메뉴 건너뛰기




Volumn 113, Issue 2, 2013, Pages 217-225

Production of milk-derived bioactive peptides as precursor chimeric proteins in chloroplasts of Chlamydomonas reinhardtii

Author keywords

Chimeric protein; Chloroplast gene expression; Nutraceutic; Transgenic

Indexed keywords

GENE EXPRESSION; MICROORGANISMS; PEPTIDES;

EID: 84876195872     PISSN: 01676857     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11240-012-0261-3     Document Type: Article
Times cited : (18)

References (45)
  • 1
    • 79952698383 scopus 로고    scopus 로고
    • Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides
    • Agyei D, Danquah K (2011) Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides. Biotechnol Adv 29: 272-277.
    • (2011) Biotechnol Adv , vol.29 , pp. 272-277
    • Agyei, D.1    Danquah, K.2
  • 2
    • 28544435241 scopus 로고    scopus 로고
    • Contribution of 50 and 30 untranslated regions of plastid mRNAs to the expression of Chlamydomonas reinhardtii chloroplast genes
    • Barnes D, Franklin S, Schultz J, Henry R, Brown E, Coragliotti A, Mayfield SP (2005) Contribution of 50 and 30 untranslated regions of plastid mRNAs to the expression of Chlamydomonas reinhardtii chloroplast genes. Mol Genet Genomics 274: 625-636.
    • (2005) Mol Genet Genomics , vol.274 , pp. 625-636
    • Barnes, D.1    Franklin, S.2    Schultz, J.3    Henry, R.4    Brown, E.5    Coragliotti, A.6    Mayfield, S.P.7
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantification 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
  • 4
    • 0032877220 scopus 로고    scopus 로고
    • Characterization of the dimer-monomer equilibrium of the papaya copper/zinc superoxide dismutase and its equilibrium shift by a single aminoacid mutation
    • Chi-Tsai L, Ti-Jung K, Jei-Fu S, Ming-Ching K (1999) Characterization of the dimer-monomer equilibrium of the papaya copper/zinc superoxide dismutase and its equilibrium shift by a single aminoacid mutation. J Agric Food Chem 47: 2944-2949.
    • (1999) J Agric Food Chem , vol.47 , pp. 2944-2949
    • Chi-Tsai, L.1    Ti-Jung, K.2    Jei-Fu, S.3    Ming-Ching, K.4
  • 5
    • 16544362025 scopus 로고    scopus 로고
    • Chloroplast genetic engineering to improve agronomic traits
    • L. Peña (Ed.), Totowa: Humana Press Inc
    • Daniell H, Ruiz O, Dhingra A (2004) Chloroplast genetic engineering to improve agronomic traits. In: Peña L (ed) Transgenic plants: methods and protocols, vol 286. Humana Press Inc., Totowa, pp 111-137.
    • (2004) Transgenic Plants: Methods and Protocols , vol.286 , pp. 111-137
    • Daniell, H.1    Ruiz, O.2    Dhingra, A.3
  • 6
    • 0035032249 scopus 로고    scopus 로고
    • When transgenes wander, should we worry?
    • Ellstrand NC (2001) When transgenes wander, should we worry? Plant Physiol 125: 1543-1545.
    • (2001) Plant Physiol , vol.125 , pp. 1543-1545
    • Ellstrand, N.C.1
  • 7
    • 43449123620 scopus 로고    scopus 로고
    • High-density seedling expression system for the production of bioactive human cardiotrophin-1, a potential therapeutic cytokine, in transgenic tobacco chloroplasts
    • Farran I, Rio-Manterola F, Iniguez M, Garate S, Prieto J, Mingo-Castel AM (2008) High-density seedling expression system for the production of bioactive human cardiotrophin-1, a potential therapeutic cytokine, in transgenic tobacco chloroplasts. Plant Biotechnol J 6: 516-527.
    • (2008) Plant Biotechnol J , vol.6 , pp. 516-527
    • Farran, I.1    Rio-Manterola, F.2    Iniguez, M.3    Garate, S.4    Prieto, J.5    Mingo-Castel, A.M.6
  • 8
    • 0025766849 scopus 로고
    • Transgenic expression of aminoglycoside adenine transferase in the chloroplast: a selectable marker for site-directed transformation of Chlamydomonas
    • Goldschmidt-Clermont M (1991) Transgenic expression of aminoglycoside adenine transferase in the chloroplast: a selectable marker for site-directed transformation of Chlamydomonas. Nucl Acids Res 19: 4083-4089.
    • (1991) Nucl Acids Res , vol.19 , pp. 4083-4089
    • Goldschmidt-Clermont, M.1
  • 9
    • 84855190526 scopus 로고    scopus 로고
    • Microalgae as platforms for production of recombinant proteins and valuable compounds: progress and prospects
    • Gong Y, Hu H, Gao Y, Xu X, Gao H (2011) Microalgae as platforms for production of recombinant proteins and valuable compounds: progress and prospects. J Ind Microbiol Biotechnol 38: 1879-1890.
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 1879-1890
    • Gong, Y.1    Hu, H.2    Gao, Y.3    Xu, X.4    Gao, H.5
  • 10
    • 33845919888 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii: a protein expression system for pharmaceutical and biotechnological proteins
    • Griesbeck C, Kobl I, Heitzer M (2006) Chlamydomonas reinhardtii: a protein expression system for pharmaceutical and biotechnological proteins. Mol Biotechnol 34: 213-223.
    • (2006) Mol Biotechnol , vol.34 , pp. 213-223
    • Griesbeck, C.1    Kobl, I.2    Heitzer, M.3
  • 11
    • 0036394055 scopus 로고    scopus 로고
    • Preparation of ovine and caprine β-Lg hydrolysates with ACE-inhibitory activity. Identification of active peptides from β-Lg hydrolysed with thermolysin
    • Hernandez-Ledesma B, Recio I, Ramos M, Amigo L (2002) Preparation of ovine and caprine β-Lg hydrolysates with ACE-inhibitory activity. Identification of active peptides from β-Lg hydrolysed with thermolysin. Int Dairy J 12: 805-812.
    • (2002) Int Dairy J , vol.12 , pp. 805-812
    • Hernandez-Ledesma, B.1    Recio, I.2    Ramos, M.3    Amigo, L.4
  • 12
    • 13244277961 scopus 로고    scopus 로고
    • Preparation of antioxidant enzymatic hydrolyzates from α-lactalbumin and β-lactoglobulin. Identification of peptides by HPLC-MS/MS
    • Hernandez-Ledesma B, Davalos A, Bartolome B, Amigo L (2005) Preparation of antioxidant enzymatic hydrolyzates from α-lactalbumin and β-lactoglobulin. Identification of peptides by HPLC-MS/MS. J Agric Food Chem 53: 588-593.
    • (2005) J Agric Food Chem , vol.53 , pp. 588-593
    • Hernandez-Ledesma, B.1    Davalos, A.2    Bartolome, B.3    Amigo, L.4
  • 13
    • 35348827743 scopus 로고    scopus 로고
    • Effect of simulated gastrointestinal digestion on the antihypertensive properties of β-lactoglobulin peptides
    • Hernandez-Ledesma B, Miguel M, Amigo L, Aleixandre MA, Recio I (2007a) Effect of simulated gastrointestinal digestion on the antihypertensive properties of β-lactoglobulin peptides. J Dairy Res 74: 336-339.
    • (2007) J Dairy Res , vol.74 , pp. 336-339
    • Hernandez-Ledesma, B.1    Miguel, M.2    Amigo, L.3    Aleixandre, M.A.4    Recio, I.5
  • 14
    • 34249339084 scopus 로고    scopus 로고
    • ACE-inhibitory and radical scavenging activity of peptides derived from β-lactoglobulin
    • Hernandez-Ledesma B, Recio I, Amigo L, Bartolomé B (2007b) ACE-inhibitory and radical scavenging activity of peptides derived from β-lactoglobulin. J Agric Food Chem 55: 3392-3397.
    • (2007) J Agric Food Chem , vol.55 , pp. 3392-3397
    • Hernandez-Ledesma, B.1    Recio, I.2    Amigo, L.3    Bartolomé, B.4
  • 15
    • 0034977585 scopus 로고    scopus 로고
    • Genetic engineering and accelerated plant improvement: opportunities and challenges
    • Jauhar PP (2001) Genetic engineering and accelerated plant improvement: opportunities and challenges. Plant Cell Tiss Organ Cult 64: 87-89.
    • (2001) Plant Cell Tiss Organ Cult , vol.64 , pp. 87-89
    • Jauhar, P.P.1
  • 17
    • 0141575314 scopus 로고    scopus 로고
    • Expression of milk-derived antihypertensive peptide in Escherichia coli
    • Lev GS, Huo GC, Fu XY (2003) Expression of milk-derived antihypertensive peptide in Escherichia coli. J Dairy Sci 86: 1927-1931.
    • (2003) J Dairy Sci , vol.86 , pp. 1927-1931
    • Lev, G.S.1    Huo, G.C.2    Fu, X.Y.3
  • 18
    • 3242774456 scopus 로고    scopus 로고
    • Shrestha, angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
    • Li GH, Le GW, Shi YH (2004) Shrestha, angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr Res 24: 469-486.
    • (2004) Nutr Res , vol.24 , pp. 469-486
    • Li, G.H.1    Le, G.W.2    Shi, Y.H.3
  • 19
    • 34447310561 scopus 로고    scopus 로고
    • High-level expression of milk-derived antihypertensive peptide in Escherichia coli and its bioactivity
    • Liu D, Sun HY, Zhang LJ, Li SM (2007) High-level expression of milk-derived antihypertensive peptide in Escherichia coli and its bioactivity. J Agric Food Chem 55: 5109-5112.
    • (2007) J Agric Food Chem , vol.55 , pp. 5109-5112
    • Liu, D.1    Sun, H.Y.2    Zhang, L.J.3    Li, S.M.4
  • 22
    • 55949087097 scopus 로고    scopus 로고
    • Plastid transformation of high-biomass tobacco variety Maryland mammoth for production of human immunodeficiency virus type 1 (HIV-1) p24 antigen
    • McCabe MS, Klaas M, Gonzalez-Rabade N, Poage M, Badillo-Corona JA, Zhou F (2008) Plastid transformation of high-biomass tobacco variety Maryland mammoth for production of human immunodeficiency virus type 1 (HIV-1) p24 antigen. Plant Biotechnol J 6: 914-929.
    • (2008) Plant Biotechnol J , vol.6 , pp. 914-929
    • McCabe, M.S.1    Klaas, M.2    Gonzalez-Rabade, N.3    Poage, M.4    Badillo-Corona, J.A.5    Zhou, F.6
  • 23
    • 0031055268 scopus 로고    scopus 로고
    • Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β-lactoglobulin
    • Mullally MM, Meisel H, Fitzgerald RJ (1997) Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β-lactoglobulin. FEBS Lett 402: 99-101.
    • (1997) FEBS Lett , vol.402 , pp. 99-101
    • Mullally, M.M.1    Meisel, H.2    Fitzgerald, R.J.3
  • 24
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production
    • Murray BA, FitzGerald RJ (2007) Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Curr Pharm Des 13: 773-791.
    • (2007) Curr Pharm Des , vol.13 , pp. 773-791
    • Murray, B.A.1    FitzGerald, R.J.2
  • 25
    • 62149100748 scopus 로고    scopus 로고
    • High-level expression of active human alpha1-antitrypsin in transgenic tobacco chloroplasts
    • Nadai M, Bally J, Vitel M, Job C, Tissot G, Botterman J (2009) High-level expression of active human alpha1-antitrypsin in transgenic tobacco chloroplasts. Transgenic Res 18: 173-183.
    • (2009) Transgenic Res , vol.18 , pp. 173-183
    • Nadai, M.1    Bally, J.2    Vitel, M.3    Job, C.4    Tissot, G.5    Botterman, J.6
  • 27
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin
    • Pellegrini A, Dettling C, Thomas U, Hunziker P (2001) Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochim Biophys Acta 1526: 131-140.
    • (2001) Biochim Biophys Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 28
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides
    • Pihlanto-Leppala A (2001) Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides. Trends Food Sci Tech 11: 347-356.
    • (2001) Trends Food Sci Tech , vol.11 , pp. 347-356
    • Pihlanto-Leppala, A.1
  • 29
    • 0032047290 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins
    • Pihlanto-Leppala A, Rokka T, Korhonen H (1998) Angiotensin I converting enzyme inhibitory peptides derived from bovine milk proteins. Int Dairy J 8: 325-331.
    • (1998) Int Dairy J , vol.8 , pp. 325-331
    • Pihlanto-Leppala, A.1    Rokka, T.2    Korhonen, H.3
  • 30
    • 0034141231 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides
    • Pihlanto-Leppala A, Koskinen P, Piilola K, Tupasela T, Coronen H (2000) Angiotensin-I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. J Dairy Res 67: 53-64.
    • (2000) J Dairy Res , vol.67 , pp. 53-64
    • Pihlanto-Leppala, A.1    Koskinen, P.2    Piilola, K.3    Tupasela, T.4    Coronen, H.5
  • 33
    • 84856953016 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii as a viable platform for the production of recombinant proteins: current status and perspectives
    • Rosales-Mendoza S, Paz-Maldonado LM, Soria-Guerra RE (2012b) Chlamydomonas reinhardtii as a viable platform for the production of recombinant proteins: current status and perspectives. Plant Cell Rep 31: 479-494.
    • (2012) Plant Cell Rep , vol.31 , pp. 479-494
    • Rosales-Mendoza, S.1    Paz-Maldonado, L.M.2    Soria-Guerra, R.E.3
  • 36
    • 0033828099 scopus 로고    scopus 로고
    • Bioactive peptides in dairy products: synthesis and interaction with proteolytic enzymes
    • Smacchi E, Gobbetti M (2000) Bioactive peptides in dairy products: synthesis and interaction with proteolytic enzymes. Food Microbiol 17: 129-141.
    • (2000) Food Microbiol , vol.17 , pp. 129-141
    • Smacchi, E.1    Gobbetti, M.2
  • 37
    • 77956747852 scopus 로고    scopus 로고
    • Micro-algae come of age as a platform for recombinant protein production
    • Specht E, Miyake-Stoner S, Mayfield S (2010) Micro-algae come of age as a platform for recombinant protein production. Biotechnol Lett 32: 1373-1383.
    • (2010) Biotechnol Lett , vol.32 , pp. 1373-1383
    • Specht, E.1    Miyake-Stoner, S.2    Mayfield, S.3
  • 38
    • 0042862830 scopus 로고    scopus 로고
    • Foot-and mouth disease virus VP1 protein fused with cholera toxin B subunit expressed in Chlamydomonas reinhardtii chloroplast
    • Sun M, Qian K, Su N, Chang H, Liu J, Shen G (2003) Foot-and mouth disease virus VP1 protein fused with cholera toxin B subunit expressed in Chlamydomonas reinhardtii chloroplast. Biotechnol Lett 25: 1087-1092.
    • (2003) Biotechnol Lett , vol.25 , pp. 1087-1092
    • Sun, M.1    Qian, K.2    Su, N.3    Chang, H.4    Liu, J.5    Shen, G.6
  • 40
    • 12344325123 scopus 로고    scopus 로고
    • Recent developments in the use of transgenic plants for the production of human therapeutics and biopharmaceuticals
    • Teli NP, Timko MP (2004) Recent developments in the use of transgenic plants for the production of human therapeutics and biopharmaceuticals. Plant Cell Tiss Organ Cult 79: 125-145.
    • (2004) Plant Cell Tiss Organ Cult , vol.79 , pp. 125-145
    • Teli, N.P.1    Timko, M.P.2
  • 41
    • 77951055907 scopus 로고    scopus 로고
    • Oral delivery of bioencapsulated coagulation factor IX prevents inhibitor formation and fatal anaphylaxis in hemophilia B mice
    • Verma D, Moghimi B, LoDuca PA, Singh HD, Hoffman BE, Herzog RW (2010) Oral delivery of bioencapsulated coagulation factor IX prevents inhibitor formation and fatal anaphylaxis in hemophilia B mice. Proc Natl Acad Sci USA 107: 7101-7106.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7101-7106
    • Verma, D.1    Moghimi, B.2    LoDuca, P.A.3    Singh, H.D.4    Hoffman, B.E.5    Herzog, R.W.6
  • 42
    • 51749125991 scopus 로고    scopus 로고
    • Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the anti-hypertensive effect of hydrolysate in spontaneously hypertensive rats
    • Wang JP, Hu JE, Cui JZ, Bai XF, Du YG, Miyaguchi Y, Lin BC (2008) Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the anti-hypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem 111: 302-308.
    • (2008) Food Chem , vol.111 , pp. 302-308
    • Wang, J.P.1    Hu, J.E.2    Cui, J.Z.3    Bai, X.F.4    Du, Y.G.5    Miyaguchi, Y.6    Lin, B.C.7
  • 43
    • 0032222184 scopus 로고    scopus 로고
    • Bioactive peptides in milk and their biological and health implications
    • Xu RJ (1998) Bioactive peptides in milk and their biological and health implications. Food Rev Int 14: 1-16.
    • (1998) Food Rev Int , vol.14 , pp. 1-16
    • Xu, R.J.1
  • 44
    • 0041317810 scopus 로고    scopus 로고
    • Characterization of β-lactotensin, a bioactive peptide derived from bovine β-lactoglobulin, as a neurotensin agonist
    • Yamauchi R, Usui H, Yunden J, Takenaka Y, Tani F, Yoshikawa M (2003) Characterization of β-lactotensin, a bioactive peptide derived from bovine β-lactoglobulin, as a neurotensin agonist. Biosci Biotechnol Biochem 67: 940-943.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 940-943
    • Yamauchi, R.1    Usui, H.2    Yunden, J.3    Takenaka, Y.4    Tani, F.5    Yoshikawa, M.6
  • 45
    • 84878362996 scopus 로고    scopus 로고
    • Manufacturing of peptides exhibiting biological activity
    • doi: 10. 1007/s00726-012-1379-7
    • Zambrowicz A, Timmer M, Polanowski A, Lubec G, Trziszka T (2012) Manufacturing of peptides exhibiting biological activity. Amino Acids. doi: 10. 1007/s00726-012-1379-7.
    • (2012) Amino Acids
    • Zambrowicz, A.1    Timmer, M.2    Polanowski, A.3    Lubec, G.4    Trziszka, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.