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Volumn 7, Issue 2, 2013, Pages 114-120

Engineering lipases for enhanced catalysis

Author keywords

Bio imprinting; Directed evolution; Error prone PCR; Rational protein design; Site directed mutagenesis

Indexed keywords

TRIACYLGLYCEROL LIPASE;

EID: 84888222127     PISSN: 22127968     EISSN: 18723136     Source Type: Journal    
DOI: 10.2174/2212796811206020123     Document Type: Review
Times cited : (5)

References (52)
  • 1
    • 71549149350 scopus 로고    scopus 로고
    • Biodiesel production through lipase catalyzed transesterification: An overview
    • Bajaj A, Lohan P, Jha PN, Mehrotra R. Biodiesel production through lipase catalyzed transesterification: An overview. J Mol Catal B: Enzym 2010; 62: 9-14.
    • (2010) J Mol Catal B: Enzym , vol.62 , pp. 9-14
    • Bajaj, A.1    Lohan, P.2    Jha, P.N.3    Mehrotra, R.4
  • 2
    • 2542506051 scopus 로고    scopus 로고
    • The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of abound inhibitor
    • Kim KK, Song HK, Shin DH, et al. The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of abound inhibitor. Structure 1997; 5(2): 173-185.
    • (1997) Structure , vol.5 , Issue.2 , pp. 173-185
    • Kim, K.K.1    Song, H.K.2    Shin, D.H.3
  • 3
    • 0026418174 scopus 로고
    • A model for interfacial activation in lipases from the structure of a fungal lipaseinhibitor complex
    • Brzozowski AM, Derewenda U, Derewenda ZS, et al. A model for interfacial activation in lipases from the structure of a fungal lipaseinhibitor complex. Nature 1991; 351: 491-494.
    • (1991) Nature , vol.351 , pp. 491-494
    • Brzozowski, A.M.1    Derewenda, U.2    Derewenda, Z.S.3
  • 6
    • 63549102137 scopus 로고    scopus 로고
    • A Review of the Current State of Biodiesel Production Using Enzymatic Transesterification
    • Fjerbaek L, Christensen KV, Norddahl B. A Review of the Current State of Biodiesel Production Using Enzymatic Transesterification. Biotechnol Bioeng 2009; 102(5): 1298-1315.
    • (2009) Biotechnol Bioeng , vol.102 , Issue.5 , pp. 1298-1315
    • Fjerbaek, L.1    Christensen, K.V.2    Norddahl, B.3
  • 7
    • 55549113867 scopus 로고    scopus 로고
    • Whole-cell biocatalysts for biodieselfuel production
    • Fukuda H, Hama S, Tamalampudi S, Noda H. Whole-cell biocatalysts for biodieselfuel production. Trends Biotechnol 2008; 26(12): 668-673.
    • (2008) Trends Biotechnol , vol.26 , Issue.12 , pp. 668-673
    • Fukuda, H.1    Hama, S.2    Tamalampudi, S.3    Noda, H.4
  • 8
    • 84858339901 scopus 로고    scopus 로고
    • Improved performance of a packed-bed reactor for biodiesel production through whole-cell biocatalysis employing a high-lipase-expression system
    • Yoshida A, Hama S, Tamadani N, et al. Improved performance of a packed-bed reactor for biodiesel production through whole-cell biocatalysis employing a high-lipase-expression system. Biochem Eng J 2012; 63: 76-80.
    • (2012) Biochem Eng J , vol.63 , pp. 76-80
    • Yoshida, A.1    Hama, S.2    Tamadani, N.3
  • 9
    • 33947601150 scopus 로고    scopus 로고
    • Biodiesel-fuel production in a packed-bed reactor using lipase-producing Rhizopus oryzae cells immobilized within biomass support particles
    • Hama S, Yamaji H, Fukumizu T, et al. Biodiesel-fuel production in a packed-bed reactor using lipase-producing Rhizopus oryzae cells immobilized within biomass support particles. Biochem Eng J 2007; 34: 273-278.
    • (2007) Biochem Eng J , vol.34 , pp. 273-278
    • Hama, S.1    Yamaji, H.2    Fukumizu, T.3
  • 10
    • 0034597427 scopus 로고    scopus 로고
    • Lipase engineering database: Understanding and exploiting sequence-structure-function relationships
    • Pleiss J, Fischer M, Peiker M, et al. Lipase engineering database: Understanding and exploiting sequence-structure-function relationships. J Mol Catal B: Enzym 2000; 109(5): 491-508.
    • (2000) J Mol Catal B: Enzym , vol.109 , Issue.5 , pp. 491-508
    • Pleiss, J.1    Fischer, M.2    Peiker, M.3
  • 11
    • 84862807289 scopus 로고    scopus 로고
    • Biocatalyst development by directed evolution
    • PMID: 22310212
    • Wang M, Si T, Zhao H. Biocatalyst development by directed evolution. Bioresource Technol 2012; PMID: 22310212.
    • (2012) Bioresource Technol
    • Wang, M.1    Si, T.2    Zhao, H.3
  • 12
    • 0028939393 scopus 로고
    • Interfacial activation-based molecular bioimprinting of lipolytic enzymes (lipases/phospholipase A2/nonaqueous media)
    • Mingarro I, Abad C, Braco L. Interfacial activation-based molecular bioimprinting of lipolytic enzymes (lipases/phospholipase A2/nonaqueous media). P Natl Acad Sci-Biol 1995; 92: 3308-3312.
    • (1995) P Natl Acad Sci-Biol , vol.92 , pp. 3308-3312
    • Mingarro, I.1    Abad, C.2    Braco, L.3
  • 13
    • 0343487855 scopus 로고    scopus 로고
    • Improving lipase activity in solventfree media by interfacial activation-based molecular bioimprinting
    • Gonzalez-Navarro H, Braco L. Improving lipase activity in solventfree media by interfacial activation-based molecular bioimprinting. J Mol Catal B: Enzym 1997; 3: 111-119.
    • (1997) J Mol Catal B: Enzym , vol.3 , pp. 111-119
    • Gonzalez-Navarro, H.1    Braco, L.2
  • 14
    • 11144277399 scopus 로고    scopus 로고
    • Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
    • Foresti ML, Alimenti GA, Ferreira ML. Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: effect on the enzymatic activity in solvent-free ethyl oleate synthesis. Enzyme Microb Tech 2005; 36: 338-349.
    • (2005) Enzyme Microb Tech , vol.36 , pp. 338-349
    • Foresti, M.L.1    Alimenti, G.A.2    Ferreira, M.L.3
  • 15
    • 0037010728 scopus 로고    scopus 로고
    • Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
    • Palomo JM, Muñoz G, Fernández-Lorente G, et al. Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases. J Mol Catal B: Enzym 2002; 19-20: 279-286.
    • (2002) J Mol Catal B: Enzym , vol.19-20 , pp. 279-286
    • Palomo, J.M.1    Muñoz, G.2    Fernández-Lorente, G.3
  • 16
    • 69249203556 scopus 로고    scopus 로고
    • Combined strategy for preparation of a bioimprinted Geotrichum sp. lipase biocatalyst effective in non-aqueous media
    • Yan JY, Yan YJ, Yang JK, et al. Combined strategy for preparation of a bioimprinted Geotrichum sp. lipase biocatalyst effective in non-aqueous media. Process Biochem 2009; 44: 1128-1132.
    • (2009) Process Biochem , vol.44 , pp. 1128-1132
    • Yan, J.Y.1    Yan, Y.J.2    Yang, J.K.3
  • 17
    • 74149085150 scopus 로고    scopus 로고
    • Combination of bioimprinting and silane precursor alkyls improved the activity of sol-gel-encapsulated lipase
    • Yang J, Liu L, Cao X. Combination of bioimprinting and silane precursor alkyls improved the activity of sol-gel-encapsulated lipase. Enzyme Microb Tech 2010; 46: 257-261.
    • (2010) Enzyme Microb Tech , vol.46 , pp. 257-261
    • Yang, J.1    Liu, L.2    Cao, X.3
  • 18
    • 0038069176 scopus 로고    scopus 로고
    • Orlistat-induced molecular bio-imprinting of microbial lipase
    • Yilmaz E. Orlistat-induced molecular bio-imprinting of microbial lipase. World J Microb Biot 2003; 19: 161-165.
    • (2003) World J Microb Biot , vol.19 , pp. 161-165
    • Yilmaz, E.1
  • 19
    • 0036125656 scopus 로고    scopus 로고
    • Bio-imprinting of microbial lipase at air-water interface
    • Yilmaz E. Bio-imprinting of microbial lipase at air-water interface. World J Microb Biot 2002; 18: 141-145.
    • (2002) World J Microb Biot , vol.18 , pp. 141-145
    • Yilmaz, E.1
  • 21
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner O, Arnold FH. Directed evolution of enzyme catalysts. Trends Biotechol 1997; 15: 523-530.
    • (1997) Trends Biotechol , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 22
    • 33845288649 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability
    • Reetz MT, Carballeira JD, Vogel A. Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability. Angew Chem Int Ed 2006; 45: 7745-7751.
    • (2006) Angew Chem Int Ed , vol.45 , pp. 7745-7751
    • Reetz, M.T.1    Carballeira, J.D.2    Vogel, A.3
  • 23
    • 77954274719 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: Rigorous comparison with traditional methods
    • Reetz MT, Prasad S, Carballeira JD, et al. Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: rigorous comparison with traditional methods. J Am Chem Soc 2010; 132: 9144-9152.
    • (2010) J Am Chem Soc , vol.132 , pp. 9144-9152
    • Reetz, M.T.1    Prasad, S.2    Carballeira, J.D.3
  • 24
    • 79957559287 scopus 로고    scopus 로고
    • Revisiting the lipase from Pseudomonas aeruginosa: Directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis
    • Prasad S, Bocola M, Reetz MT. Revisiting the lipase from Pseudomonas aeruginosa: directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis. Chem Phys Chem 2011; 12: 1550-1557.
    • (2011) Chem Phys Chem , vol.12 , pp. 1550-1557
    • Prasad, S.1    Bocola, M.2    Reetz, M.T.3
  • 25
    • 84875113842 scopus 로고    scopus 로고
    • Approach of directed evolution of microbial lipases and biodiesel catalysis
    • Li J, Chen S, Li L, et al. Approach of directed evolution of microbial lipases and biodiesel catalysis. Afr J Microb Res 2012; 6(3): 637-642.
    • (2012) Afr J Microb Res , vol.6 , Issue.3 , pp. 637-642
    • Li, J.1    Chen, S.2    Li, L.3
  • 26
    • 80054032745 scopus 로고    scopus 로고
    • Isolation of a thermostable variant of Lip2 lipase from Yarrowia lipolytica by directed evolution and deeper insight into the denaturation mechanisms involved
    • Bordes F, Tarquis L, Nicaud J-M, Marty A. Isolation of a thermostable variant of Lip2 lipase from Yarrowia lipolytica by directed evolution and deeper insight into the denaturation mechanisms involved. J Biotechnol 2011; 156: 117-124.
    • (2011) J Biotechnol , vol.156 , pp. 117-124
    • Bordes, F.1    Tarquis, L.2    Nicaud, J.-M.3    Marty, A.4
  • 27
    • 66349117989 scopus 로고    scopus 로고
    • Thermally denatured state determines refolding in lipase: Mutational analysis
    • Ahmad S, Rao NM. Thermally denatured state determines refolding in lipase: Mutational analysis. Protein Sci 2009; 18: 1183-1196.
    • (2009) Protein Sci , vol.18 , pp. 1183-1196
    • Ahmad, S.1    Rao, N.M.2
  • 28
    • 0141817121 scopus 로고    scopus 로고
    • Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution
    • Zhang N, Suen WC, Windsor W, et al. Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Protein Eng 2003; 16(8): 599-605.
    • (2003) Protein Eng , vol.16 , Issue.8 , pp. 599-605
    • Zhang, N.1    Suen, W.C.2    Windsor, W.3
  • 29
    • 4143110558 scopus 로고    scopus 로고
    • Structural Basis of Selection and Thermostability of Laboratory Evolved Bacillus subtilisLipase
    • Acharya P, Rajakumara E, Sankaranarayanan R, Rao NM. Structural Basis of Selection and Thermostability of Laboratory Evolved Bacillus subtilisLipase. J Mol Biol 2004; 341: 1271-1281.
    • (2004) J Mol Biol , vol.341 , pp. 1271-1281
    • Acharya, P.1    Rajakumara, E.2    Sankaranarayanan, R.3    Rao, N.M.4
  • 30
    • 1842765645 scopus 로고    scopus 로고
    • Improved activity and thermostability of Candida antarcticalipase B by DNA family shuffing
    • Suen W-C, Zhang N, Xiao L, et al. Improved activity and thermostability of Candida antarcticalipase B by DNA family shuffing. Protein Eng Des Sel 2004; 17(2): 133-140.
    • (2004) Protein Eng Des Sel , vol.17 , Issue.2 , pp. 133-140
    • Suen, W.-C.1    Zhang, N.2    Xiao, L.3
  • 31
    • 0006688434 scopus 로고    scopus 로고
    • 1by Evolutionary Molecular Engineering
    • 1by Evolutionary Molecular Engineering. Appl Environ Microb 2000; 66(3): 890-894.
    • (2000) Appl Environ Microb , vol.66 , Issue.3 , pp. 890-894
    • Song, J.K.1    Rhee, J.S.2
  • 32
    • 44749086283 scopus 로고    scopus 로고
    • Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase
    • Lafranconi PG, Caldarazzo SM, Villa A, et al. Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase. FEBS Lett 2008; 582: 2313-2318.
    • (2008) FEBS Lett , vol.582 , pp. 2313-2318
    • Lafranconi, P.G.1    Caldarazzo, S.M.2    Villa, A.3
  • 33
    • 57549091573 scopus 로고    scopus 로고
    • Improvement of alkaline lipase from Proteus vulgaris T6 by directed evolution
    • Fang Y, Lu Y, Lv F, et al. Improvement of alkaline lipase from Proteus vulgaris T6 by directed evolution. Enzyme Microb Tech 2009; 44: 84-88.
    • (2009) Enzyme Microb Tech , vol.44 , pp. 84-88
    • Fang, Y.1    Lu, Y.2    Lv, F.3
  • 34
    • 31544477181 scopus 로고    scopus 로고
    • Design and Evolution of New Catalytic Activity with an Existing Protein Scaffold
    • Park HS, Nam SH, Lee JK, et al. Design and Evolution of New Catalytic Activity with an Existing Protein Scaffold. Science 2006; 311: 535-538.
    • (2006) Science , vol.311 , pp. 535-538
    • Park, H.S.1    Nam, S.H.2    Lee, J.K.3
  • 35
    • 69849112765 scopus 로고    scopus 로고
    • Directed Evolution of Lipase of Bacillus pumilus YZ02 by Error-prone PCR
    • Huang Y, Cai Y, Yang JK, Yan YJ. Directed Evolution of Lipase of Bacillus pumilus YZ02 by Error-prone PCR. Chin J Biotech 2008; 24(3): 445-451.
    • (2008) Chin J Biotech , vol.24 , Issue.3 , pp. 445-451
    • Huang, Y.1    Cai, Y.2    Yang, J.K.3    Yan, Y.J.4
  • 36
    • 80051473563 scopus 로고    scopus 로고
    • Engineering of Bacillus lipase by directed evolution for enhanced thermal stability: Effect of isoleucine to threonine mutation at protein surface
    • Khurana J, Singh R, Kaur J. Engineering of Bacillus lipase by directed evolution for enhanced thermal stability: effect of isoleucine to threonine mutation at protein surface. Mol Biol Rep 2011; 38: 2919-2926.
    • (2011) Mol Biol Rep , vol.38 , pp. 2919-2926
    • Khurana, J.1    Singh, R.2    Kaur, J.3
  • 37
    • 0035844691 scopus 로고    scopus 로고
    • 1in organic solvents by directed evolution
    • 1in organic solvents by directed evolution. Biochim Biophys Acta 2001; 1547: 370-378.
    • (2001) Biochim Biophys Acta , vol.1547 , pp. 370-378
    • Song, J.K.1    Rhee, J.S.2
  • 38
    • 2442508067 scopus 로고    scopus 로고
    • Molecular engineering of Rhizopus oryzae lipase using a combinatorial protein library constructed on the yeast cell surface
    • Shibamoto H, Matsumoto T, Fukuda H, Kondo A. Molecular engineering of Rhizopus oryzae lipase using a combinatorial protein library constructed on the yeast cell surface. J Mol Catal B: Enzym 2004; 28: 235-239.
    • (2004) J Mol Catal B: Enzym , vol.28 , pp. 235-239
    • Shibamoto, H.1    Matsumoto, T.2    Fukuda, H.3    Kondo, A.4
  • 39
    • 27544481402 scopus 로고    scopus 로고
    • Creation of Rhizopus oryzae lipase having a unique oxyanion hole by combinatorial mutagenesis in the lid domain
    • Shiraga S, Ishiguro M, Fukami H, et al. Creation of Rhizopus oryzae lipase having a unique oxyanion hole by combinatorial mutagenesis in the lid domain Appl Microbiol Biotechnol 2005; 68: 779-785
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 779-785
    • Shiraga, S.1    Ishiguro, M.2    Fukami, H.3
  • 40
    • 0242490876 scopus 로고    scopus 로고
    • Bacterial cell surface display of lipase and its randomly mutated library facilitates high-throughput screening of mutants showing higher specific activities
    • Jung HC, Ko S, Ju SJ, et al. Bacterial cell surface display of lipase and its randomly mutated library facilitates high-throughput screening of mutants showing higher specific activities. J Mol Catal B: Enzym 2003; 26(3): 177-184.
    • (2003) J Mol Catal B: Enzym , vol.26 , Issue.3 , pp. 177-184
    • Jung, H.C.1    Ko, S.2    Ju, S.J.3
  • 41
    • 17644394187 scopus 로고    scopus 로고
    • Directed evolution of Pseudomonas aeruginosa lipase for improved amide-hydrolyzing activity
    • Fujii R, Nakagawa Y, Hiratake J, et al. Directed evolution of Pseudomonas aeruginosa lipase for improved amide-hydrolyzing activity. Protein Eng Des Sel 2005; 18: 93-101.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 93-101
    • Fujii, R.1    Nakagawa, Y.2    Hiratake, J.3
  • 42
    • 0032432424 scopus 로고    scopus 로고
    • Improvement in the Organic Solvent Stability of Pseudomonas Lipase by Random Mutation
    • Nakano H, Ide Y, Tsuda T, et al. Improvement in the Organic Solvent Stability of Pseudomonas Lipase by Random Mutation. Ann N Y Acad Sci 1998; 864: 431-434.
    • (1998) Ann N Y Acad Sci , vol.864 , pp. 431-434
    • Nakano, H.1    Ide, Y.2    Tsuda, T.3
  • 43
  • 44
    • 34447105646 scopus 로고    scopus 로고
    • Lipase-catalyzed biodiesel production from soybean oil in ionic liquids
    • Ha SH, Lan MN, Lee SH, et al. Lipase-catalyzed biodiesel production from soybean oil in ionic liquids. Enzyme Microb Tech 2007; 41: 480-483.
    • (2007) Enzyme Microb Tech , vol.41 , pp. 480-483
    • Ha, S.H.1    Lan, M.N.2    Lee, S.H.3
  • 45
    • 5644247368 scopus 로고    scopus 로고
    • Protein engineering and applications of Candida rugosa lipase isoforms
    • Akoh CC, Lee GC, Shaw JF. Protein engineering and applications of Candida rugosa lipase isoforms. Lipids 2004; 39: 513-526.
    • (2004) Lipids , vol.39 , pp. 513-526
    • Akoh, C.C.1    Lee, G.C.2    Shaw, J.F.3
  • 47
    • 60349109395 scopus 로고    scopus 로고
    • Understanding the plasticity of the alpha/beta hydrolase fold: Lid swapping on the Candidaantarctica lipase B results in chimeras with interesting biocatalytic properties
    • Skjøt M, Maria LD, Chatterjee R, et al. Understanding the plasticity of the alpha/beta hydrolase fold: Lid swapping on the Candidaantarctica lipase B results in chimeras with interesting biocatalytic properties. ChemBioChem 2009; 10: 520-527.
    • (2009) ChemBioChem , vol.10 , pp. 520-527
    • Skjøt, M.1    Maria, L.D.2    Chatterjee, R.3
  • 48
    • 49449092589 scopus 로고    scopus 로고
    • Loop grafting of Bacillus subtilislipase A: Inversion of enantioselectivity
    • Boersma YL, Pijning T, Bosma MS, et al. Loop grafting of Bacillus subtilislipase A: Inversion of enantioselectivity. Chem Biol 2008; 15: 782-789.
    • (2008) Chem Biol , vol.15 , pp. 782-789
    • Boersma, Y.L.1    Pijning, T.2    Bosma, M.S.3
  • 49
    • 17644419962 scopus 로고    scopus 로고
    • Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase
    • Santarossa G, Lafranconi PG, Alquati C, DeGioia L, et al. Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase. FEBS Lett 2005; 579: 2383-2386.
    • (2005) FEBS Lett , vol.579 , pp. 2383-2386
    • Santarossa, G.1    Lafranconi, P.G.2    Alquati, C.3    DeGioia, L.4
  • 50
    • 0029821990 scopus 로고    scopus 로고
    • The consequences of engineering an extra disulfide bond in the Penicillium camembertii mono-and diglyceride specific lipase
    • Yamaguchi S, Takeuchi K, Mase T, Oikawa K, et al. The consequences of engineering an extra disulfide bond in the Penicillium camembertii mono-and diglyceride specific lipase. Protein Eng 1996; 9(9): 789-795.
    • (1996) Protein Eng , vol.9 , Issue.9 , pp. 789-795
    • Yamaguchi, S.1    Takeuchi, K.2    Mase, T.3    Oikawa, K.4
  • 51
    • 20544446894 scopus 로고    scopus 로고
    • Rational Strategies for Directed Evolution of Biocatalysts. Application to Candida antarcticalipase B (CALB)
    • Chodorge M, Fourage L, Ullmann C, et al. Rational Strategies for Directed Evolution of Biocatalysts. Application to Candida antarcticalipase B (CALB). Adv Synth Catal 2005; 347: 1022-1026.
    • (2005) Adv Synth Catal , vol.347 , pp. 1022-1026
    • Chodorge, M.1    Fourage, L.2    Ullmann, C.3
  • 52
    • 66149174591 scopus 로고    scopus 로고
    • Increasing activity of lipase from Bacillus subtilis by directed evolution
    • Zhao B, Tao J, Ma JS, et al. Increasing activity of lipase from Bacillus subtilis by directed evolution. Chin J Catal 2009; 30(4): 291-296.
    • (2009) Chin J Catal , vol.30 , Issue.4 , pp. 291-296
    • Zhao, B.1    Tao, J.2    Ma, J.S.3


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