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Volumn 48, Issue 7, 2013, Pages 1018-1024

Isolation and properties of β-xylosidase from Aspergillus niger GS1 using corn pericarp upon solid state fermentation

Author keywords

xylosidase; Aspergillus niger; Circular dichroism; Purification; Solid state fermentation

Indexed keywords

AGRO-INDUSTRIAL BYPRODUCTS; ALKALINE ELECTROLYZED WATERS; ASPERGILLUS NIGER; CHEMICAL-AND-HEAT TREATMENT; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; OPTIMAL TEMPERATURE; SOLID-STATE FERMENTATION; XYLOSIDASE;

EID: 84880049877     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2013.05.003     Document Type: Article
Times cited : (25)

References (56)
  • 1
    • 0001719868 scopus 로고
    • Xylan structure, microbial xylanases, and their mode of action
    • 10.1007/BF01198746
    • K. Bastawde Xylan structure, microbial xylanases, and their mode of action World J Microbiol Biotechnol 8 4 1992 353 368 10.1007/BF01198746
    • (1992) World J Microbiol Biotechnol , vol.8 , Issue.4 , pp. 353-368
    • Bastawde, K.1
  • 2
    • 0037088547 scopus 로고    scopus 로고
    • Investigation of the active site of the extracellular β-xylosidase from Aspergillus carbonarius
    • 10.1006/abbi.2002.2753
    • T. Kiss, A. Erdei, and L. Kiss Investigation of the active site of the extracellular β-xylosidase from Aspergillus carbonarius Arch Biochem Biophys 399 2 2002 188 194 10.1006/abbi.2002.2753
    • (2002) Arch Biochem Biophys , vol.399 , Issue.2 , pp. 188-194
    • Kiss, T.1    Erdei, A.2    Kiss, L.3
  • 3
    • 0037623814 scopus 로고    scopus 로고
    • Hemicellulose bioconversion
    • 10.1007/s10295-003-0049-x
    • B. Saha Hemicellulose bioconversion J Ind Microbiol Biotechnol 30 5 2003 279 291 10.1007/s10295-003-0049-x
    • (2003) J Ind Microbiol Biotechnol , vol.30 , Issue.5 , pp. 279-291
    • Saha, B.1
  • 5
    • 0035342183 scopus 로고    scopus 로고
    • Biotechnology and the utilization of biowaste as a resource for bioproduct development
    • 10.1007/s00449-012-0705-5
    • J.P.H. van Wyk Biotechnology and the utilization of biowaste as a resource for bioproduct development Trends Biotechnol 19 5 2001 172 177 10.1007/s00449-012-0705-5
    • (2001) Trends Biotechnol , vol.19 , Issue.5 , pp. 172-177
    • Van Wyk, J.P.H.1
  • 6
    • 80054043792 scopus 로고    scopus 로고
    • Optimization of fibrolytic enzyme production by Aspergillus japonicus C03 with potential application in ruminant feed and their effects on tropical forages hydrolysis
    • 10.1007/s00449-011-0553-8
    • F.D.A. Facchini, A.C. Vici, V.M. Benassi, L.A.P. Freitas, R.A. Reis, J.A. Jorge, H.F. Terenzi, and M.L.T.M. Polizeli Optimization of fibrolytic enzyme production by Aspergillus japonicus C03 with potential application in ruminant feed and their effects on tropical forages hydrolysis Bioprocess Biosyst 34 2011 1027 1038 10.1007/s00449-011-0553-8
    • (2011) Bioprocess Biosyst , vol.34 , pp. 1027-1038
    • Facchini, F.D.A.1    Vici, A.C.2    Benassi, V.M.3    Freitas, L.A.P.4    Reis, R.A.5    Jorge, J.A.6    Terenzi, H.F.7    Polizeli, M.L.T.M.8
  • 7
    • 28244477099 scopus 로고    scopus 로고
    • Structural insights into the β-xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy
    • 10.1021/bi050826j
    • A.L. Rojas, H. Fischer, E.V. Eneiskaya, A.A. Kulminskaya, K.A. Shabalin, K.N. Neustroev, A.F. Craievich, A.M. Golubev, and I. Polikarpov Structural insights into the β-xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scattering and circular dichroism spectroscopy Biochemistry 44 47 2005 15578 15584 10.1021/bi050826j
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15578-15584
    • Rojas, A.L.1    Fischer, H.2    Eneiskaya, E.V.3    Kulminskaya, A.A.4    Shabalin, K.A.5    Neustroev, K.N.6    Craievich, A.F.7    Golubev, A.M.8    Polikarpov, I.9
  • 8
    • 0024087074 scopus 로고
    • Multiplicity of β-1,4-xylanase in microorganisms: Functions and applications
    • K. Wong, L. Tan, and J. Saddler Multiplicity of β-1,4-xylanase in microorganisms: functions and applications Microbiol Rev 52 3 1988 305 317
    • (1988) Microbiol Rev , vol.52 , Issue.3 , pp. 305-317
    • Wong, K.1    Tan, L.2    Saddler, J.3
  • 9
    • 33646059703 scopus 로고    scopus 로고
    • Xylanolytic enzymes
    • J. Whitaker, W.S. Dominic, CRC Press New York 10.1201/9780203910450 [Chapter 71]
    • P. Biely Xylanolytic enzymes J. Whitaker, W.S. Dominic, Handbook of food enzymology 2002 CRC Press New York 879 915 10.1201/9780203910450 [Chapter 71]
    • (2002) Handbook of Food Enzymology , pp. 879-915
    • Biely, P.1
  • 10
    • 77950459098 scopus 로고    scopus 로고
    • β-Xylosidases from filamentous fungi: An overview
    • 10.1007/s11274-009-0190-4
    • A. Knob, C.R.F. Terrasan, and E.C. Carmona β-Xylosidases from filamentous fungi: an overview World J Microbiol Biotechnol 26 3 2010 389 407 10.1007/s11274-009-0190-4
    • (2010) World J Microbiol Biotechnol , vol.26 , Issue.3 , pp. 389-407
    • Knob, A.1    Terrasan, C.R.F.2    Carmona, E.C.3
  • 11
    • 0030642144 scopus 로고    scopus 로고
    • Xylanolytic enzymes from fungi and bacteria
    • 10.3109/07388559709146606
    • A. Sunna, and G. Antranikian Xylanolytic enzymes from fungi and bacteria Crit Rev Biotechnol 17 1 1997 39 67 10.3109/07388559709146606
    • (1997) Crit Rev Biotechnol , vol.17 , Issue.1 , pp. 39-67
    • Sunna, A.1    Antranikian, G.2
  • 12
    • 77957732016 scopus 로고    scopus 로고
    • Production and extraction optimization of xylanase from Aspergillus niger DFR-5 through solid-state-fermentation
    • 10.1016/j.biortech.2010.04.033
    • A. Pal, and F. Khanum Production and extraction optimization of xylanase from Aspergillus niger DFR-5 through solid-state-fermentation Bioresour Technol 101 19 2010 7563 7569 10.1016/j.biortech.2010.04.033
    • (2010) Bioresour Technol , vol.101 , Issue.19 , pp. 7563-7569
    • Pal, A.1    Khanum, F.2
  • 13
    • 77952549893 scopus 로고    scopus 로고
    • Advancement and comparative profiles in the production technologies using solid-state and submerged fermentation for microbial cellulases
    • 10.1016/j.enzmictec.2010.03.010
    • R.R. Singhania, R.K. Sukumaran, A.K. Patel, C. Larroche, and A. Pandey Advancement and comparative profiles in the production technologies using solid-state and submerged fermentation for microbial cellulases Enzyme Microb Technol 46 7 2010 541 549 10.1016/j.enzmictec.2010.03.010
    • (2010) Enzyme Microb Technol , vol.46 , Issue.7 , pp. 541-549
    • Singhania, R.R.1    Sukumaran, R.K.2    Patel, A.K.3    Larroche, C.4    Pandey, A.5
  • 14
    • 0037367678 scopus 로고    scopus 로고
    • Solid-state fermentation
    • 10.1016/S1369-703X(02)00121-3
    • A. Pandey Solid-state fermentation Biochem Eng J 13 2-3 2003 81 84 10.1016/S1369-703X(02)00121-3
    • (2003) Biochem Eng J , vol.13 , Issue.23 , pp. 81-84
    • Pandey, A.1
  • 15
    • 84862794694 scopus 로고    scopus 로고
    • Flow-through pretreatment with strongly acidic electrolyzed water for hemicellulose removal and enzymatic hydrolysis of corn stover
    • 10.1016/j.biortech.2011.12.062
    • H. Pei, L. Liu, X. Zhang, and J. Sun Flow-through pretreatment with strongly acidic electrolyzed water for hemicellulose removal and enzymatic hydrolysis of corn stover Bioresour Technol 110 April 2012 292 296 10.1016/j.biortech.2011.12.062
    • (2012) Bioresour Technol , vol.110 , Issue.APRIL , pp. 292-296
    • Pei, H.1    Liu, L.2    Zhang, X.3    Sun, J.4
  • 16
    • 84864721448 scopus 로고    scopus 로고
    • Pretreatment of switchgrass with electrolyzed water and a two-stage method for bioethanol production
    • 10.1007/s12257-011-0583-8
    • X. Wang, H. Feng, and Z. Li Pretreatment of switchgrass with electrolyzed water and a two-stage method for bioethanol production Biotechnol Bioprocess Eng 17 3 2012 624 633 10.1007/s12257-011-0583-8
    • (2012) Biotechnol Bioprocess Eng , vol.17 , Issue.3 , pp. 624-633
    • Wang, X.1    Feng, H.2    Li, Z.3
  • 17
    • 84884309629 scopus 로고    scopus 로고
    • Ethanol production from corn stover pretreated by electrolyzed water and a two-step pretreatment method
    • 10.1007/s11434-012-5079-1
    • X. Wang, H. Feng, and Z.Y. Li Ethanol production from corn stover pretreated by electrolyzed water and a two-step pretreatment method Chin Sci Bull 57 15 2012 1796 1802 10.1007/s11434-012-5079-1
    • (2012) Chin Sci Bull , vol.57 , Issue.15 , pp. 1796-1802
    • Wang, X.1    Feng, H.2    Li, Z.Y.3
  • 18
    • 84868638669 scopus 로고    scopus 로고
    • Biobutanol production from fiber-enhanced DDGS pretreated with electrolyzed water
    • 10.1016/j.renene.2012.10.011
    • X. Wang, Y. Wang, B. Wang, H. Blaschek, H. Feng, and Z. Li Biobutanol production from fiber-enhanced DDGS pretreated with electrolyzed water Renew Energy 52 April 2013 16 22 10.1016/j.renene.2012.10.011
    • (2013) Renew Energy , vol.52 , Issue.APRIL , pp. 16-22
    • Wang, X.1    Wang, Y.2    Wang, B.3    Blaschek, H.4    Feng, H.5    Li, Z.6
  • 19
    • 84880062760 scopus 로고    scopus 로고
    • Pretreatment of corn stover by acidic electrolyzed water for enhancing hemicellulose degradation
    • 10.1166/jbmb.2011.1164
    • H. Pei, J. Sun, L. Liu, J. Hu, X. Zhang, and J. Zhang Pretreatment of corn stover by acidic electrolyzed water for enhancing hemicellulose degradation J Biobased Mater Bioenergy 5 3 2011 403 408 10.1166/jbmb.2011.1164
    • (2011) J Biobased Mater Bioenergy , vol.5 , Issue.3 , pp. 403-408
    • Pei, H.1    Sun, J.2    Liu, L.3    Hu, J.4    Zhang, X.5    Zhang, J.6
  • 20
    • 84873447333 scopus 로고    scopus 로고
    • Characterization of an ethanol-tolerant 1,4-B-D-xylosidase produced by Pichia membranifaciens
    • 10.1111/j.1472-765X.2012.03297.x
    • A.M. Romero, J.J. Mateo, and S. Maicas Characterization of an ethanol-tolerant 1,4-B-D-xylosidase produced by Pichia membranifaciens Lett Appl Microbiol 55 5 2012 354 361 10.1111/j.1472-765X.2012.03297.x
    • (2012) Lett Appl Microbiol , vol.55 , Issue.5 , pp. 354-361
    • Romero, A.M.1    Mateo, J.J.2    Maicas, S.3
  • 21
    • 84880058775 scopus 로고    scopus 로고
    • Family 30; 2012. [accessed 31.08.2012]
    • Glycoside hydrolase. Family 30; 2012. http://www.cazy.org/GH30.html [accessed 31.08.2012].
    • Glycoside Hydrolase
  • 23
    • 84880052852 scopus 로고    scopus 로고
    • Loss on drying (moisture) for feeds
    • 17th ed. W. Horwitz, AOAC International Maryland, USA
    • AOAC ed. Method 930.15 Loss on drying (moisture) for feeds 17th ed. W. Horwitz, Official methods of analysis of AOAC international vol. I 2002 AOAC International Maryland, USA
    • (2002) Official Methods of Analysis of AOAC International , vol.1
  • 24
    • 84880053491 scopus 로고    scopus 로고
    • Protein (crude) in animal feed and pet food
    • 17th ed. W. Horwitz, AOAC International Maryland, USA
    • AOAC ed. Method 954.01 Protein (crude) in animal feed and pet food 17th ed. W. Horwitz, Official methods of analysis of AOAC international vol. I 2002 AOAC International Maryland, USA
    • (2002) Official Methods of Analysis of AOAC International , vol.1
  • 25
    • 67349087226 scopus 로고    scopus 로고
    • Fat (crude) or ether extract in animal feed
    • 17th ed. W. Horwitz, AOAC International Maryland, USA
    • AOAC, Method 920.39 Fat (crude) or ether extract in animal feed 17th ed. W. Horwitz, Official methods of analysis of AOAC international vol. I 2002 AOAC International Maryland, USA
    • (2002) Official Methods of Analysis of AOAC International , vol.1
  • 26
    • 84904464532 scopus 로고    scopus 로고
    • Ash of animal feed
    • W. Horwitz, 17th ed. AOAC International: Maryland USA
    • AOAC, ed. Method 942.05 Ash of animal feed W. Horwitz, 17th ed. Official methods of analysis of AOAC international vol. I. 2002 AOAC International: Maryland USA
    • (2002) Official Methods of Analysis of AOAC International , vol.1
  • 29
  • 30
    • 79955490391 scopus 로고    scopus 로고
    • Production of hemicellulolytic enzymes through solid substrate fermentation and their application in the production of balanced feed for broilers
    • I. Lagunas-Bernabé, B. Garcia-Almendárez, E. Castaño-Tostado, C. Regalado González, and E. Ávila González Production of hemicellulolytic enzymes through solid substrate fermentation and their application in the production of balanced feed for broilers Vet Mex 37 1 2006 1 13
    • (2006) Vet Mex , vol.37 , Issue.1 , pp. 1-13
    • Lagunas-Bernabé, I.1    Garcia-Almendárez, B.2    Castaño-Tostado, E.3    Regalado González, C.4    Ávila González, E.5
  • 31
    • 18844363446 scopus 로고    scopus 로고
    • Effect of media composition and growth conditions on production of β-glucosidase by Aspergillus niger C-6
    • O. Garcia-Kirchner, M. Segura-Granados, and P. Rodriguez-Pascual Effect of media composition and growth conditions on production of β-glucosidase by Aspergillus niger C-6 Appl Biochem Biotechnol 121 1-3 2005 347 359
    • (2005) Appl Biochem Biotechnol , vol.121 , Issue.13 , pp. 347-359
    • Garcia-Kirchner, O.1    Segura-Granados, M.2    Rodriguez-Pascual, P.3
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3
    • M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1-2 1976 248 254 10.1016/0003-2697(76)90527-3
    • (1976) Anal Biochem , vol.72 , Issue.12 , pp. 248-254
    • Bradford, M.1
  • 33
    • 34147156264 scopus 로고    scopus 로고
    • Identification of thermostable β-xylosidase activities produced by Aspergillus brasiliensis and Aspergillus niger
    • 10.1007/s10529-007-9314-9
    • M. Pedersen, H. Lauritzen, J. Frisvad, and A. Meyer Identification of thermostable β-xylosidase activities produced by Aspergillus brasiliensis and Aspergillus niger Biotechnol Lett 29 5 2007 743 748 10.1007/s10529-007-9314- 9
    • (2007) Biotechnol Lett , vol.29 , Issue.5 , pp. 743-748
    • Pedersen, M.1    Lauritzen, H.2    Frisvad, J.3    Meyer, A.4
  • 34
    • 33747333106 scopus 로고
    • Use of dinitrosalicilyc acid reagent for determination of reducing sugar
    • G.L. Miller Use of dinitrosalicilyc acid reagent for determination of reducing sugar Anal Chem 31 3 1959 426 428
    • (1959) Anal Chem , vol.31 , Issue.3 , pp. 426-428
    • Miller, G.L.1
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0
    • U. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 5259 1970 680 685 10.1038/227680a0
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.1
  • 36
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • 10.1002/elps.1150080203
    • H. Blum, H. Beier, and H.J. Gross Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels Electrophoresis 8 2 1987 93 99 10.1002/elps.1150080203
    • (1987) Electrophoresis , vol.8 , Issue.2 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 37
    • 33947661471 scopus 로고    scopus 로고
    • Isolation and characterization of a thermostable β-xylosidase in the thermophilic bacterium Geobacillus pallidus
    • 10.1016/j.bbapap.2007.02.002
    • D. Quintero, Z. Velasco, E. Hurtado-Gomez, J.L. Neira, and L.M. Contreras Isolation and characterization of a thermostable β-xylosidase in the thermophilic bacterium Geobacillus pallidus BBA-Proteins Proteom 1774 4 2007 510 518 10.1016/j.bbapap.2007.02.002
    • (2007) BBA-Proteins Proteom , vol.1774 , Issue.4 , pp. 510-518
    • Quintero, D.1    Velasco, Z.2    Hurtado-Gomez, E.3    Neira, J.L.4    Contreras, L.M.5
  • 38
    • 78049264854 scopus 로고    scopus 로고
    • Consolidation of glycosyl hydrolase family 30: A dual domain 4/7 hydrolase family consisting of two structurally distinct groups
    • 10.1016/j.febslet.2010.09.051
    • F.J. St John, J.M. González, and E. Pozharski Consolidation of glycosyl hydrolase family 30: A dual domain 4/7 hydrolase family consisting of two structurally distinct groups FEBS Lett 584 21 2010 4435 4441 10.1016/j.febslet.2010.09.051
    • (2010) FEBS Lett , vol.584 , Issue.21 , pp. 4435-4441
    • St John, F.J.1    González, J.M.2    Pozharski, E.3
  • 39
    • 72449126528 scopus 로고    scopus 로고
    • Nanostructural assembly of cellulose, hemicellulose, and lignin in the middle layer of secondary wall of ginkgo tracheid
    • 10.1007/s10086-009-1049-x
    • N. Terashima, K. Kitano, M. Kojima, M. Yoshida, H. Yamamoto, and U. Westermark Nanostructural assembly of cellulose, hemicellulose, and lignin in the middle layer of secondary wall of ginkgo tracheid J Wood Sci 55 6 2009 409 416 10.1007/s10086-009-1049-x
    • (2009) J Wood Sci , vol.55 , Issue.6 , pp. 409-416
    • Terashima, N.1    Kitano, K.2    Kojima, M.3    Yoshida, M.4    Yamamoto, H.5    Westermark, U.6
  • 41
    • 67650567113 scopus 로고    scopus 로고
    • Pretreatment and conversion of distiller's dried grains with solubles for acetone-butanol-ethanol (ABE) production
    • B. Wang, T. Ezeji, Z. Shi, H. Feng, and H.P. Blaschek Pretreatment and conversion of distiller's dried grains with solubles for acetone-butanol-ethanol (ABE) production Trans ASABE 52 3 2009 885 892
    • (2009) Trans ASABE , vol.52 , Issue.3 , pp. 885-892
    • Wang, B.1    Ezeji, T.2    Shi, Z.3    Feng, H.4    Blaschek, H.P.5
  • 42
    • 83055165705 scopus 로고    scopus 로고
    • Chemical characterization of Klason lignin preparations from plant-based foods
    • 10.1021/jf2031378
    • M. Bunzel, A. Schüßler, and G. Saha Chemical characterization of Klason lignin preparations from plant-based foods J Agric Food Chem 59 23 2011 12506 12513 10.1021/jf2031378
    • (2011) J Agric Food Chem , vol.59 , Issue.23 , pp. 12506-12513
    • Bunzel, M.1    Schüßler, A.2    Saha, G.3
  • 43
    • 84861861916 scopus 로고    scopus 로고
    • Plant fatty acyl reductases: Enzymes generating fatty alcohols for protective layers with potential for industrial applications
    • 10.1016/j.plantsci.2012.05.002
    • O. Rowland, and F. Domergue Plant fatty acyl reductases: enzymes generating fatty alcohols for protective layers with potential for industrial applications Plant Sci 193-194 2012 28 38 10.1016/j.plantsci.2012.05.002
    • (2012) Plant Sci , vol.193-194 , pp. 28-38
    • Rowland, O.1    Domergue, F.2
  • 44
    • 0035873049 scopus 로고    scopus 로고
    • Diferulates as structural components in soluble and insoluble cereal dietary fibre
    • 10.1021/jf2031378
    • M. Bunzel, J. Ralph, J.M. Marita, R.D. Hatfield, and H. Steinhart Diferulates as structural components in soluble and insoluble cereal dietary fibre J Sci Food Agric 81 2001 653 660 10.1021/jf2031378
    • (2001) J Sci Food Agric , vol.81 , pp. 653-660
    • Bunzel, M.1    Ralph, J.2    Marita, J.M.3    Hatfield, R.D.4    Steinhart, H.5
  • 45
    • 0038157323 scopus 로고    scopus 로고
    • Microbial hemicellulases
    • 10.1016/S1369-5274(03)00056-0
    • D. Shallom, and Y. Shoham Microbial hemicellulases Curr Opin Microbiol 6 3 2003 219 228 10.1016/S1369-5274(03)00056-0
    • (2003) Curr Opin Microbiol , vol.6 , Issue.3 , pp. 219-228
    • Shallom, D.1    Shoham, Y.2
  • 46
    • 72449210541 scopus 로고    scopus 로고
    • Isolation and properties of extracellular β-xylosidases from fungi Aspergillus japonicus and Trichoderma reesei
    • 10.1134/S0006297909090089
    • M. Semenova, M. Drachevskaya, O. Sinitsyna, A. Gusakov, and A. Sinitsyn Isolation and properties of extracellular β-xylosidases from fungi Aspergillus japonicus and Trichoderma reesei Biochem (Moscow) 74 9 2009 1002 1008 10.1134/S0006297909090089
    • (2009) Biochem (Moscow) , vol.74 , Issue.9 , pp. 1002-1008
    • Semenova, M.1    Drachevskaya, M.2    Sinitsyna, O.3    Gusakov, A.4    Sinitsyn, A.5
  • 47
    • 47549099453 scopus 로고    scopus 로고
    • Performance of Aspergillus niger B 03 β-xylosidase immobilized on polyamide membrane support
    • 10.1016/j.molcatb.2007.12.019
    • G. Delcheva, G. Dobrev, and I. Pishtiyski Performance of Aspergillus niger B 03 β-xylosidase immobilized on polyamide membrane support J Mol Catal B: Enzym 54 3-4 2008 109 115 10.1016/j.molcatb.2007.12.019
    • (2008) J Mol Catal B: Enzym , vol.54 , Issue.34 , pp. 109-115
    • Delcheva, G.1    Dobrev, G.2    Pishtiyski, I.3
  • 48
    • 84873423709 scopus 로고    scopus 로고
    • Immobilization and biochemical properties of a β-xylosidase activated by glucose/xylose from Aspergillus niger USP-67 with transxylosylation activity
    • 10.1016/j.molcatb.2012.12.010
    • V.M. Benassi, T. Marcio-da Silva, B.C. Pessela, J.M. Guisan, C. Mateo, M.S. Lima, J.A. Jorge, and M.L.T.M. Polizeli Immobilization and biochemical properties of a β-xylosidase activated by glucose/xylose from Aspergillus niger USP-67 with transxylosylation activity J Mol Catal B: Enzym 89 2013 93 101 10.1016/j.molcatb.2012.12.010
    • (2013) J Mol Catal B: Enzym , vol.89 , pp. 93-101
    • Benassi, V.M.1    Marcio-Da Silva, T.2    Pessela, B.C.3    Guisan, J.M.4    Mateo, C.5    Lima, M.S.6    Jorge, J.A.7    Polizeli, M.L.T.M.8
  • 49
    • 4344599124 scopus 로고    scopus 로고
    • Effect of carbon source on the biochemical properties of β-xylosidases produced by Aspergillus versicolor
    • 10.1016/j.procbio.2003.09.024
    • S. Andrade, M.L.T.M. Polizeli, H.F. Terenzi, and J.A. Jorge Effect of carbon source on the biochemical properties of β-xylosidases produced by Aspergillus versicolor Process Biochem 39 12 2004 1931 1938 10.1016/j.procbio. 2003.09.024
    • (2004) Process Biochem , vol.39 , Issue.12 , pp. 1931-1938
    • Andrade, S.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 50
    • 74049085053 scopus 로고    scopus 로고
    • Characterization of Aspergillus oryzae glycoside hydrolase family 43 β-xylosidase expressed in Escherichia coli
    • 10.1016/j.jbiosc.2009.07.018
    • S. Suzuki, M. Fukuoka, H. Ookuchi, M. Sano, K. Ozeki, E. Nagaioshi, Y. Takii, M. Matsushita, S. Tada, and K.I. Kusumoto Characterization of Aspergillus oryzae glycoside hydrolase family 43 β-xylosidase expressed in Escherichia coli J Biosci Bioeng 109 2 2010 115 117 10.1016/j.jbiosc.2009.07.018
    • (2010) J Biosci Bioeng , vol.109 , Issue.2 , pp. 115-117
    • Suzuki, S.1    Fukuoka, M.2    Ookuchi, H.3    Sano, M.4    Ozeki, K.5    Nagaioshi, E.6    Takii, Y.7    Matsushita, M.8    Tada, S.9    Kusumoto, K.I.10
  • 53
    • 0030061755 scopus 로고    scopus 로고
    • Purification and regulation of the synthesis of β-xylosidase from Aspergillus nidulans
    • 10.1111/j.1574-6968.1996.tb08003.x
    • S. Kumar, and D. Ramón Purification and regulation of the synthesis of β-xylosidase from Aspergillus nidulans FEMS Microbiol Lett 135 2-3 1996 287 293 10.1111/j.1574-6968.1996.tb08003.x
    • (1996) FEMS Microbiol Lett , vol.135 , Issue.23 , pp. 287-293
    • Kumar, S.1    Ramón, D.2
  • 54
    • 54949145317 scopus 로고    scopus 로고
    • The family 52 β-xylosidase from Geobacillus stearothermophilus is a dimer: Structural and biophysical characterization of a glycoside hydrolase
    • 10.1016/j.bbapap.2008.06.019
    • L. Contreras, J. Gómez, J. Prieto, J. Clemente-Jiménez, F. Las Heras-Vázquez, F. Rodríguez-Vico, F. Blanco, and J. Neira The family 52 β-xylosidase from Geobacillus stearothermophilus is a dimer: structural and biophysical characterization of a glycoside hydrolase BBA-Proteins Proteom 1784 12 2008 1924 1934 10.1016/j.bbapap.2008.06.019
    • (2008) BBA-Proteins Proteom , vol.1784 , Issue.12 , pp. 1924-1934
    • Contreras, L.1    Gómez, J.2    Prieto, J.3    Clemente-Jiménez, J.4    Las Heras-Vázquez, F.5    Rodríguez-Vico, F.6    Blanco, F.7    Neira, J.8
  • 55
    • 84862906889 scopus 로고    scopus 로고
    • Thermal denaturation of a blue-copper laccase: Formation of a compact denatured state with residual structure linked to pH changes in the region of histidine protonation
    • 10.1016/j.bpc.2012.04.004
    • C. Toledo-Núñez, J.I. López-Cruz, and A. Hernández-Arana Thermal denaturation of a blue-copper laccase: formation of a compact denatured state with residual structure linked to pH changes in the region of histidine protonation Biophys Chem 167 2012 36 42 10.1016/j.bpc.2012.04.004
    • (2012) Biophys Chem , vol.167 , pp. 36-42
    • Toledo-Núñez, C.1    López-Cruz, J.I.2    Hernández- Arana, A.3
  • 56
    • 33947148277 scopus 로고    scopus 로고
    • Kinetic parameters and thermodynamic values of β-xylosidase production by Kluyveromyces marxianus
    • 10.1016/j.biortech.2006.08.029
    • M.I. Rajoka Kinetic parameters and thermodynamic values of β-xylosidase production by Kluyveromyces marxianus Bioresour Technol 98 11 2007 2212 2219 10.1016/j.biortech.2006.08.029
    • (2007) Bioresour Technol , vol.98 , Issue.11 , pp. 2212-2219
    • Rajoka, M.I.1


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