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Volumn 100, Issue 3, 2016, Pages 1365-1376

Evaluation of 3-hydroxybutyrate as an enzyme-protective agent against heating and oxidative damage and its potential role in stress response of poly(3-hydroxybutyrate) accumulating cells

Author keywords

3 Hydroxybutyrate; Chemical chaperone; Compatible solutes; PHB; PHB cycle; Poly(3 hydroxybutyrate)

Indexed keywords

CARBON; DIFFERENTIAL SCANNING CALORIMETRY; DYNAMIC LIGHT SCATTERING; LIGHT SCATTERING; METABOLISM;

EID: 84955212772     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-7162-4     Document Type: Article
Times cited : (67)

References (44)
  • 1
    • 0034525598 scopus 로고    scopus 로고
    • Stabilizing effect of chemical additives against oxidation of lactate dehydrogenase
    • PID: 11115385, COI: 1:CAS:528:DC%2BD3MXktVGrsQ%3D%3D
    • Andersson MM, Breccia JD, Hatti-Kaul R (2000) Stabilizing effect of chemical additives against oxidation of lactate dehydrogenase. Biotechnol Appl Biochem 32:145–153
    • (2000) Biotechnol Appl Biochem , vol.32 , pp. 145-153
    • Andersson, M.M.1    Breccia, J.D.2    Hatti-Kaul, R.3
  • 2
    • 35349002347 scopus 로고    scopus 로고
    • The polyhydroxyalkanoate genes of a stress resistant Antarctic Pseudomonas are situated within a genomic island
    • PID: 17629557, COI: 1:CAS:528:DC%2BD2sXht1WqtLnN
    • Ayub ND, Pettinari MJ, Mendez BS, Lopez NI (2007) The polyhydroxyalkanoate genes of a stress resistant Antarctic Pseudomonas are situated within a genomic island. Plasmid 58:240–248
    • (2007) Plasmid , vol.58 , pp. 240-248
    • Ayub, N.D.1    Pettinari, M.J.2    Mendez, B.S.3    Lopez, N.I.4
  • 3
    • 58149204233 scopus 로고    scopus 로고
    • Polyhydroxyalkanoates are essential for maintenance of redox state in the Antarctic bacterium Pseudomonas sp. 14–3 during low temperature adaptation
    • PID: 18931822, COI: 1:CAS:528:DC%2BD1cXhsFCgsL7N
    • Ayub ND, Tribelli PM, Lopez NI (2009) Polyhydroxyalkanoates are essential for maintenance of redox state in the Antarctic bacterium Pseudomonas sp. 14–3 during low temperature adaptation. Extremophiles 13:59–66
    • (2009) Extremophiles , vol.13 , pp. 59-66
    • Ayub, N.D.1    Tribelli, P.M.2    Lopez, N.I.3
  • 4
    • 31144446559 scopus 로고    scopus 로고
    • ZERO calibrated modulated temperature differential scanning calorimetry to characterize model protein formulations
    • PID: 16386393, COI: 1:CAS:528:DC%2BD28XnvVWgsg%3D%3D
    • ZERO calibrated modulated temperature differential scanning calorimetry to characterize model protein formulations. Int J Pharm 309:146–156
    • (2006) Int J Pharm , vol.309 , pp. 146-156
    • Badkar, A.1    Yohannes, P.2    Banga, A.3
  • 5
    • 0034082797 scopus 로고    scopus 로고
    • Compatible-solutes-supported periplasmic expression of functional recombinant proteins under stress conditions
    • COI: 1:CAS:528:DC%2BD3cXisVWmtL0%3D
    • Barth S, Huhn M, Matthey B, Klimka A, Galinski EA, Engert A (2000) Compatible-solutes-supported periplasmic expression of functional recombinant proteins under stress conditions. Appl Microbiol Biotechnol 66:1572–1579
    • (2000) Appl Microbiol Biotechnol , vol.66 , pp. 1572-1579
    • Barth, S.1    Huhn, M.2    Matthey, B.3    Klimka, A.4    Galinski, E.A.5    Engert, A.6
  • 6
    • 68049100110 scopus 로고    scopus 로고
    • Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
    • PID: 19561621, COI: 1:CAS:528:DC%2BD1MXnslKqtLc%3D
    • Bennett BD, Kimball EH, Gao M, Osterhout R, Van Dien SJ, Rabinowitz JD (2009) Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat Chem Biol 5:593–599
    • (2009) Nat Chem Biol , vol.5 , pp. 593-599
    • Bennett, B.D.1    Kimball, E.H.2    Gao, M.3    Osterhout, R.4    Van Dien, S.J.5    Rabinowitz, J.D.6
  • 7
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: natural selection of a thermodynamic force in protein folding
    • PID: 11502004, COI: 1:CAS:528:DC%2BD3MXmslShtbo%3D
    • Bolen DW, Baskakov IV (2001) The osmophobic effect: natural selection of a thermodynamic force in protein folding. J Mol Biol 310:955–963
    • (2001) J Mol Biol , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 8
    • 0036599177 scopus 로고    scopus 로고
    • Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes
    • PID: 12072956, COI: 1:CAS:528:DC%2BD38XltlGksLs%3D
    • Borges N, Ramos A, Raven NDH, Sharp RJ, Santos H (2002) Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes. Extremophiles 6:209–216
    • (2002) Extremophiles , vol.6 , pp. 209-216
    • Borges, N.1    Ramos, A.2    Raven, N.D.H.3    Sharp, R.J.4    Santos, H.5
  • 9
    • 84868618672 scopus 로고    scopus 로고
    • Whole-genome microarray and gene deletion studies reveal regulation of the polyhydroxyalkanoate production cycle by the stringent response in Ralstonia eutropha H16
    • PID: 22961894, COI: 1:CAS:528:DC%2BC38Xhs1eisr%2FJ
    • Brigham CJ, Speth DR, Rha CK, Sinskey AJ (2012) Whole-genome microarray and gene deletion studies reveal regulation of the polyhydroxyalkanoate production cycle by the stringent response in Ralstonia eutropha H16. Appl Environ Microbiol 78:8033–8044
    • (2012) Appl Environ Microbiol , vol.78 , pp. 8033-8044
    • Brigham, C.J.1    Speth, D.R.2    Rha, C.K.3    Sinskey, A.J.4
  • 10
    • 0021278385 scopus 로고
    • Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation
    • PID: 6426525, COI: 1:CAS:528:DyaL2cXktlGjtbk%3D
    • Busby TF, Ingham KC (1984) Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation. Biochim Biophys Acta 799:80–89
    • (1984) Biochim Biophys Acta , vol.799 , pp. 80-89
    • Busby, T.F.1    Ingham, K.C.2
  • 11
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis RJ (2001) Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 10:597–604
    • (2001) Trends Biochem Sci , vol.10 , pp. 597-604
    • Ellis, R.J.1
  • 12
    • 55049115053 scopus 로고    scopus 로고
    • Design of new enzyme stabilizers inspired by glycosides of hyperthermophilic microorganisms
    • PID: 18822412, COI: 1:CAS:528:DC%2BD1cXhtlOhtr3E
    • Faria TQ, Mingote A, Siopa F, Ventura R, Maycock C, Santos H (2008) Design of new enzyme stabilizers inspired by glycosides of hyperthermophilic microorganisms. Carbohydr Res 343:3025–3033
    • (2008) Carbohydr Res , vol.343 , pp. 3025-3033
    • Faria, T.Q.1    Mingote, A.2    Siopa, F.3    Ventura, R.4    Maycock, C.5    Santos, H.6
  • 13
    • 84896319714 scopus 로고    scopus 로고
    • Enhancement of stress tolerance in polyhydroxyalkanoate producers without mobilization of the accumulated granules
    • PID: 24233544, COI: 1:CAS:528:DC%2BC3sXhslKqsrzI
    • Goh L-K, Purama RK, Sudesh K (2014) Enhancement of stress tolerance in polyhydroxyalkanoate producers without mobilization of the accumulated granules. Appl Biochem Biotechnol 172:1585–1598
    • (2014) Appl Biochem Biotechnol , vol.172 , pp. 1585-1598
    • Goh, L.-K.1    Purama, R.K.2    Sudesh, K.3
  • 14
    • 0039801358 scopus 로고    scopus 로고
    • Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solutes additives
    • COI: 1:CAS:528:DyaK1MXlsFyjt7k%3D
    • Goller K, Galinski EA (1999) Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solutes additives. J Mol Catal B: Enzym 7:37–45
    • (1999) J Mol Catal B: Enzym , vol.7 , pp. 37-45
    • Goller, K.1    Galinski, E.A.2
  • 15
    • 44949190443 scopus 로고    scopus 로고
    • s, affects polyhydroxyalkanoate metabolism in Pseudomonas putida
    • s, affects polyhydroxyalkanoate metabolism in Pseudomonas putida. FEMS Microbiol Lett 284:218–224
    • (2008) FEMS Microbiol Lett , vol.284 , pp. 218-224
    • Iustman, L.J.R.1    Ruiz, J.A.2
  • 16
    • 84919762170 scopus 로고    scopus 로고
    • Genome sequence analysis of Pseudomonas extremaustralis provides new insights into environmental adaptability and extreme conditions resistance
    • Iustman LJR, Tribelli PM, Ibarra JG, Catone MV, Venero ECS, Lopez NI (2015) Genome sequence analysis of Pseudomonas extremaustralis provides new insights into environmental adaptability and extreme conditions resistance. Extremophiles 19:207–220
    • (2015) Extremophiles , vol.19 , pp. 207-220
    • Iustman, L.J.R.1    Tribelli, P.M.2    Ibarra, J.G.3    Catone, M.V.4    Venero, E.C.S.5    Lopez, N.I.6
  • 17
    • 58149477054 scopus 로고    scopus 로고
    • Effect of trehalose on protein structure
    • PID: 19177348, COI: 1:CAS:528:DC%2BD1MXmslCiuro%3D
    • Jain NK, Roy I (2009) Effect of trehalose on protein structure. Protein Sci 18:24–36
    • (2009) Protein Sci , vol.18 , pp. 24-36
    • Jain, N.K.1    Roy, I.2
  • 18
    • 0036271335 scopus 로고    scopus 로고
    • Identification and isolation of genes involved in poly(beta-hydroxybutyrate) biosynthesis in Azospirillum brasilense and characterization of a phbC mutant
    • PID: 12039753, COI: 1:CAS:528:DC%2BD38XksVWqtrs%3D
    • Kadouri D, Burdman S, Jurkevitch E, Okon Y (2002) Identification and isolation of genes involved in poly(beta-hydroxybutyrate) biosynthesis in Azospirillum brasilense and characterization of a phbC mutant. Appl Environ Microbiol 68:2943–2949
    • (2002) Appl Environ Microbiol , vol.68 , pp. 2943-2949
    • Kadouri, D.1    Burdman, S.2    Jurkevitch, E.3    Okon, Y.4
  • 19
    • 0242408950 scopus 로고    scopus 로고
    • Poly beta-hydroxybutyrate depolymerase (PhaZ) in Azospirillum brasilense and characterization of a phaZ mutant
    • PID: 12898135, COI: 1:CAS:528:DC%2BD3sXovVKnurw%3D
    • Kadouri D, Jurkevitch E, Okon Y (2003) Poly beta-hydroxybutyrate depolymerase (PhaZ) in Azospirillum brasilense and characterization of a phaZ mutant. Arch Microbiol 180:309–318
    • (2003) Arch Microbiol , vol.180 , pp. 309-318
    • Kadouri, D.1    Jurkevitch, E.2    Okon, Y.3
  • 20
    • 19944369426 scopus 로고    scopus 로고
    • Ecological and agricultural significance of bacterial polyhydroxyalkanoates
    • PID: 15986831, COI: 1:CAS:528:DC%2BD2MXjvVOltrw%3D
    • Kadouri D, Jurkevitch E, Okon Y (2005) Ecological and agricultural significance of bacterial polyhydroxyalkanoates. Crit Rev Microbiol 31:55–67
    • (2005) Crit Rev Microbiol , vol.31 , pp. 55-67
    • Kadouri, D.1    Jurkevitch, E.2    Okon, Y.3
  • 21
    • 0032924058 scopus 로고    scopus 로고
    • A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions
    • PID: 10210200, COI: 1:CAS:528:DyaK1MXlsFCitQ%3D%3D
    • Kaushik JK, Bhat R (1999) A mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions. Protein Sci 8:222–233
    • (1999) Protein Sci , vol.8 , pp. 222-233
    • Kaushik, J.K.1    Bhat, R.2
  • 22
    • 33746083974 scopus 로고    scopus 로고
    • Compatible solutes as protectants for zymogenes against proteolysis
    • PID: 16797260, COI: 1:CAS:528:DC%2BD28Xnt1ymtrc%3D
    • Kolp S, Pietsch M, Galinski EA, Gutschow M (2006) Compatible solutes as protectants for zymogenes against proteolysis. Biochim Biophys Acta 1764:1234–1242
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1234-1242
    • Kolp, S.1    Pietsch, M.2    Galinski, E.A.3    Gutschow, M.4
  • 23
    • 36549004138 scopus 로고    scopus 로고
    • Stress responses of bacteria
    • PID: 17920859, COI: 1:CAS:528:DC%2BD2sXhtlyktLbN
    • Marles-Wright J, Lewis RJ (2007) Stress responses of bacteria. Curr Opin Struct Biol 17:755–760
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 755-760
    • Marles-Wright, J.1    Lewis, R.J.2
  • 24
    • 0345357141 scopus 로고    scopus 로고
    • Solute accumulation in the deep-sea bacterium Photobacterium profundum
    • PID: 12486460, COI: 1:CAS:528:DC%2BD38XpsFKrtL4%3D
    • Martin DD, Bartlett DH, Roberts MF (2002) Solute accumulation in the deep-sea bacterium Photobacterium profundum. Extremophiles 6:507–514
    • (2002) Extremophiles , vol.6 , pp. 507-514
    • Martin, D.D.1    Bartlett, D.H.2    Roberts, M.F.3
  • 25
    • 35148874214 scopus 로고    scopus 로고
    • Hydration in protein folding: thermal unfolding/refolding of human serum albumin
    • PID: 17711315, COI: 1:CAS:528:DC%2BD2sXpt1Witbc%3D
    • Mitra RK, Sinha SS, Pal SK (2007) Hydration in protein folding: thermal unfolding/refolding of human serum albumin. Langmuir 23:10224–10229
    • (2007) Langmuir , vol.23 , pp. 10224-10229
    • Mitra, R.K.1    Sinha, S.S.2    Pal, S.K.3
  • 26
    • 55949110298 scopus 로고    scopus 로고
    • Thermodynamic, kinetic, and operational stabilities of yeast alcohol dehydrogenase in sugar and compatible osmolyte solutions
    • COI: 1:CAS:528:DC%2BD1cXhsVSgsbrI
    • Miyawaki O, Ma GL, Horie T, Hibi A, Ishikawa T, Kimura S (2008) Thermodynamic, kinetic, and operational stabilities of yeast alcohol dehydrogenase in sugar and compatible osmolyte solutions. Enzyme Microb Technol 43:495–499
    • (2008) Enzyme Microb Technol , vol.43 , pp. 495-499
    • Miyawaki, O.1    Ma, G.L.2    Horie, T.3    Hibi, A.4    Ishikawa, T.5    Kimura, S.6
  • 27
    • 0344875683 scopus 로고    scopus 로고
    • Oxidative inactivation of paraoxonase1, an antioxidant protein and its effect on antioxidant action
    • PID: 14753756, COI: 1:CAS:528:DC%2BD3sXpsVCls7o%3D
    • Nguyen SD, Sok DE (2003) Oxidative inactivation of paraoxonase1, an antioxidant protein and its effect on antioxidant action. Free Radic Res 37:1319–1330
    • (2003) Free Radic Res , vol.37 , pp. 1319-1330
    • Nguyen, S.D.1    Sok, D.E.2
  • 28
    • 77953715749 scopus 로고    scopus 로고
    • Effect of ethanol and hydrogen peroxide on poly(3-hydroxybutyrate) biosynthetic pathway in Cupriavidus necator H16
    • PID: 24026931, COI: 1:CAS:528:DC%2BC3cXntlOhs7k%3D
    • Obruca S, Marova I, Stankova M, Mravcova L, Svoboda Z (2010a) Effect of ethanol and hydrogen peroxide on poly(3-hydroxybutyrate) biosynthetic pathway in Cupriavidus necator H16. World J Microbiol Biotechnol 26:1261–1267
    • (2010) World J Microbiol Biotechnol , vol.26 , pp. 1261-1267
    • Obruca, S.1    Marova, I.2    Stankova, M.3    Mravcova, L.4    Svoboda, Z.5
  • 29
    • 77949906673 scopus 로고    scopus 로고
    • Use of controlled exogenous stress for improvement of poly(3-hydroxybutyrate) production in Wautersia eutropha: a preliminary study
    • COI: 1:CAS:528:DC%2BC3cXjvVGmsLs%3D
    • Obruca S, Marova I, Svoboda Z, Mikulikova R (2010b) Use of controlled exogenous stress for improvement of poly(3-hydroxybutyrate) production in Wautersia eutropha: a preliminary study. Folia Microbiol 55:17–22
    • (2010) Folia Microbiol , vol.55 , pp. 17-22
    • Obruca, S.1    Marova, I.2    Svoboda, Z.3    Mikulikova, R.4
  • 30
    • 84903593978 scopus 로고    scopus 로고
    • Utilization of oil extracted from spent coffee grounds for sustainable production of polyhydroxyalkanoates
    • PID: 24652066, COI: 1:CAS:528:DC%2BC2cXkslemsbw%3D
    • Obruca S, Petrik S, Benesova P, Svoboda Z, Eremka L, Marova I (2014) Utilization of oil extracted from spent coffee grounds for sustainable production of polyhydroxyalkanoates. Appl Microbiol Biotechnol 98:5883–8590
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 5883-8590
    • Obruca, S.1    Petrik, S.2    Benesova, P.3    Svoboda, Z.4    Eremka, L.5    Marova, I.6
  • 32
    • 71449111444 scopus 로고    scopus 로고
    • Poly-β-hydroxyalkanoate exert protective effect against carbon starvation and frozen conditions in Sphingopyxis chilensis
    • PID: 19727947, COI: 1:CAS:528:DC%2BD1MXhsValurjL
    • Pavez P, Castillo JL, Gonzales C, Martinez M (2009) Poly-β-hydroxyalkanoate exert protective effect against carbon starvation and frozen conditions in Sphingopyxis chilensis. Curr Microbiol 59:636–640
    • (2009) Curr Microbiol , vol.59 , pp. 636-640
    • Pavez, P.1    Castillo, J.L.2    Gonzales, C.3    Martinez, M.4
  • 34
    • 76849099236 scopus 로고    scopus 로고
    • Synthesis and production of polyhydroxyalkanoates by halophiles: current potential and future prospects
    • PID: 20024541, COI: 1:CAS:528:DC%2BC3cXhtVaqu7c%3D
    • Quillaguaman J, Guzman H, Van-Thouc D, Hatti-Kaul R (2010) Synthesis and production of polyhydroxyalkanoates by halophiles: current potential and future prospects. Appl Microbiol Biotechnol 85:1687–1696
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1687-1696
    • Quillaguaman, J.1    Guzman, H.2    Van-Thouc, D.3    Hatti-Kaul, R.4
  • 35
    • 84900419352 scopus 로고    scopus 로고
    • A closer look on the polyhydroxybutyrate- (PHB-) negative phenotype of Ralstonia eutropha PHB-4
    • PID: 24787649
    • Raberg M, Voigt B, Hecker M, Steinbuchel A (2014) A closer look on the polyhydroxybutyrate- (PHB-) negative phenotype of Ralstonia eutropha PHB-4. PLoS One 9, e95907
    • (2014) PLoS One , vol.9
    • Raberg, M.1    Voigt, B.2    Hecker, M.3    Steinbuchel, A.4
  • 36
    • 33646498780 scopus 로고    scopus 로고
    • Organic compatible solutes of halotolerant and halophilic microorganisms
    • PID: 16176595
    • Roberts MF (2005) Organic compatible solutes of halotolerant and halophilic microorganisms. Saline Syst 1:5. doi:10.1186/1746-1448-1-5
    • (2005) Saline Syst , vol.1 , pp. 5
    • Roberts, M.F.1
  • 37
    • 0035167677 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate degradation is associated with nucleotide accumulation and enhances stress resistance and survival of Pseudomonas oleovorans in natural water microcosm
    • PID: 11133449, COI: 1:CAS:528:DC%2BD3MXjtVWnsw%3D%3D
    • Ruiz JA, Lopez NI, Fernandez RO, Mendez BS (2001) Polyhydroxyalkanoate degradation is associated with nucleotide accumulation and enhances stress resistance and survival of Pseudomonas oleovorans in natural water microcosm. Appl Environ Microbiol 67:225–230
    • (2001) Appl Environ Microbiol , vol.67 , pp. 225-230
    • Ruiz, J.A.1    Lopez, N.I.2    Fernandez, R.O.3    Mendez, B.S.4
  • 38
    • 0026631716 scopus 로고
    • Increased thermal-stability of proteins in the presence of naturally occurring osmolytes
    • PID: 1376620, COI: 1:CAS:528:DyaK38XktVaqt70%3D
    • Santoro MM, Liu YF, Khan SMA, Hou LX, Bolen DW (1992) Increased thermal-stability of proteins in the presence of naturally occurring osmolytes. Biochemistry 31:5278–5283
    • (1992) Biochemistry , vol.31 , pp. 5278-5283
    • Santoro, M.M.1    Liu, Y.F.2    Khan, S.M.A.3    Hou, L.X.4    Bolen, D.W.5
  • 39
    • 84860835149 scopus 로고    scopus 로고
    • Hydroxybutyrate prevents protein aggregation in the halotolerant bacterium Pseudomonas sp. CT13 under abiotic stress
    • COI: 1:CAS:528:DC%2BC38XmvVKhu70%3D
    • Soto G, Setten L, Lisi C, Maurelis C, Mozzicafreddo M, Cuccioloni M, Angeletti M, Ayub ND (2012) Hydroxybutyrate prevents protein aggregation in the halotolerant bacterium Pseudomonas sp. CT13 under abiotic stress. Exremophiles 16:455–462
    • (2012) Exremophiles , vol.16 , pp. 455-462
    • Soto, G.1    Setten, L.2    Lisi, C.3    Maurelis, C.4    Mozzicafreddo, M.5    Cuccioloni, M.6    Angeletti, M.7    Ayub, N.D.8
  • 40
    • 84879838220 scopus 로고    scopus 로고
    • Ectoine-mediated protection of enzyme from the effect of pH and temperature stress: a study using Bacillus halodurans xylanase as a model
    • PID: 23132342, COI: 1:CAS:528:DC%2BC3sXhtVCrt7zL
    • Van-Thuoc D, Hashim SO, Hatti-Kaul R, Mamo G (2013) Ectoine-mediated protection of enzyme from the effect of pH and temperature stress: a study using Bacillus halodurans xylanase as a model. Appl Microbiol Biotechnol 97:6271–6278
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 6271-6278
    • Van-Thuoc, D.1    Hashim, S.O.2    Hatti-Kaul, R.3    Mamo, G.4
  • 41
    • 71849088356 scopus 로고    scopus 로고
    • Ectoine improves yield of biodiesel catalyzed by immobilized lipase
    • COI: 1:CAS:528:DC%2BC3cXnsVamtrY%3D
    • Wang Y, Zhang L (2010) Ectoine improves yield of biodiesel catalyzed by immobilized lipase. J Mol Catal B: Enzym 62:90–95
    • (2010) J Mol Catal B: Enzym , vol.62 , pp. 90-95
    • Wang, Y.1    Zhang, L.2
  • 42
    • 33947341681 scopus 로고
    • The oxidation of alpha- and beta-hydroxybutyric acids with hydrogen peroxide
    • COI: 1:CAS:528:DyaB28XkvVem
    • Witzemann EJ (1926) The oxidation of alpha- and beta-hydroxybutyric acids with hydrogen peroxide. J Am Chem Soc 48:211–222
    • (1926) J Am Chem Soc , vol.48 , pp. 211-222
    • Witzemann, E.J.1
  • 43
    • 79959716368 scopus 로고    scopus 로고
    • Proteomic analysis reveals the strategies of Bacillus thuringiensis YBT-1520 for survival under long-term heat stress
    • PID: 21630448, COI: 1:CAS:528:DC%2BC3MXnvF2quro%3D
    • Wu D, He J, Gong Y, Chen D, Zhu X, Qiu N, Sun M, Li M, Yu Z (2011) Proteomic analysis reveals the strategies of Bacillus thuringiensis YBT-1520 for survival under long-term heat stress. Proteomics 11:2580–2591
    • (2011) Proteomics , vol.11 , pp. 2580-2591
    • Wu, D.1    He, J.2    Gong, Y.3    Chen, D.4    Zhu, X.5    Qiu, N.6    Sun, M.7    Li, M.8    Yu, Z.9
  • 44
    • 35448967425 scopus 로고    scopus 로고
    • Disruption of the polyhydroxyalkanoate synthase gene in Aeromonas hydrophila reduces its survival ability under stress conditions
    • PID: 17888005, COI: 1:CAS:528:DC%2BD2sXht1yqtbzM
    • Zhao YH, Li HM, Qin LF, Wang HH, Chen GQ (2007) Disruption of the polyhydroxyalkanoate synthase gene in Aeromonas hydrophila reduces its survival ability under stress conditions. FEMS Microbiol Lett 276:34–41
    • (2007) FEMS Microbiol Lett , vol.276 , pp. 34-41
    • Zhao, Y.H.1    Li, H.M.2    Qin, L.F.3    Wang, H.H.4    Chen, G.Q.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.