal B Enzym , vol.56 , pp. 34-40
    • Kannan, K.1    Jasra, R.V.2
  • 20
    • 78650701414 scopus 로고    scopus 로고
    • Immobilization of penicillin G acylase on macro-mesoporous silica spheres
    • Zhao J, Wang Y, Luo G, Zhu S (2011) Immobilization of penicillin G acylase on macro-mesoporous silica spheres. Bioresour Technol 102: 529-535.
    • (2011) Bioresour Technol , vol.102 , pp. 529-535
    • Zhao, J.1    Wang, Y.2    Luo, G.3    Zhu, S.4
  • 21
    • 0025397824 scopus 로고
    • Novel Ligand-Exchange Chromatographic Resolution of DL-Amino Acids using Nucleotides and Coenzymes
    • Fukuhara T, Yuasa S (1990) Novel Ligand-Exchange Chromatographic Resolution of DL-Amino Acids using Nucleotides and Coenzymes. J Chromategr Sci 28: 114-117.
    • (1990) J Chromategr Sci , vol.28 , pp. 114-117
    • Fukuhara, T.1    Yuasa, S.2
  • 22
    • 76749111010 scopus 로고    scopus 로고
    • Effect of pore diameter and cross-linking method on the immobilization efficiency of Candida rugosa lipase in SBA-15
    • Gao S, Wang Y, Diao X, Luo G, Dai Y (2010) Effect of pore diameter and cross-linking method on the immobilization efficiency of Candida rugosa lipase in SBA-15. Bioresour Technol 101: 3830-3837.
    • (2010) Bioresour Technol , vol.101 , pp. 3830-3837
    • Gao, S.1    Wang, Y.2    Diao, X.3    Luo, G.4    Dai, Y.5
  • 23
    • 84880082972 scopus 로고    scopus 로고
    • Immobilization of enzymes on porous silicas -benefits and challenges
    • Hartmann M, Kostrov X (2013) Immobilization of enzymes on porous silicas -benefits and challenges. Chem Soc Rev 42: 6277-6289.
    • (2013) Chem Soc Rev , vol.42 , pp. 6277-6289
    • Hartmann, M.1    Kostrov, X.2
  • 24
    • 84878698340 scopus 로고    scopus 로고
    • Immobilisation of enzymes on mesoporous silicate materials
    • Magner E (2013) Immobilisation of enzymes on mesoporous silicate materials. Chem Soc Rev 42: 6213-6222.
    • (2013) Chem Soc Rev , vol.42 , pp. 6213-6222
    • Magner, E.1
  • 25
    • 34347376588 scopus 로고    scopus 로고
    • A modern view of phenylalanine ammonia lyase
    • MacDonald MJ, D'Cunha GB (2007) A modern view of phenylalanine ammonia lyase. Biochem Cell Biol 85: 273-282.
    • (2007) Biochem Cell Biol , vol.85 , pp. 273-282
    • MacDonald, M.J.1    D'Cunha, G.B.2
  • 26
    • 67849135034 scopus 로고    scopus 로고
    • Amine functionalized MCM-41: An active and reusable catalyst for Knoevenagel condensation reaction
    • Parida KM, Rath D (2009) Amine functionalized MCM-41: An active and reusable catalyst for Knoevenagel condensation reaction. J Mol Catal A Chem 310: 93-100.
    • (2009) J Mol Catal A Chem , vol.310 , pp. 93-100
    • Parida, K.M.1    Rath, D.2
  • 27
    • 18844440954 scopus 로고    scopus 로고
    • A new mesoporous micelle-templated silica route for enzyme encapsulation
    • Mureseanu M, Galarneau A, Renard G, Fajula F (2005) A new mesoporous micelle-templated silica route for enzyme encapsulation. Langmuir 21: 4648 -4655.
    • (2005) Langmuir , vol.21 , pp. 4648-4655
    • Mureseanu, M.1    Galarneau, A.2    Renard, G.3    Fajula, F.4
  • 28
    • 10044285891 scopus 로고    scopus 로고
    • Studies on the activity and stability of immobilized a-amylase in ordered mesoporous silicas
    • Pandya PH, Jasra RV, Newalkar BL, Bhatt PN (2005) Studies on the activity and stability of immobilized a-amylase in ordered mesoporous silicas. Micropor Mesopor Mater 77: 67-77.
    • (2005) Micropor Mesopor Mater , vol.77 , pp. 67-77
    • Pandya, P.H.1    Jasra, R.V.2    Newalkar, B.L.3    Bhatt, P.N.4
  • 29
    • 34248336588 scopus 로고    scopus 로고
    • β-Galactosidase from Talaromyces thermophilus immobilized on to Eupergit C for production of galacto-oligosaccharides during lactose hydrolysis in batch and packed-bed reactor
    • Nakkharat P, Haltrich D (2007) β-Galactosidase from Talaromyces thermophilus immobilized on to Eupergit C for production of galacto-oligosaccharides during lactose hydrolysis in batch and packed-bed reactor. World J Microbiol Biotechnol 23: 759-764.
    • (2007) World J Microbiol Biotechnol , vol.23 , pp. 759-764
    • Nakkharat, P.1    Haltrich, D.2
  • 30
    • 84892527003 scopus 로고    scopus 로고
    • Efficient preparation of enantiopure L-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium
    • Liu W, Luo J, Zhuang X, Shen W, Zhang Y, et al. (2014) Efficient preparation of enantiopure L-tert-leucine through immobilized penicillin G acylase catalyzed kinetic resolution in aqueous medium. Biochem Eng J 83: 116-120.
    • (2014) Biochem Eng J , vol.83 , pp. 116-120
    • Liu, W.1    Luo, J.2    Zhuang, X.3    Shen, W.4    Zhang, Y.5
  • 31
    • 84875795467 scopus 로고    scopus 로고
    • Efficient production of S-(+)-2-chlorophenylglycine by immobilized penicillin G acylase in a recirculating packed bed reactor
    • Xue YP, Jiang T, Liu X, Zheng YG (2013) Efficient production of S-(+)-2-chlorophenylglycine by immobilized penicillin G acylase in a recirculating packed bed reactor. Biochem Eng J 74: 88-94.
    • (2013) Biochem Eng J , vol.74 , pp. 88-94
    • Xue, Y.P.1    Jiang, T.2    Liu, X.3    Zheng, Y.G.4
  • 32
    • 33646574270 scopus 로고    scopus 로고
    • Continuous production of L-phenylalanine from phenylpyruvic acid and L-aspartic acid by immobilized recombinant Escherichia coli SW0209-52
    • Leng Y, Zheng P, Sun ZH (2006) Continuous production of L-phenylalanine from phenylpyruvic acid and L-aspartic acid by immobilized recombinant Escherichia coli SW0209-52. Process Biochem 41: 1669-1672.
    • (2006) Process Biochem , vol.41 , pp. 1669-1672
    • Leng, Y.1    Zheng, P.2    Sun, Z.H.3
  • 33
    • 1842735631 scopus 로고    scopus 로고
    • Immobilised lipase-catalysed resolution of (R, S)-1-phenylethanol in recirculated packed bed reactor
    • Chua LS, Sarmidi MR (2004) Immobilised lipase-catalysed resolution of (R, S)-1-phenylethanol in recirculated packed bed reactor. J Mol Catal B Enzym 28: 111-119.
    • (2004) J Mol Catal B Enzym , vol.28 , pp. 111-119
    • Chua, L.S.1    Sarmidi, M.R.2
  • 35
    • 0035988011 scopus 로고    scopus 로고
    • Directed evolution of N-carbamyl-D-amino acid amidohydrolase for simultaneous improvement of oxidative and thermal stability
    • Oh KH, Nam SH, Kim HS (2002) Directed evolution of N-carbamyl-D-amino acid amidohydrolase for simultaneous improvement of oxidative and thermal stability. Biotechnol Prog 18: 413-417.
    • (2002) Biotechnol Prog , vol.18 , pp. 413-417
    • Oh, K.H.1    Nam, S.H.2    Kim, H.S.3
  • 36
    • 84892749983 scopus 로고    scopus 로고
    • Process parameter optimization for hydantoinase-mediated synthesis of optically pure carbamoyl amino acids of industrial value using Pseudomonas aeruginosa resting cells
    • Engineer AS, Dhakephalkar AP, Gaikaiwari RP, Dhakephalkar PK (2013) Process parameter optimization for hydantoinase-mediated synthesis of optically pure carbamoyl amino acids of industrial value using Pseudomonas aeruginosa resting cells. J Ind Microbiol Biotechnol 40: 1367-1372.
    • (2013) J Ind Microbiol Biotechnol , vol.40 , pp. 1367-1372
    • Engineer, A.S.1    Dhakephalkar, A.P.2    Gaikaiwari, R.P.3    Dhakephalkar, P.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.