메뉴 건너뛰기




Volumn 251, Issue 3, 2014, Pages 639-648

Chloroplast molecular farming: Efficient production of a thermostable xylanase by Nicotiana tabacum plants and long-term conservation of the recombinant enzyme

Author keywords

Chloroplast transformation; Enzyme long term storage; Photosynthetic performance of tobacco transplastomic plants; Plant biofactory; Recombinant thermostable xylanase

Indexed keywords

NICOTIANA TABACUM;

EID: 84926637048     PISSN: 0033183X     EISSN: 16156102     Source Type: Journal    
DOI: 10.1007/s00709-013-0564-1     Document Type: Article
Times cited : (20)

References (35)
  • 1
    • 84871691222 scopus 로고    scopus 로고
    • Photosynthetic responses of plants to excess light: Mechanisms and conditions for photoinhibition, excess energy dissipation and repair
    • Eaton JJ, Tripathy BC, Sharkey TD, Springer, Dordrecht
    • Allahverdiyeva T, Aro E-M (2012) Photosynthetic responses of plants to excess light: mechanisms and conditions for photoinhibition, excess energy dissipation and repair. In: Eaton JJ, Tripathy BC, Sharkey TD (eds) Photosynthesis: plastid biology, energy conversion and carbon assimilation. Advances in photosynthesis and respiration. Springer, Dordrecht, pp 275–297
    • (2012) Photosynthesis: Plastid Biology, Energy Conversion and Carbon Assimilation. Advances in Photosynthesis and Respiration , pp. 275-297
    • Allahverdiyeva, T.1    Aro, E.-M.2
  • 2
    • 0002276039 scopus 로고
    • Photoregulation of the composition, function, and structure of thylakoid membranes
    • Anderson JM (1986) Photoregulation of the composition, function, and structure of thylakoid membranes. Annu Rev Plant Physiol Plant Mol Biol 37:93–136
    • (1986) Annu Rev Plant Physiol Plant Mol Biol , vol.37 , pp. 93-136
    • Anderson, J.M.1
  • 4
    • 77949540390 scopus 로고    scopus 로고
    • Morpho-physiological and biochemical responses in the floating lamina of Trapa natans exposed to molybdenum
    • Baldisserotto C, Ferroni L, Zanzi C, Marchesini R, Pagnoni A, Pancaldi S (2010) Morpho-physiological and biochemical responses in the floating lamina of Trapa natans exposed to molybdenum. Protoplasma 240:83–97
    • (2010) Protoplasma , vol.240 , pp. 83-97
    • Baldisserotto, C.1    Ferroni, L.2    Zanzi, C.3    Marchesini, R.4    Pagnoni, A.5    Pancaldi, S.6
  • 5
    • 67650166213 scopus 로고    scopus 로고
    • DubaldM(2009) Plant physiological adaptations to the massive foreign protein synthesis occurring in recombinant chloroplasts
    • Bally J, Nadai M, Vitel M, Rolland A, Dumain R, DubaldM(2009) Plant physiological adaptations to the massive foreign protein synthesis occurring in recombinant chloroplasts. Plant Physiol 150:1474–1481
    • Plant Physiol , vol.150 , pp. 1474-1481
    • Bally, J.1    Nadai, M.2    Vitel, M.3    Rolland, A.4    Dumain, R.5
  • 6
    • 77956204645 scopus 로고    scopus 로고
    • The critical role of N- and C-terminal contact in protein stability and folding of a family 10 xylanase under extreme conditions
    • Bhardwaj A, Leelavathi S, Mazumdar-Leighton S, Ghosh A, Ramakumar S, Reddy VS (2010) The critical role of N- and C-terminal contact in protein stability and folding of a family 10 xylanase under extreme conditions. Plos One 5:e11347
    • (2010) Plos One , vol.5
    • Bhardwaj, A.1    Leelavathi, S.2    Mazumdar-Leighton, S.3    Ghosh, A.4    Ramakumar, S.5    Reddy, V.S.6
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgramquantities 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
  • 10
    • 79954759457 scopus 로고    scopus 로고
    • Protein bodyinducing fusions for high-level production and purification of recombinant proteins in plants
    • Conley AJ, Joensuu JJ, Richman A, Manassa R (2011) Protein bodyinducing fusions for high-level production and purification of recombinant proteins in plants. Plant Biotechnol J 9:419–433
    • (2011) Plant Biotechnol J , vol.9 , pp. 419-433
    • Conley, A.J.1    Joensuu, J.J.2    Richman, A.3    Manassa, R.4
  • 11
    • 33747141725 scopus 로고    scopus 로고
    • Foreign protein degradation and instability in plants and plant tissue cultures
    • Doran PM (2006) Foreign protein degradation and instability in plants and plant tissue cultures. Trends Biotechnol 24:426–432
    • (2006) Trends Biotechnol , vol.24 , pp. 426-432
    • Doran, P.M.1
  • 12
    • 84943470296 scopus 로고
    • Measurements of cellulase activities
    • Ghose TK (1987) Measurements of cellulase activities. Pure Appl Chem 59:257–268
    • (1987) Pure Appl Chem , vol.59 , pp. 257-268
    • Ghose, T.K.1
  • 13
    • 0034041260 scopus 로고    scopus 로고
    • Cloning, expression, and sequence analysis of the gene encoding the alkali-stable, thermostable endoxylanase from alkalophilic, mesophilic Bacillus sp. Strain NG-27
    • Gupta N, Reddy VS, Maiti S, Ghosh A (2000) Cloning, expression, and sequence analysis of the gene encoding the alkali-stable, thermostable endoxylanase from alkalophilic, mesophilic Bacillus sp. strain NG-27. Appl Environ Microbiol 66:2631–2635
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2631-2635
    • Gupta, N.1    Reddy, V.S.2    Maiti, S.3    Ghosh, A.4
  • 14
    • 2942526709 scopus 로고    scopus 로고
    • A simple alternative approach to assessing the fate of absorbed light energy using chlorophyll fluorescence
    • Hendrickson L, Furbank RT, Chow WS (2004) A simple alternative approach to assessing the fate of absorbed light energy using chlorophyll fluorescence. Photosynth Res 82:73–81
    • (2004) Photosynth Res , vol.82 , pp. 73-81
    • Hendrickson, L.1    Furbank, R.T.2    Chow, W.S.3
  • 16
    • 82755194791 scopus 로고    scopus 로고
    • The role of the xanthophyll cycle and of lutein in photoprotection of photosystem
    • Jahns P, Holzwarth AR (2012) The role of the xanthophyll cycle and of lutein in photoprotection of photosystem. Biochim Biophys Acta 1817:182–193
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 182-193
    • Jahns, P.1    Holzwarth, A.R.2
  • 17
    • 84865431024 scopus 로고    scopus 로고
    • Microbial xylanases: Engineering, production and industrial applications
    • Juturu V, Wu JC (2012) Microbial xylanases: engineering, production and industrial applications. Biotechnol Adv 30:1219–1227
    • (2012) Biotechnol Adv , vol.30 , pp. 1219-1227
    • Juturu, V.1    Wu, J.C.2
  • 18
    • 79953727143 scopus 로고    scopus 로고
    • Production of hyperthermostable GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants enables complete hydrolysis of methylglucuronoxylan to fermentable sugars for biofuel production
    • Kim JY, Kavas M, Fouad WM, Nong G, Preston JF, Altpeter F (2011) Production of hyperthermostable GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants enables complete hydrolysis of methylglucuronoxylan to fermentable sugars for biofuel production. Plant Mol Biol 76:357–369
    • (2011) Plant Mol Biol , vol.76 , pp. 357-369
    • Kim, J.Y.1    Kavas, M.2    Fouad, W.M.3    Nong, G.4    Preston, J.F.5    Altpeter, F.6
  • 19
    • 73249116038 scopus 로고    scopus 로고
    • Complementary PSII quantum yields calculated from simple fluorescence parameters measured byPAM fluorometry and the saturation pulse method
    • Klughammer C, Schreiber U (2008) Complementary PSII quantum yields calculated from simple fluorescence parameters measured byPAM fluorometry and the saturation pulse method. PAM Appl Notes 1: 27–35
    • (2008) PAM Appl Notes , vol.1 , pp. 27-35
    • Klughammer, C.1    Schreiber, U.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0037280809 scopus 로고    scopus 로고
    • Overproduction of an alkali- and thermo-stable xylanase in tobacco chloroplasts and efficient recovery of the enzyme
    • Leelavathi S, Gupta N, Maiti S, Ghosh A, Reddy VS (2003) Overproduction of an alkali- and thermo-stable xylanase in tobacco chloroplasts and efficient recovery of the enzyme. Mol Breed 11:59–67
    • (2003) Mol Breed , vol.11 , pp. 59-67
    • Leelavathi, S.1    Gupta, N.2    Maiti, S.3    Ghosh, A.4    Reddy, V.S.5
  • 22
    • 26444609627 scopus 로고    scopus 로고
    • How to correctly determine the different chlorophyll fluorescence parameters and the chlorophyll fluorescence decrease ratio R-Fd of leaves with the PAM fluorometer
    • Lichtenthaler HK, Buschmann C, Knapp M (2005) How to correctly determine the different chlorophyll fluorescence parameters and the chlorophyll fluorescence decrease ratio R-Fd of leaves with the PAM fluorometer. Photosynthetica 43:379–393
    • (2005) Photosynthetica , vol.43 , pp. 379-393
    • Lichtenthaler, H.K.1    Buschmann, C.2    Knapp, M.3
  • 23
    • 4444319506 scopus 로고    scopus 로고
    • T7 RNA polymerase-directed expression of an antibody fragment transgene in plastids causes a semi-lethal pale-green seedling phenotype
    • Magee AM, Coyne S, Murphy D, Horvath EM, Medgyesy P, Kavanagh TA (2004) T7 RNA polymerase-directed expression of an antibody fragment transgene in plastids causes a semi-lethal pale-green seedling phenotype. Transgenic Res 13:325–337
    • (2004) Transgenic Res , vol.13 , pp. 325-337
    • Magee, A.M.1    Coyne, S.2    Murphy, D.3    Horvath, E.M.4    Medgyesy, P.5    Kavanagh, T.A.6
  • 24
    • 11144248633 scopus 로고    scopus 로고
    • Populations of photo inactivated photosystem II reaction centers characterized by chlorophyll a fluorescence lifetime in vivo
    • Matsubara S, Chow WS (2004) Populations of photo inactivated photosystem II reaction centers characterized by chlorophyll a fluorescence lifetime in vivo. PNAS 101:18234–18239
    • (2004) PNAS , vol.101 , pp. 18234-18239
    • Matsubara, S.1    Chow, W.S.2
  • 25
    • 77957017735 scopus 로고    scopus 로고
    • Nuclear and plastid genetic engineering of plants: Comparison of opportunities and challenges
    • Meyers B, Zaltsman A, Lacroix B, Kozlovsky SV, Krichevsky A (2010) Nuclear and plastid genetic engineering of plants: comparison of opportunities and challenges. Biotechnol Adv 28:747–756
    • (2010) Biotechnol Adv , vol.28 , pp. 747-756
    • Meyers, B.1    Zaltsman, A.2    Lacroix, B.3    Kozlovsky, S.V.4    Krichevsky, A.5
  • 26
    • 84982358134 scopus 로고
    • A revised mediumfor rapid growth and bio assays with tobacco tissue cultures
    • Murashige T, Skoog F (1962) A revised mediumfor rapid growth and bio assays with tobacco tissue cultures. Physiol Plant 15:473–497
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 28
    • 77950337763 scopus 로고    scopus 로고
    • Plant cell wall polymers as precursors for biofuels
    • Pauly M, Keegstra K (2010) Plant cell wall polymers as precursors for biofuels. Curr Opin Plant Biol 13:305–312
    • (2010) Curr Opin Plant Biol , vol.13 , pp. 305-312
    • Pauly, M.1    Keegstra, K.2
  • 29
    • 80054026725 scopus 로고    scopus 로고
    • Postsynthetic modification of plant cell walls by expression of microbial hydrolases in the apoplast
    • Pogorelko G, Fursova O, Lin M, Pyle E, Jass J, Zabotina OA (2011) Postsynthetic modification of plant cell walls by expression of microbial hydrolases in the apoplast. Plant Mol Biol 77:433–445
    • (2011) Plant Mol Biol , vol.77 , pp. 433-445
    • Pogorelko, G.1    Fursova, O.2    Lin, M.3    Pyle, E.4    Jass, J.5    Zabotina, O.A.6
  • 30
    • 80052599264 scopus 로고    scopus 로고
    • The photoprotective molecular switch in the photosystem II antenna
    • Ruban AV, Johnson MP, Duffy CDP (2012) The photoprotective molecular switch in the photosystem II antenna. BBA Bioenergetics 1817: 167–181
    • (2012) BBA Bioenergetics , vol.1817 , pp. 167-181
    • Ruban, A.V.1    Johnson, M.P.2    Duffy, C.3
  • 31
    • 48749115802 scopus 로고    scopus 로고
    • The long-term response to fluctuating light quality is an important and distinct light acclimation mechanism that supports survival of Arabidopsis thaliana under low light conditions
    • Wagner R, Dietzel L, Braeutigam K, Fischer W, Pfannschmidt T (2008) The long-term response to fluctuating light quality is an important and distinct light acclimation mechanism that supports survival of Arabidopsis thaliana under low light conditions. Planta 228:573–587
    • (2008) Planta , vol.228 , pp. 573-587
    • Wagner, R.1    Dietzel, L.2    Braeutigam, K.3    Fischer, W.4    Pfannschmidt, T.5
  • 32
    • 0028007844 scopus 로고
    • The spectral determination of chlorophyll-a and chlorophyll-b, as well as total carotenoids, using various solvents with spectrophotometers of different resolution
    • Wellburn AR (1994) The spectral determination of chlorophyll-a and chlorophyll-b, as well as total carotenoids, using various solvents with spectrophotometers of different resolution. J Plant Physiol 144: 307–313
    • (1994) J Plant Physiol , vol.144 , pp. 307-313
    • Wellburn, A.R.1
  • 33
    • 84864941692 scopus 로고    scopus 로고
    • Green factory: Plants as bioproduction platforms for recombinant proteins
    • Xu J, Dolan MC, Medrano G, Cramer CL, Weathers PJ (2012) Green factory: plants as bioproduction platforms for recombinant proteins. Biotechnol Adv 30:1171–1184
    • (2012) Biotechnol Adv , vol.30 , pp. 1171-1184
    • Xu, J.1    Dolan, M.C.2    Medrano, G.3    Cramer, C.L.4    Weathers, P.J.5
  • 34
    • 84862796517 scopus 로고    scopus 로고
    • Advancements and future directions in enzyme technology for biomass conversion
    • Zhang Z, Donaldson AA, Ma X (2012) Advancements and future directions in enzyme technology for biomass conversion. Biotechnol Adv 30:913–919
    • (2012) Biotechnol Adv , vol.30 , pp. 913-919
    • Zhang, Z.1    Donaldson, A.A.2    Ma, X.3
  • 35
    • 84860176049 scopus 로고    scopus 로고
    • Enzymatic pretreatment of lignocellulosic wastes to improve biogas production
    • Zieminski K, Romanowska I, Kowalska M (2012) Enzymatic pretreatment of lignocellulosic wastes to improve biogas production. Waste Manag 32:1131–1137
    • (2012) Waste Manag , vol.32 , pp. 1131-1137
    • Zieminski, K.1    Romanowska, I.2    Kowalska, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.