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Volumn 91, Issue , 2016, Pages 8-16

Production of glucaric acid from myo-inositol in engineered Pichia pastoris

Author keywords

Glucaric acid; Metabolic engineering; MIOX; Myo inositol; Pichia pastoris

Indexed keywords

ALCOHOLS; BACTERIA; BATCH CELL CULTURE; GLUCOSE; METABOLIC ENGINEERING; SUBSTRATES; YEAST;

EID: 84973102495     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2016.05.009     Document Type: Article
Times cited : (46)

References (38)
  • 1
    • 84881028723 scopus 로고    scopus 로고
    • Toward biotechnological production of adipic acid and precursors from biorenewables
    • Polen T., Spelberg M., Bott M. Toward biotechnological production of adipic acid and precursors from biorenewables. J. Biotechnol. 2013, 167:75-84.
    • (2013) J. Biotechnol. , vol.167 , pp. 75-84
    • Polen, T.1    Spelberg, M.2    Bott, M.3
  • 2
    • 84894639711 scopus 로고    scopus 로고
    • Green and sustainable manufacture of chemicals from biomass: state of the art
    • Sheldon R.A. Green and sustainable manufacture of chemicals from biomass: state of the art. Green. Chem. 2014, 16:950-963.
    • (2014) Green. Chem. , vol.16 , pp. 950-963
    • Sheldon, R.A.1
  • 4
    • 84891045972 scopus 로고    scopus 로고
    • Improving glucaric acid production from myo-inositol in E. coli by increasing MIOX stability and myo-inositol transport
    • Shiue E., Prather K.L.J. Improving glucaric acid production from myo-inositol in E. coli by increasing MIOX stability and myo-inositol transport. Metab. Eng. 2014, 22:22-31.
    • (2014) Metab. Eng. , vol.22 , pp. 22-31
    • Shiue, E.1    Prather, K.L.J.2
  • 5
    • 80051704380 scopus 로고    scopus 로고
    • Engineering microbial factories for synthesis of value-added products
    • Du J., Shao Z., Zhao H. Engineering microbial factories for synthesis of value-added products. J. Ind. Microbiol. Biotechnol. 2011, 38:873-890.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 873-890
    • Du, J.1    Shao, Z.2    Zhao, H.3
  • 6
    • 33845717875 scopus 로고    scopus 로고
    • Vitamin C-biosynthesis, recycling and degradation in mammals
    • Linster C.L., Van Schaftingen E. Vitamin C-biosynthesis, recycling and degradation in mammals. FEBS J. 2007, 274:1-22.
    • (2007) FEBS J. , vol.274 , pp. 1-22
    • Linster, C.L.1    Van Schaftingen, E.2
  • 8
    • 77950863739 scopus 로고    scopus 로고
    • Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. coli
    • Moon T.S., Dueber J.E., Shiue E., Prather K.L.J. Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. coli. Metab. Eng. 2010, 12:298-305.
    • (2010) Metab. Eng. , vol.12 , pp. 298-305
    • Moon, T.S.1    Dueber, J.E.2    Shiue, E.3    Prather, K.L.J.4
  • 9
    • 84922775359 scopus 로고    scopus 로고
    • Improving product yields on glucose in Escherichia coli via knock out of pgi and zwf and feeding of supplemental carbon sources
    • Shiue E., Brockman I.M., Prather K.L.J. Improving product yields on glucose in Escherichia coli via knock out of pgi and zwf and feeding of supplemental carbon sources. Biotechnol. Bioeng. 2015, 112:579-587.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 579-587
    • Shiue, E.1    Brockman, I.M.2    Prather, K.L.J.3
  • 10
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22:1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 11
    • 84909983203 scopus 로고    scopus 로고
    • Multivariate modular engineering of the protein secretory pathway for production of heterologous glucose oxidase in Pichia pastoris
    • Gu L., Zhang J., Du G., Chen J. Multivariate modular engineering of the protein secretory pathway for production of heterologous glucose oxidase in Pichia pastoris. Enzyme Microb. Technol. 2015, 68:33-42.
    • (2015) Enzyme Microb. Technol. , vol.68 , pp. 33-42
    • Gu, L.1    Zhang, J.2    Du, G.3    Chen, J.4
  • 12
    • 84878538709 scopus 로고    scopus 로고
    • Rational design of a novel propeptide for improving active production of Streptomyces griseus trypsin in Pichia pastoris
    • Ling Z., Liu Y., Teng S., Kang Z., Zhang J., Chen J., et al. Rational design of a novel propeptide for improving active production of Streptomyces griseus trypsin in Pichia pastoris. Appl. Environ. Microbiol. 2013, 79:3851-3855.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 3851-3855
    • Ling, Z.1    Liu, Y.2    Teng, S.3    Kang, Z.4    Zhang, J.5    Chen, J.6
  • 13
    • 80051790743 scopus 로고    scopus 로고
    • Combinatorial strategy of sorbitol feeding and low-temperature induction leads to high-level production of alkaline beta-mannanase in Pichia pastoris
    • Zhu T., You L., Gong F., Xie M., Xue Y., Li Y., et al. Combinatorial strategy of sorbitol feeding and low-temperature induction leads to high-level production of alkaline beta-mannanase in Pichia pastoris. Enzyme Microb. Technol. 2011, 49:407-412.
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 407-412
    • Zhu, T.1    You, L.2    Gong, F.3    Xie, M.4    Xue, Y.5    Li, Y.6
  • 16
    • 84899802037 scopus 로고    scopus 로고
    • Production of the sesquiterpenoid (+)-nootkatone by metabolic engineering of Pichia pastoris
    • Wriessnegger T., Augustin P., Engleder M., Leitner E., Muller M., Kaluzna I., et al. Production of the sesquiterpenoid (+)-nootkatone by metabolic engineering of Pichia pastoris. Metab. Eng. 2014, 24:18-29.
    • (2014) Metab. Eng. , vol.24 , pp. 18-29
    • Wriessnegger, T.1    Augustin, P.2    Engleder, M.3    Leitner, E.4    Muller, M.5    Kaluzna, I.6
  • 17
    • 84921059312 scopus 로고    scopus 로고
    • Biochemical characterization of uronate dehydrogenases from three Pseudomonads Chromohalobacter salixigens, and Polaromonas naphthalenivorans
    • Wagschal K., Jordan D.B., Lee C.C., Younger A., Braker J.D., Chan V.J. Biochemical characterization of uronate dehydrogenases from three Pseudomonads Chromohalobacter salixigens, and Polaromonas naphthalenivorans. Enzyme Microb. Technol. 2015, 69:62-68.
    • (2015) Enzyme Microb. Technol. , vol.69 , pp. 62-68
    • Wagschal, K.1    Jordan, D.B.2    Lee, C.C.3    Younger, A.4    Braker, J.D.5    Chan, V.J.6
  • 18
    • 0034496492 scopus 로고    scopus 로고
    • Low-copy plasmids can perform as well as or better than high-copy plasmids for metabolic engineering of bacteria
    • Jones K.L., Kim S.W., Keasling J.D. Low-copy plasmids can perform as well as or better than high-copy plasmids for metabolic engineering of bacteria. Metab. Eng. 2000, 2:328-338.
    • (2000) Metab. Eng. , vol.2 , pp. 328-338
    • Jones, K.L.1    Kim, S.W.2    Keasling, J.D.3
  • 19
    • 0033199419 scopus 로고    scopus 로고
    • Biosynthetic burden and plasmid burden limit expression of chromosomally integrated heterologous genes (pdc adhB) in Escherichia coli
    • Martinez A., York S.W., Yomano L.P., Pineda V.L., Davis F.C., Shelton J.C., et al. Biosynthetic burden and plasmid burden limit expression of chromosomally integrated heterologous genes (pdc adhB) in Escherichia coli. Biotechnol. Prog. 1999, 15:891-897.
    • (1999) Biotechnol. Prog. , vol.15 , pp. 891-897
    • Martinez, A.1    York, S.W.2    Yomano, L.P.3    Pineda, V.L.4    Davis, F.C.5    Shelton, J.C.6
  • 20
    • 65549130083 scopus 로고    scopus 로고
    • Redundancy of enzymes for formaldehyde detoxification in Pseudomonas putida
    • Roca A., Rodriguez-Herva J.J., Ramos J.L. Redundancy of enzymes for formaldehyde detoxification in Pseudomonas putida. J. Bacteriol. 2009, 191:3367-3374.
    • (2009) J. Bacteriol. , vol.191 , pp. 3367-3374
    • Roca, A.1    Rodriguez-Herva, J.J.2    Ramos, J.L.3
  • 21
    • 79551478567 scopus 로고    scopus 로고
    • Diversion of flux toward sesquiterpene production in Saccharomyces cerevisiae by fusion of host and heterologous enzymes
    • Albertsen L., Chen Y., Bach L.S., Rattleff S., Maury J., Brix S., et al. Diversion of flux toward sesquiterpene production in Saccharomyces cerevisiae by fusion of host and heterologous enzymes. Appl. Environ. Microbiol. 2011, 77:1033-1040.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 1033-1040
    • Albertsen, L.1    Chen, Y.2    Bach, L.S.3    Rattleff, S.4    Maury, J.5    Brix, S.6
  • 22
    • 0034788744 scopus 로고    scopus 로고
    • Design of the linkers which effectively separate domains of a bifunctional fusion protein
    • Arai R., Ueda H., Kitayama A., Kamiya N., Nagamune T. Design of the linkers which effectively separate domains of a bifunctional fusion protein. Protein. Eng. 2001, 14:529-532.
    • (2001) Protein. Eng. , vol.14 , pp. 529-532
    • Arai, R.1    Ueda, H.2    Kitayama, A.3    Kamiya, N.4    Nagamune, T.5
  • 23
    • 0004198722 scopus 로고
    • Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli
    • Huston J.S., Levinson D., Mudgett-Hunter M., Tai M.S., Novotny J., Margolies M.N., et al. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 1988, 85:5879-5883.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 5879-5883
    • Huston, J.S.1    Levinson, D.2    Mudgett-Hunter, M.3    Tai, M.S.4    Novotny, J.5    Margolies, M.N.6
  • 24
    • 35048850985 scopus 로고    scopus 로고
    • Strategy for selecting and characterizing linker peptides for CBM9-tagged fusion proteins expressed in Escherichia coli
    • Kavoosi M., Creagh A.L., Kilburn D.G., Haynes C.A. Strategy for selecting and characterizing linker peptides for CBM9-tagged fusion proteins expressed in Escherichia coli. Biotechnol. Bioeng. 2007, 98:599-610.
    • (2007) Biotechnol. Bioeng. , vol.98 , pp. 599-610
    • Kavoosi, M.1    Creagh, A.L.2    Kilburn, D.G.3    Haynes, C.A.4
  • 25
    • 84868198332 scopus 로고    scopus 로고
    • Functional expression of trypsin from Streptomyces griseus by Pichia pastoris
    • Ling Z., Ma T., Li J., Du G., Kang Z., Chen J. Functional expression of trypsin from Streptomyces griseus by Pichia pastoris. J. Ind. Microbiol. Biotechnol. 2012, 39:1651-1662.
    • (2012) J. Ind. Microbiol. Biotechnol. , vol.39 , pp. 1651-1662
    • Ling, Z.1    Ma, T.2    Li, J.3    Du, G.4    Kang, Z.5    Chen, J.6
  • 26
    • 84878266682 scopus 로고    scopus 로고
    • Use of LC-MS/MS for the open detection of steroid metabolites conjugated with glucuronic acid
    • Fabregat A., Pozo O.J., Marcos J., Segura J., Ventura R. Use of LC-MS/MS for the open detection of steroid metabolites conjugated with glucuronic acid. Anal. Chem. 2013, 85:5005-5014.
    • (2013) Anal. Chem. , vol.85 , pp. 5005-5014
    • Fabregat, A.1    Pozo, O.J.2    Marcos, J.3    Segura, J.4    Ventura, R.5
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0035587071 scopus 로고    scopus 로고
    • Myo-inositol oxygenase: molecular cloning and expression of a unique enzyme that oxidizes myo-inositol and chiro-inositol
    • Arner R.J., Prabhu K.S., Thompson J.T., Hildenbrandt G.R., Liken A.D., Reddy C.C. Myo-inositol oxygenase: molecular cloning and expression of a unique enzyme that oxidizes myo-inositol and chiro-inositol. Biochem. J. 2001, 360:313-320.
    • (2001) Biochem. J. , vol.360 , pp. 313-320
    • Arner, R.J.1    Prabhu, K.S.2    Thompson, J.T.3    Hildenbrandt, G.R.4    Liken, A.D.5    Reddy, C.C.6
  • 30
    • 21244440659 scopus 로고    scopus 로고
    • Up-regulation of human myo-inositol oxygenase by hyperosmotic stress in renal proximal tubular epithelial cells
    • Prabhu K.S., Arner R.J., Vunta H., Reddy C.C. Up-regulation of human myo-inositol oxygenase by hyperosmotic stress in renal proximal tubular epithelial cells. J. Biol. Chem. 2005, 280:19895-19901.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19895-19901
    • Prabhu, K.S.1    Arner, R.J.2    Vunta, H.3    Reddy, C.C.4
  • 31
    • 14344261707 scopus 로고    scopus 로고
    • Molecular cloning expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney
    • Arner R.J., Prabhu K.S., Reddy C.C. Molecular cloning expression, and characterization of myo-inositol oxygenase from mouse, rat, and human kidney. Biochem. Biophys. Res. Commun. 2004, 324:1386-1392.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1386-1392
    • Arner, R.J.1    Prabhu, K.S.2    Reddy, C.C.3
  • 32
    • 44649144487 scopus 로고    scopus 로고
    • Bifunctional enhancement of a β-glucanase-xylanase fusion enzyme by optimization of peptide linkers
    • Lu P., Feng M.G. Bifunctional enhancement of a β-glucanase-xylanase fusion enzyme by optimization of peptide linkers. Appl. Microbiol. Biotechnol. 2008, 79:579-587.
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 579-587
    • Lu, P.1    Feng, M.G.2
  • 33
    • 0034869823 scopus 로고    scopus 로고
    • Expression of bifunctional enzymes with xylose reductase and xylitol dehydrogenase activity in Saccharomyces cerevisiae alters product formation during xylose fermentation
    • Anderlund M., Radstrom P., Hahn-Hagerdal B. Expression of bifunctional enzymes with xylose reductase and xylitol dehydrogenase activity in Saccharomyces cerevisiae alters product formation during xylose fermentation. Metab. Eng. 2001, 3:226-235.
    • (2001) Metab. Eng. , vol.3 , pp. 226-235
    • Anderlund, M.1    Radstrom, P.2    Hahn-Hagerdal, B.3
  • 34
    • 84920913613 scopus 로고    scopus 로고
    • Improving and repurposing biocatalysts via directed evolution
    • Denard C.A., Ren H.Q., Zhao H.M. Improving and repurposing biocatalysts via directed evolution. Curr. Opin. Chem. Biol. 2015, 25:55-64.
    • (2015) Curr. Opin. Chem. Biol. , vol.25 , pp. 55-64
    • Denard, C.A.1    Ren, H.Q.2    Zhao, H.M.3
  • 35
    • 84946828928 scopus 로고    scopus 로고
    • Directed evolution combined with synthetic biology strategies expedite semi-rational engineering of genes and genomes
    • Kang Z., Zhang J., Jin P., Yang S. Directed evolution combined with synthetic biology strategies expedite semi-rational engineering of genes and genomes. Bioengineered 2015, 6:136-140.
    • (2015) Bioengineered , vol.6 , pp. 136-140
    • Kang, Z.1    Zhang, J.2    Jin, P.3    Yang, S.4
  • 36
    • 84931574824 scopus 로고    scopus 로고
    • Methods for the directed evolution of proteins
    • Packer M.S., Liu D.R. Methods for the directed evolution of proteins. Nat. Rev. Genet. 2015, 16:379-394.
    • (2015) Nat. Rev. Genet. , vol.16 , pp. 379-394
    • Packer, M.S.1    Liu, D.R.2
  • 38
    • 84889102274 scopus 로고    scopus 로고
    • Hepatoprotective effects of kombucha tea: identification of functional strains and quantification of functional components
    • Wang Y., Ji B.P., Wu W., Wang R.J., Yang Z.W., Zhang D., et al. Hepatoprotective effects of kombucha tea: identification of functional strains and quantification of functional components. J. Sci. Food. Agric. 2014, 94:265-272.
    • (2014) J. Sci. Food. Agric. , vol.94 , pp. 265-272
    • Wang, Y.1    Ji, B.P.2    Wu, W.3    Wang, R.J.4    Yang, Z.W.5    Zhang, D.6


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