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Volumn 7, Issue 23, 2008, Pages 4251-4259

Cloning, sequencing and expression of a novel xylanase cDNA from a newly isolated Aspergillus awamori in Pichia pastoris

Author keywords

Aspergillus awamori; cDNA; Cloning; Eukaryotic expression; Purification and characterization; Xylanase

Indexed keywords

ALCOHOL OXIDASE; AMINO ACID; COMPLEMENTARY DNA; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 57649239132     PISSN: None     EISSN: 16845315     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (42)
  • 2
    • 0028419723 scopus 로고
    • Production and characterization of thermostable xylanases by Thermomyces lanuginosus and Thermoascus aurantiacus grown on lignocelluloses
    • Alam M, Gomes I, Mohiuddin G, Hoq MM (1994). Production and characterization of thermostable xylanases by Thermomyces lanuginosus and Thermoascus aurantiacus grown on lignocelluloses. Enzyme Microb Technol 16: 298-302.
    • (1994) Enzyme Microb Technol , vol.16 , pp. 298-302
    • Alam, M.1    Gomes, I.2    Mohiuddin, G.3    Hoq, M.M.4
  • 3
    • 33847303968 scopus 로고    scopus 로고
    • Production of xylanase by Trichoderma longibrachiatum on a mixture of wheat bran and wheat straw Optimization of culture condition by Taguchi method
    • Azin M, Moravej R, Zareh D (2007). Production of xylanase by Trichoderma longibrachiatum on a mixture of wheat bran and wheat straw Optimization of culture condition by Taguchi method. Enzyme Microbiol Technol 40: 801-805.
    • (2007) Enzyme Microbiol Technol , vol.40 , pp. 801-805
    • Azin, M.1    Moravej, R.2    Zareh, D.3
  • 4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermentor cultures of the yeast Pichia pastoris
    • Cereghino GC, Cereghino J, Ilgen C, Cregg J (2002). Production of recombinant proteins in fermentor cultures of the yeast Pichia pastoris. Curr. Opin. Biotechnol. 13: 329-332.
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 329-332
    • Cereghino, G.C.1    Cereghino, J.2    Ilgen, C.3    Cregg, J.4
  • 7
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction
    • Chomczynski P, Sacchi N (1987). Single step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction. Anal. Biochem. 162: 156-159.
    • (1987) Anal. Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 8
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung CT, Niemela SL, Miller RH (1989). One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA. 86: 2172-2175.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 9
    • 0142061109 scopus 로고    scopus 로고
    • Damaso MCT, Almeida MS, Kurtenbach E, Martins OB, Pereira N, Andrade CMM, Albano RM (2003). Optimized expression of a thermostable xylanase from Theromyces langinosus in Pichia pastoris. Appl. Environ. Microbio. l69: 6064-6072.
    • Damaso MCT, Almeida MS, Kurtenbach E, Martins OB, Pereira N, Andrade CMM, Albano RM (2003). Optimized expression of a thermostable xylanase from Theromyces langinosus in Pichia pastoris. Appl. Environ. Microbio. l69: 6064-6072.
  • 10
    • 0002594984 scopus 로고
    • A rapid DNA isolation procedure for small quantities of fresh leaf tissues
    • Doyle JJ, Doyle JL (1987). A rapid DNA isolation procedure for small quantities of fresh leaf tissues. Phytochem. Bull. 19: 11-15.
    • (1987) Phytochem. Bull , vol.19 , pp. 11-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 11
    • 0028200558 scopus 로고
    • Purification, characterization, and substrate specificities of multiple xylanases from Streptomyces sp. strain B-l 2-2
    • Eliger G, Szakiics G, Jeffries TW (1994). Purification, characterization, and substrate specificities of multiple xylanases from Streptomyces sp. strain B-l 2-2. Appl. Environ. Microbial. 60: 2609-2615.
    • (1994) Appl. Environ. Microbial , vol.60 , pp. 2609-2615
    • Eliger, G.1    Szakiics, G.2    Jeffries, T.W.3
  • 12
    • 0028119339 scopus 로고
    • Identification of the ectomycorrhizal basidiomycete tylospora-fibrillosa donk by RFLP analysis of the PCR-amplified ITS and IGS regions of ribosomal DNA
    • Erland S, Henrion B, Martin F, Glover LA, Alexander IJ (1994). Identification of the ectomycorrhizal basidiomycete tylospora-fibrillosa donk by RFLP analysis of the PCR-amplified ITS and IGS regions of ribosomal DNA. New Phytol. 126: 525-532.
    • (1994) New Phytol , vol.126 , pp. 525-532
    • Erland, S.1    Henrion, B.2    Martin, F.3    Glover, L.A.4    Alexander, I.J.5
  • 13
    • 0018727624 scopus 로고
    • Use of competitive inhibitors to study substrate binding order
    • Fromm HJ (1979). Use of competitive inhibitors to study substrate binding order. Methods Enzymol. 63: 467-486.
    • (1979) Methods Enzymol , vol.63 , pp. 467-486
    • Fromm, H.J.1
  • 14
    • 0027580147 scopus 로고
    • ITS primers with enhanced specificity for basidiomycetes-application to the identification of mycorrhizae and rusts
    • Gardes M, Bruns TD (1993). ITS primers with enhanced specificity for basidiomycetes-application to the identification of mycorrhizae and rusts. Mol. Ecol. 2: 113-118.
    • (1993) Mol. Ecol , vol.2 , pp. 113-118
    • Gardes, M.1    Bruns, T.D.2
  • 15
    • 0027284092 scopus 로고
    • Aspergillus sydowii MG 49 is a strong producer of thermostable xylanolytic enzyme
    • Ghosh M, Das A, Mishra AK, Nanda G (1993). Aspergillus sydowii MG 49 is a strong producer of thermostable xylanolytic enzyme. Enzyme Microbiol. Technol. 15: 703-709.
    • (1993) Enzyme Microbiol. Technol , vol.15 , pp. 703-709
    • Ghosh, M.1    Das, A.2    Mishra, A.K.3    Nanda, G.4
  • 16
    • 0027468318 scopus 로고    scopus 로고
    • Gilbert HJ, Hazlewood GP (1993). Bacterial ceilulases and xyianases. J. Gen. Microbiot. 39: 187-194.
    • Gilbert HJ, Hazlewood GP (1993). Bacterial ceilulases and xyianases. J. Gen. Microbiot. 39: 187-194.
  • 19
    • 0141973993 scopus 로고
    • Acid stable xylanase from Aspergillus kawachii
    • Ito K (1993). Acid stable xylanase from Aspergillus kawachii. J. Brew. Soc. Jpn. 88: 920-928.
    • (1993) J. Brew. Soc. Jpn , vol.88 , pp. 920-928
    • Ito, K.1
  • 20
    • 21344435552 scopus 로고    scopus 로고
    • Characterization of a xylanase from the newly isolated thermophilic Thermomyces lanuginosus CAU44 and its application in bread making
    • Jiang ZQ, Yang SQ, Tan SS, Li LT, Li XT (2005). Characterization of a xylanase from the newly isolated thermophilic Thermomyces lanuginosus CAU44 and its application in bread making. Lett. Appl. Microbiol. 41: 69-76.
    • (2005) Lett. Appl. Microbiol , vol.41 , pp. 69-76
    • Jiang, Z.Q.1    Yang, S.Q.2    Tan, S.S.3    Li, L.T.4    Li, X.T.5
  • 21
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni N, Shendye A, Rao M, (1999). Molecular and biotechnological aspects of xylanases. FEMS Microbiol. Rev. 23: 411-456.
    • (1999) FEMS Microbiol. Rev , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 22
    • 33847743042 scopus 로고    scopus 로고
    • Improvement of xylanase production by Penicillium oxalicum ZH-30 using response surface methodology
    • Li Y, Cui F, Liu Z, Xu Y, Zhao H (2007a). Improvement of xylanase production by Penicillium oxalicum ZH-30 using response surface methodology. Enzyme Microbiol. Technol. 40: 1381-1388.
    • (2007) Enzyme Microbiol. Technol , vol.40 , pp. 1381-1388
    • Li, Y.1    Cui, F.2    Liu, Z.3    Xu, Y.4    Zhao, H.5
  • 23
    • 33847341579 scopus 로고    scopus 로고
    • Statistical optimization of xylanase production from new isolated Penicillium oxalicum ZH-30 in submerged fermentation
    • Li Y, Liu Z, Zhao H, Xu Y, Cui F (2007b). Statistical optimization of xylanase production from new isolated Penicillium oxalicum ZH-30 in submerged fermentation. Biochem. Eng. J. 34: 82-86.
    • (2007) Biochem. Eng. J , vol.34 , pp. 82-86
    • Li, Y.1    Liu, Z.2    Zhao, H.3    Xu, Y.4    Cui, F.5
  • 24
    • 13244296962 scopus 로고    scopus 로고
    • Cloning and expression of D-lactonohydrolase cDNA from Fusarium moniliforme in Saccharomyces cerevisiae
    • Liu ZQ, Sun ZH (2004). Cloning and expression of D-lactonohydrolase cDNA from Fusarium moniliforme in Saccharomyces cerevisiae. Biotech. Lett. 26: 1861-1865.
    • (2004) Biotech. Lett , vol.26 , pp. 1861-1865
    • Liu, Z.Q.1    Sun, Z.H.2
  • 25
    • 33748432544 scopus 로고    scopus 로고
    • Directed Evolution of D-pactonohydrolase from Fusarium moniliforme
    • Liu ZQ, Sun ZH, Leng Y (2006). Directed Evolution of D-pactonohydrolase from Fusarium moniliforme. J. Agric. Food Chem. 54: 5823-5830.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 5823-5830
    • Liu, Z.Q.1    Sun, Z.H.2    Leng, Y.3
  • 26
    • 21644469289 scopus 로고    scopus 로고
    • Effects of molecular weight and concentration of arabinoxylans on the membrane plugging
    • Liu J, Li Y, Gu GX, Mao Z (2005). Effects of molecular weight and concentration of arabinoxylans on the membrane plugging. J. Agric. Food Chem. 53: 4996-5002.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 4996-5002
    • Liu, J.1    Li, Y.2    Gu, G.X.3    Mao, Z.4
  • 27
    • 39149137161 scopus 로고    scopus 로고
    • Production of astaxanthin from a newly isolated phaffia rhodozyma mutant by low-energy ions beam implantation
    • Liu ZQ, Zhang JF, Zheng YG, Shen YC (2008). Production of astaxanthin from a newly isolated phaffia rhodozyma mutant by low-energy ions beam implantation. J. Appl. Microbiol. 108: 861-872.
    • (2008) J. Appl. Microbiol , vol.108 , pp. 861-872
    • Liu, Z.Q.1    Zhang, J.F.2    Zheng, Y.G.3    Shen, Y.C.4
  • 28
    • 57649147665 scopus 로고    scopus 로고
    • Maat J, Roza M, Verbakel J, Stam H, DaSilra MJS, Egmond MR, Hagemans MLD, Gorcom RFM, Hessing JGM, Van den Hondel, CAMJJ, Van Rotterdam C (1992). Xylanases and their application in bakery. Xylanases and Their Applications in Bakery. In: Xylan and Xylanases, Progress in Biotechnology No. 7, Visser J, Kusters van Someren MA, Beldman G, Voragen AGJ (Eds.), Elsevier Science Publishers, Amsterdam, The Netherlands pp. 349-360.
    • Maat J, Roza M, Verbakel J, Stam H, DaSilra MJS, Egmond MR, Hagemans MLD, Gorcom RFM, Hessing JGM, Van den Hondel, CAMJJ, Van Rotterdam C (1992). Xylanases and their application in bakery. Xylanases and Their Applications in Bakery. In: Xylan and Xylanases, Progress in Biotechnology No. 7, Visser J, Kusters van Someren MA, Beldman G, Voragen AGJ (Eds.), Elsevier Science Publishers, Amsterdam, The Netherlands pp. 349-360.
  • 29
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller GL (1959). Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 31: 426-428.
    • (1959) Anal. Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 30
    • 33744515651 scopus 로고    scopus 로고
    • Thermal Stabilization of Bacillus subtilis Family-11 Xylanase by Directed Evolution
    • Miyazaki K, Takenouchi M, Kondo H, Noro N, Suzuki M, Tsuda S (2006). Thermal Stabilization of Bacillus subtilis Family-11 Xylanase by Directed Evolution. J. Biol. Chem. 281: 10236-10242.
    • (2006) J. Biol. Chem , vol.281 , pp. 10236-10242
    • Miyazaki, K.1    Takenouchi, M.2    Kondo, H.3    Noro, N.4    Suzuki, M.5    Tsuda, S.6
  • 31
    • 0027968572 scopus 로고
    • Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans
    • Moreau A, Roberge M, Manin C, Shareck F, Kluepfel D, Morosoli R (1994). Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans. Biochem. J. 302: 291-295.
    • (1994) Biochem. J , vol.302 , pp. 291-295
    • Moreau, A.1    Roberge, M.2    Manin, C.3    Shareck, F.4    Kluepfel, D.5    Morosoli, R.6
  • 32
    • 0001466504 scopus 로고
    • Production and characterization of xylanase from a Strepfomyces species grown on agricultural wastes
    • Patel BN, Ray RM (1994). Production and characterization of xylanase from a Strepfomyces species grown on agricultural wastes. World J. Microbial. Biotechnol. 10: 599-605.
    • (1994) World J. Microbial. Biotechnol , vol.10 , pp. 599-605
    • Patel, B.N.1    Ray, R.M.2
  • 35
    • 13844272454 scopus 로고    scopus 로고
    • Xylanase production by a newly isolated Aspergillus foetidus strain and its characterization
    • Shah AR, Madamwar D (2005). Xylanase production by a newly isolated Aspergillus foetidus strain and its characterization. Process Biochem. 40: 1763-1771.
    • (2005) Process Biochem , vol.40 , pp. 1763-1771
    • Shah, A.R.1    Madamwar, D.2
  • 36
    • 33645736445 scopus 로고    scopus 로고
    • A study on the interaction of xylanase and phytase enzymes in wheat-based diets fed to commercial white and brown egg laying hens
    • Silversides FG, Scott TA, Korver DR, Afsharmanesh M, Hruby M (2006). A study on the interaction of xylanase and phytase enzymes in wheat-based diets fed to commercial white and brown egg laying hens. Poultry Sci. 85: 297-305.
    • (2006) Poultry Sci , vol.85 , pp. 297-305
    • Silversides, F.G.1    Scott, T.A.2    Korver, D.R.3    Afsharmanesh, M.4    Hruby, M.5
  • 37
    • 34250512499 scopus 로고
    • Recent progress in the chemistry of wood hemicelluloses
    • Timell TE (1967). Recent progress in the chemistry of wood hemicelluloses. Wood Sci. Technol. 1: 45-70.
    • (1967) Wood Sci. Technol , vol.1 , pp. 45-70
    • Timell, T.E.1
  • 38
    • 0025132809 scopus 로고
    • Purification and properties of three types of xylanases produced by an alkalophilic actinomycete
    • Tsujibo H, Sakamoto T, Nishino N, Hasegawa T, Inamori Y (1990). Purification and properties of three types of xylanases produced by an alkalophilic actinomycete. J. Appl. Bacterial. 69: 398-405.
    • (1990) J. Appl. Bacterial , vol.69 , pp. 398-405
    • Tsujibo, H.1    Sakamoto, T.2    Nishino, N.3    Hasegawa, T.4    Inamori, Y.5
  • 39
    • 0029311205 scopus 로고
    • Assessment of various commercial enzymes in the bleaching of radiata pine kraft pulps
    • Vicuna R, Oyarzum E, Osses M (1995). Assessment of various commercial enzymes in the bleaching of radiata pine kraft pulps. J. Biotechnol. 40: 163-168.
    • (1995) J. Biotechnol , vol.40 , pp. 163-168
    • Vicuna, R.1    Oyarzum, E.2    Osses, M.3
  • 40
    • 0027367326 scopus 로고
    • Xylanases from Srrepromyces cyaneus: Their production, purification, and characterization
    • Wang P, Mason JC, Broda P (1993). Xylanases from Srrepromyces cyaneus: Their production, purification, and characterization. J. Gen. Microbial. 139: 1987-1993.
    • (1993) J. Gen. Microbial , vol.139 , pp. 1987-1993
    • Wang, P.1    Mason, J.C.2    Broda, P.3
  • 41
    • 0024087074 scopus 로고
    • Multiplicity of β-1,4-xylanase in microorganisms: Function and applicants
    • Wong KKY, Tan LUL, Saddler JN (1988). Multiplicity of β-1,4-xylanase in microorganisms: function and applicants. Microbiol. Rev. 52: 305-317.
    • (1988) Microbiol. Rev , vol.52 , pp. 305-317
    • Wong, K.K.Y.1    Tan, L.U.L.2    Saddler, J.N.3
  • 42
    • 45649085057 scopus 로고    scopus 로고
    • Comparative study on application of T. lanuginosus SSBP xylanase and commercial xylanase on biobleaching of non wood pulps
    • Ziaie-Shirkolaee Y, Talebizadeh A, Soltanali S (2008). Comparative study on application of T. lanuginosus SSBP xylanase and commercial xylanase on biobleaching of non wood pulps. Bioresour. Technol. 99: 7433-7437.
    • (2008) Bioresour. Technol , vol.99 , pp. 7433-7437
    • Ziaie-Shirkolaee, Y.1    Talebizadeh, A.2    Soltanali, S.3


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