메뉴 건너뛰기




Volumn 28, Issue 6, 2011, Pages 627-638

Lipase from marine Aspergillus awamori BTMFW032: Production, partial purification and application in oil effluent treatment

Author keywords

[No Author keywords available]

Indexed keywords

ASPERGILLUS AWAMORI; ENZYME PRODUCTION; EXTRACELLULAR LIPASE; INCUBATION TEMPERATURES; ION EXCHANGE CHROMATOGRAPHY; LIPASE PRODUCTION; MARINE FUNGUS; OIL CONTENTS; OIL EFFLUENT TREATMENT; OPTIMAL ACTIVITY; OPTIMAL CONDITIONS; OPTIMIZED CONDITIONS; PARTIAL PURIFICATION; POTENTIAL APPLICATIONS; RESPONSE SURFACE METHOD; RICE BRANS; SOYABEANS; SPECIFIC ACTIVITY; STATISTICAL MODELING; SUBMERGED FERMENTATION; TIME-COURSE EXPERIMENTS;

EID: 80052964918     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2011.04.007     Document Type: Article
Times cited : (83)

References (61)
  • 1
    • 33747518326 scopus 로고    scopus 로고
    • Industrial applications of microbial lipases
    • Hasan F., et al. Industrial applications of microbial lipases. Enzyme Microb. Technol. 2006, 39:235-251.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 235-251
    • Hasan, F.1
  • 2
    • 77952888862 scopus 로고    scopus 로고
    • A review on microbial lipases production
    • Treichel H., et al. A review on microbial lipases production. Food Bioprocess Technol. 2010, 3:182-196.
    • (2010) Food Bioprocess Technol. , vol.3 , pp. 182-196
    • Treichel, H.1
  • 3
    • 78049259303 scopus 로고    scopus 로고
    • Characterization of the lipase from Carica papaya residues
    • Paques F.W., et al. Characterization of the lipase from Carica papaya residues. Braz. J. Food Technol. 2008, 11:20-27.
    • (2008) Braz. J. Food Technol. , vol.11 , pp. 20-27
    • Paques, F.W.1
  • 4
    • 33644893060 scopus 로고    scopus 로고
    • Plant lipases from latex: properties and industrial applications
    • Paques F.W., Macedo G.A. Plant lipases from latex: properties and industrial applications. Quím. Nova 2006, 29:93-99.
    • (2006) Quím. Nova , vol.29 , pp. 93-99
    • Paques, F.W.1    Macedo, G.A.2
  • 5
    • 67749139446 scopus 로고    scopus 로고
    • The stabilizing effects of polyols and sugars on porcine pancreatic lipase
    • Gangadhara, et al. The stabilizing effects of polyols and sugars on porcine pancreatic lipase. J. Am. Oil Chem. Soc. 2009, 86:773-781.
    • (2009) J. Am. Oil Chem. Soc. , vol.86 , pp. 773-781
    • Gangadhara1
  • 6
    • 70449346397 scopus 로고    scopus 로고
    • Breed difference and regulation of the porcine adipose triglyceride lipase and hormone sensitive lipase by TNFa
    • Shan T., et al. Breed difference and regulation of the porcine adipose triglyceride lipase and hormone sensitive lipase by TNFa. Anim. Genet. 2009, 40:863-870.
    • (2009) Anim. Genet. , vol.40 , pp. 863-870
    • Shan, T.1
  • 7
    • 78049287602 scopus 로고    scopus 로고
    • Aspergillus sp. lipase: potential biocatalyst for industrial use
    • Contesini F.J., et al. Aspergillus sp. lipase: potential biocatalyst for industrial use. J. Mol. Catal. B: Enzym. 2010, 67:163-171.
    • (2010) J. Mol. Catal. B: Enzym. , vol.67 , pp. 163-171
    • Contesini, F.J.1
  • 8
    • 23744435735 scopus 로고    scopus 로고
    • Potential of enantioselective biocatalysis by microbial lipases
    • Carvalho P.O., et al. Potential of enantioselective biocatalysis by microbial lipases. Quím. Nova 2005, 28:614-621.
    • (2005) Quím. Nova , vol.28 , pp. 614-621
    • Carvalho, P.O.1
  • 9
    • 0000812432 scopus 로고    scopus 로고
    • Lipase production by Penicillium restrictum in a bench-scale fermenter
    • Freire D.M., et al. Lipase production by Penicillium restrictum in a bench-scale fermenter. Appl. Biochem. Biotechnol. 1997, 63:409-421.
    • (1997) Appl. Biochem. Biotechnol. , vol.63 , pp. 409-421
    • Freire, D.M.1
  • 10
    • 0037207024 scopus 로고    scopus 로고
    • Production of acidic lipase by Aspergillus niger in solid state fermentation
    • Mahadik N.D., et al. Production of acidic lipase by Aspergillus niger in solid state fermentation. Process Biochem. 2002, 38:715-721.
    • (2002) Process Biochem. , vol.38 , pp. 715-721
    • Mahadik, N.D.1
  • 11
    • 67649171603 scopus 로고    scopus 로고
    • Gene analysis, optimized production and property of marine lipase from Bacillus pumilus B106 associated with South China Sea sponge Halichondria rugosa
    • Zhang H., et al. Gene analysis, optimized production and property of marine lipase from Bacillus pumilus B106 associated with South China Sea sponge Halichondria rugosa. World J. Microbiol. Biotechnol. 2009, 25:1267-1274.
    • (2009) World J. Microbiol. Biotechnol. , vol.25 , pp. 1267-1274
    • Zhang, H.1
  • 12
    • 33947215960 scopus 로고    scopus 로고
    • Alkaline lipase from a novel strain Burkholderia multivorans: statistical medium optimization and production in a bioreactor
    • Gupta N., et al. Alkaline lipase from a novel strain Burkholderia multivorans: statistical medium optimization and production in a bioreactor. Process Biochem. 2007, 42:518-526.
    • (2007) Process Biochem. , vol.42 , pp. 518-526
    • Gupta, N.1
  • 13
    • 0036843484 scopus 로고    scopus 로고
    • Response surface analysis of lipase production by freely suspended Rhizopus arrhizus
    • Elibol M., Ozer D. Response surface analysis of lipase production by freely suspended Rhizopus arrhizus. Process Biochem. 2002, 38:367-372.
    • (2002) Process Biochem. , vol.38 , pp. 367-372
    • Elibol, M.1    Ozer, D.2
  • 14
    • 33747079067 scopus 로고    scopus 로고
    • Statistical optimization of medium components and growth conditions by response surface methodology to enhance lipase production by Aspergillus carneus
    • Kaushik R., et al. Statistical optimization of medium components and growth conditions by response surface methodology to enhance lipase production by Aspergillus carneus. J. Mol. Catal. B: Enzym. 2006, 40:121-126.
    • (2006) J. Mol. Catal. B: Enzym. , vol.40 , pp. 121-126
    • Kaushik, R.1
  • 15
    • 80052971208 scopus 로고    scopus 로고
    • Production process and composition of an enzymatic preparation, and its use for the treatment of domestic and industrial effluents of high fat
    • protein and/or carbohydrate content. Brazil patent US2004/0055953A1.
    • Cammarota, M.C. et al. (2004) Production process and composition of an enzymatic preparation, and its use for the treatment of domestic and industrial effluents of high fat, protein and/or carbohydrate content. Brazil patent US2004/0055953A1.
    • (2004)
    • Cammarota, M.C.1
  • 16
    • 0030941565 scopus 로고    scopus 로고
    • An investigation into microbial removal of fats, oils and greases
    • Wakelin N.G., Forster C.F. An investigation into microbial removal of fats, oils and greases. Bioresour. Technol. 1997, 59:37-43.
    • (1997) Bioresour. Technol. , vol.59 , pp. 37-43
    • Wakelin, N.G.1    Forster, C.F.2
  • 17
    • 0034810672 scopus 로고    scopus 로고
    • Characterization and distribution of esterase activity in activated sludge
    • Boczar B.A., et al. Characterization and distribution of esterase activity in activated sludge. Water Res. 2001, 35:4208-4216.
    • (2001) Water Res. , vol.35 , pp. 4208-4216
    • Boczar, B.A.1
  • 18
    • 33745841316 scopus 로고    scopus 로고
    • A review on hydrolytic enzymes in the treatment of wastewater with high oil and grease content
    • Cammarota M., Freire D. A review on hydrolytic enzymes in the treatment of wastewater with high oil and grease content. Bioresour. Technol. 2006, 97:2195-2210.
    • (2006) Bioresour. Technol. , vol.97 , pp. 2195-2210
    • Cammarota, M.1    Freire, D.2
  • 19
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • Kouker G., Jaeger K.E. Specific and sensitive plate assay for bacterial lipases. Appl. Environ. Microb. 1987, 53:211-213.
    • (1987) Appl. Environ. Microb. , vol.53 , pp. 211-213
    • Kouker, G.1    Jaeger, K.E.2
  • 20
    • 0022534889 scopus 로고
    • Modified method for fungal slide culture
    • Harris J.L. Modified method for fungal slide culture. J. Clin. Microbiol. 1986, 24:460-461.
    • (1986) J. Clin. Microbiol. , vol.24 , pp. 460-461
    • Harris, J.L.1
  • 22
    • 0025183708 scopus 로고
    • Basic local alignment search tool
    • Altschul S.F., et al. Basic local alignment search tool. J. Mol. Biol. 1980, 215:403-410.
    • (1980) J. Mol. Biol. , vol.215 , pp. 403-410
    • Altschul, S.F.1
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., et al. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1
  • 24
    • 0038353703 scopus 로고    scopus 로고
    • Use of methylumbeliferyl-derivative substrates for lipase activity characterization
    • Prim N., et al. Use of methylumbeliferyl-derivative substrates for lipase activity characterization. J. Mol. Catal. B: Enzym. 2003, 22:339-346.
    • (2003) J. Mol. Catal. B: Enzym. , vol.22 , pp. 339-346
    • Prim, N.1
  • 25
    • 0000795704 scopus 로고
    • Crystalline soybean trysin inhibitor II. General properties
    • Kunitz M. Crystalline soybean trysin inhibitor II. General properties. J. Gen. Physiol. 1947, 30:291-310.
    • (1947) J. Gen. Physiol. , vol.30 , pp. 291-310
    • Kunitz, M.1
  • 26
    • 71849104860 scopus 로고
    • Protein measurement with Folin phenol reagent
    • Lowry O.H., et al. Protein measurement with Folin phenol reagent. J. Biol. Chem. 1951, 193:265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1
  • 27
    • 0001131698 scopus 로고
    • The design of optimum multifactorial experiments
    • Plackett R.L., Burman J.P. The design of optimum multifactorial experiments. Biometrika 1946, 33:305-325.
    • (1946) Biometrika , vol.33 , pp. 305-325
    • Plackett, R.L.1    Burman, J.P.2
  • 28
    • 84946657020 scopus 로고
    • Some new three level designs for the study of quantitative variables
    • Box G.E.F., Behnken D.W. Some new three level designs for the study of quantitative variables. Technometrics 1960, 24:455-475.
    • (1960) Technometrics , vol.24 , pp. 455-475
    • Box, G.E.F.1    Behnken, D.W.2
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmlli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmlli, U.K.1
  • 30
    • 0032869128 scopus 로고    scopus 로고
    • Direct fluorescence based lipase activity assay
    • Diaz P., et al. Direct fluorescence based lipase activity assay. BioTechniques 1999, 27:696-700.
    • (1999) BioTechniques , vol.27 , pp. 696-700
    • Diaz, P.1
  • 33
    • 48749116260 scopus 로고    scopus 로고
    • Purification and characteristics of feruloyl esterase from Aspergillus awamori G-2 strain
    • Kanauchi M., et al. Purification and characteristics of feruloyl esterase from Aspergillus awamori G-2 strain. J. Food Sci. 2008, 73:C458-C463.
    • (2008) J. Food Sci. , vol.73
    • Kanauchi, M.1
  • 34
    • 0015509413 scopus 로고
    • Studies on soil fungi from teak forests of Gorakhpur II - a contribution to Indian Aspergilli
    • Kamal, Bhargava K.S. Studies on soil fungi from teak forests of Gorakhpur II - a contribution to Indian Aspergilli. Mycopathol. Mycol. Appl. 1972, 47:59-72.
    • (1972) Mycopathol. Mycol. Appl. , vol.47 , pp. 59-72
    • Kamal1    Bhargava, K.S.2
  • 35
    • 0030907763 scopus 로고    scopus 로고
    • Identification of clinically important Ascomycetous yeasts based on nucleotide divergence in the 5' end of the large-subunit (26S) ribosomal DNA gene
    • Kurtzman C.P., Robnett C.J. Identification of clinically important Ascomycetous yeasts based on nucleotide divergence in the 5' end of the large-subunit (26S) ribosomal DNA gene. J. Clin. Microbiol. 1997, 35:1216-1223.
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 1216-1223
    • Kurtzman, C.P.1    Robnett, C.J.2
  • 36
    • 0029682616 scopus 로고    scopus 로고
    • Microbial lipases: production and application
    • Ghosh P.K., et al. Microbial lipases: production and application. Sci. Prog. 1996, 79:119-157.
    • (1996) Sci. Prog. , vol.79 , pp. 119-157
    • Ghosh, P.K.1
  • 37
    • 0031773198 scopus 로고    scopus 로고
    • Production of extracellular lipases by Saccharomyces cerevisae
    • Shirazi S.H., et al. Production of extracellular lipases by Saccharomyces cerevisae. World J. Microbiol. Biotechnol. 1998, 14:595-597.
    • (1998) World J. Microbiol. Biotechnol. , vol.14 , pp. 595-597
    • Shirazi, S.H.1
  • 38
    • 0242289262 scopus 로고    scopus 로고
    • Optimization of extracellular lipase production by Geotrichum sp. using factorial design
    • Burkert J.F.M., et al. Optimization of extracellular lipase production by Geotrichum sp. using factorial design. Bioresour. Technol. 2004, 91:77-84.
    • (2004) Bioresour. Technol. , vol.91 , pp. 77-84
    • Burkert, J.F.M.1
  • 39
    • 0347544012 scopus 로고    scopus 로고
    • Statistical media optimization and alkaline protease production from Bacillus mojavensis in a bioreactor
    • Beg Q.K., et al. Statistical media optimization and alkaline protease production from Bacillus mojavensis in a bioreactor. Process Biochem. 2003, 39:203-209.
    • (2003) Process Biochem. , vol.39 , pp. 203-209
    • Beg, Q.K.1
  • 41
    • 0036446073 scopus 로고    scopus 로고
    • Statistical medium optimization and production of a hyperthermostable lipase from Burkholderia cepacia
    • Rathi P., et al. Statistical medium optimization and production of a hyperthermostable lipase from Burkholderia cepacia. J. Appl. Microbiol. 2002, 93:930-936.
    • (2002) J. Appl. Microbiol. , vol.93 , pp. 930-936
    • Rathi, P.1
  • 42
    • 0034800699 scopus 로고    scopus 로고
    • Optimal design for the maximization of Penicillium cyclopium lipase production
    • Vanot G., et al. Optimal design for the maximization of Penicillium cyclopium lipase production. Appl. Microbiol. Biotechnol. 2001, 57:342-345.
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 342-345
    • Vanot, G.1
  • 43
    • 77949264234 scopus 로고    scopus 로고
    • Optimization of critical medium components using response surface methodology for lipase production by Rhizopus delemar
    • Açikel Ü., et al. Optimization of critical medium components using response surface methodology for lipase production by Rhizopus delemar. Food Bioproducts Process. 2010, 88:31-39.
    • (2010) Food Bioproducts Process. , vol.88 , pp. 31-39
    • Açikel, Ü.1
  • 44
    • 0037129173 scopus 로고    scopus 로고
    • Microwave assisted rapid characterization of lipase selectivities
    • Bradoo S., et al. Microwave assisted rapid characterization of lipase selectivities. J. Biochem. Biophys. Meth. 2002, 51:115-120.
    • (2002) J. Biochem. Biophys. Meth. , vol.51 , pp. 115-120
    • Bradoo, S.1
  • 45
    • 0023875609 scopus 로고
    • Control of lipase production by Rhizopus oligosporus under various growth conditions
    • Nahas E. Control of lipase production by Rhizopus oligosporus under various growth conditions. J. Gen. Microbiol. 1988, 134:227-233.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 227-233
    • Nahas, E.1
  • 46
    • 3543022150 scopus 로고    scopus 로고
    • Investigation of lipase production by a new isolate of Aspergillus sp.
    • Cihangir N., Sarakaya E. Investigation of lipase production by a new isolate of Aspergillus sp. World J. Microbiol. Biotechnol. 2004, 20:193-197.
    • (2004) World J. Microbiol. Biotechnol. , vol.20 , pp. 193-197
    • Cihangir, N.1    Sarakaya, E.2
  • 47
    • 80052966904 scopus 로고
    • Effect of various carbon and nitrogen sources on microbial lipase biosynthesis
    • Petrovic S.E., et al. Effect of various carbon and nitrogen sources on microbial lipase biosynthesis. Biotechnol. Lett. 1990, 12:61-66.
    • (1990) Biotechnol. Lett. , vol.12 , pp. 61-66
    • Petrovic, S.E.1
  • 48
    • 1642568647 scopus 로고    scopus 로고
    • Production of lipase by immobilized cells of Aspergillus niger
    • Ellaiah P., et al. Production of lipase by immobilized cells of Aspergillus niger. Process Biochem. 2004, 39:525-528.
    • (2004) Process Biochem. , vol.39 , pp. 525-528
    • Ellaiah, P.1
  • 49
    • 0032827502 scopus 로고    scopus 로고
    • A novel alkaline, thermostable, protease-free lipase from Pseudomonas sp.
    • Kulkarni N., Gadre R.V. A novel alkaline, thermostable, protease-free lipase from Pseudomonas sp. Biotechnol. Lett. 1999, 21:897-899.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 897-899
    • Kulkarni, N.1    Gadre, R.V.2
  • 50
    • 0347544003 scopus 로고    scopus 로고
    • Purification and characterization of an alkaline thermostable lipase from Aspergillus carneus
    • Saxena R.K., et al. Purification and characterization of an alkaline thermostable lipase from Aspergillus carneus. Process Biochem. 2003, 39:239-247.
    • (2003) Process Biochem. , vol.39 , pp. 239-247
    • Saxena, R.K.1
  • 51
    • 0037208467 scopus 로고    scopus 로고
    • Purification strategies for microbial lipases
    • Saxena R.K., et al. Purification strategies for microbial lipases. J. Microbiol. Meth. 2003, 52:1-18.
    • (2003) J. Microbiol. Meth. , vol.52 , pp. 1-18
    • Saxena, R.K.1
  • 52
    • 0002967929 scopus 로고    scopus 로고
    • Strategies in downstream processing
    • Wiley-VCH, G. Subramanian (Ed.)
    • Chisti Y. Strategies in downstream processing. Bioseparation and Bioprocessing: A Handbook 1998, 3-30. Wiley-VCH. G. Subramanian (Ed.).
    • (1998) Bioseparation and Bioprocessing: A Handbook , pp. 3-30
    • Chisti, Y.1
  • 53
    • 34447341128 scopus 로고    scopus 로고
    • Isolation and characterisation of three distinct forms of lipases from Candida rugosa produced in Solid State Fermentation
    • Benjamin S., Pandey A. Isolation and characterisation of three distinct forms of lipases from Candida rugosa produced in Solid State Fermentation. Braz. Arch. Biol. Technol. 2000, 43:453-460.
    • (2000) Braz. Arch. Biol. Technol. , vol.43 , pp. 453-460
    • Benjamin, S.1    Pandey, A.2
  • 54
    • 32044435832 scopus 로고    scopus 로고
    • Yeast lipases: enzyme purification, biochemical properties and gene cloning
    • Vakhlu J., Kour A. Yeast lipases: enzyme purification, biochemical properties and gene cloning. Electron. J. Biotechnol. 2006, 9:69-85.
    • (2006) Electron. J. Biotechnol. , vol.9 , pp. 69-85
    • Vakhlu, J.1    Kour, A.2
  • 55
    • 33745784439 scopus 로고    scopus 로고
    • Lipase localization in Rhizopus oryzae cells immobilized within biomass support particles for use as whole-cell biocatalysts in biodiesel-fuel production
    • Hama S., et al. Lipase localization in Rhizopus oryzae cells immobilized within biomass support particles for use as whole-cell biocatalysts in biodiesel-fuel production. J. Biosci. Bioeng. 2006, 101:328-333.
    • (2006) J. Biosci. Bioeng. , vol.101 , pp. 328-333
    • Hama, S.1
  • 56
    • 0037299885 scopus 로고    scopus 로고
    • Oil/mineral-salts medium designed for easy recovery of extracellular lipase from Fusarium oxysporum AM3
    • Camargo-de-Morais M.M., et al. Oil/mineral-salts medium designed for easy recovery of extracellular lipase from Fusarium oxysporum AM3. World J. Microbiol. Biotechnol. 2003, 19:17-20.
    • (2003) World J. Microbiol. Biotechnol. , vol.19 , pp. 17-20
    • Camargo-de-Morais, M.M.1
  • 57
    • 0028527576 scopus 로고
    • Lipase from a Brazilian strain of Penicillium citrinum
    • Pimentel M.C.B., et al. Lipase from a Brazilian strain of Penicillium citrinum. Appl. Biochem. Biotechnol. 1994, 49:59-74.
    • (1994) Appl. Biochem. Biotechnol. , vol.49 , pp. 59-74
    • Pimentel, M.C.B.1
  • 58
    • 0032469024 scopus 로고    scopus 로고
    • Production of extracellular lipase by a Candida rugosa strain isolated in Pernambuco, Brazil
    • Camargo-de-Morais M.M., et al. Production of extracellular lipase by a Candida rugosa strain isolated in Pernambuco, Brazil. Braz. J. Microbiol. 1998, 29:134-137.
    • (1998) Braz. J. Microbiol. , vol.29 , pp. 134-137
    • Camargo-de-Morais, M.M.1
  • 59
    • 0343526885 scopus 로고    scopus 로고
    • Effect of culture conditions on lipase production by Fusarium solani in batch fermentation
    • Maia M., et al. Effect of culture conditions on lipase production by Fusarium solani in batch fermentation. Bioresour. Technol. 2001, 76:23-27.
    • (2001) Bioresour. Technol. , vol.76 , pp. 23-27
    • Maia, M.1
  • 60
    • 0029186834 scopus 로고
    • Interesterification of butter fat by partially purified extracellular lipases from Pseudomonas putida, Aspergillus niger and Rhizopus oryzae
    • Pabai F., et al. Interesterification of butter fat by partially purified extracellular lipases from Pseudomonas putida, Aspergillus niger and Rhizopus oryzae. World J. Microbiol. Biotechnol. 1995, 11:669-677.
    • (1995) World J. Microbiol. Biotechnol. , vol.11 , pp. 669-677
    • Pabai, F.1
  • 61
    • 0031774033 scopus 로고    scopus 로고
    • Lipase from Pseudomonas aeruginosa LP602: biochemical properties and application for wastewater treatment
    • Dharmsthiti S., Kuhasuntisuk B. Lipase from Pseudomonas aeruginosa LP602: biochemical properties and application for wastewater treatment. J. Ind. Microbiol. Biotechnol. 1998, 21:75-80.
    • (1998) J. Ind. Microbiol. Biotechnol. , vol.21 , pp. 75-80
    • Dharmsthiti, S.1    Kuhasuntisuk, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.