메뉴 건너뛰기




Volumn 11, Issue 6, 2011, Pages 607-614

Aspergillus niger exo-inulinase purification by three phase partitioning

Author keywords

Aspergillus; Inulinase; PH; Temperature; Three phase partitioning

Indexed keywords

AMMONIUM SULFATE; ASPERGILLUS NIGER; BENEFIT/COST RATIOS; CRUDE EXTRACT; DOWNSTREAM PROCESS; ENZYME PURIFICATION; INULINASE; OPTIMUM CONDITIONS; PURIFICATION TECHNIQUES; SDS-PAGE ANALYSIS; T-BUTANOL; TECHNICAL VIABILITY; THREE-PHASE PARTITIONING;

EID: 83755225640     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.201000180     Document Type: Article
Times cited : (24)

References (39)
  • 2
    • 0036085307 scopus 로고    scopus 로고
    • Technological functionality of inulin and oligofructose
    • Franck, A., Technological functionality of inulin and oligofructose. Brit. J. Nutr. 2002, 87, 287-291.
    • (2002) Brit. J. Nutr. , vol.87 , pp. 287-291
    • Franck, A.1
  • 3
    • 0021392580 scopus 로고
    • Production and properties of Aspergillus niger inulinase
    • Derycke, D. G., Vandamme, E. J., Production and properties of Aspergillus niger inulinase. J. Chem. Tech. Biotechnol. 1984, 34, 45-51.
    • (1984) J. Chem. Tech. Biotechnol. , vol.34 , pp. 45-51
    • Derycke, D.G.1    Vandamme, E.J.2
  • 4
    • 0032846870 scopus 로고    scopus 로고
    • Recent developments in microbial inulinases: its production, properties and industrial applications
    • Pandey, A., Soccol, C. R., Selvakumar, P., Soccol, V. T. et al., Recent developments in microbial inulinases: its production, properties and industrial applications. Appl. Biochem. Biotechnol. 1999, 81, 35-52.
    • (1999) Appl. Biochem. Biotechnol. , vol.81 , pp. 35-52
    • Pandey, A.1    Soccol, C.R.2    Selvakumar, P.3    Soccol, V.T.4
  • 6
    • 59449083826 scopus 로고    scopus 로고
    • Inulinase-expressing microorganisms and applications of inulinases
    • Chi, Z., Chi, Z., Zhang, T., Liu, G., Yue, L., Inulinase-expressing microorganisms and applications of inulinases. Appl. Microbiol. Biotechnol. 2009, 82, 211-220.
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 211-220
    • Chi, Z.1    Chi, Z.2    Zhang, T.3    Liu, G.4    Yue, L.5
  • 7
    • 34548562485 scopus 로고    scopus 로고
    • The state of the art in the production of fructose from inulin enzymatic hydrolysis
    • Ricca, E., Calabrò, V., Curcio, S., Iorio, G., The state of the art in the production of fructose from inulin enzymatic hydrolysis. Crit. Rev. Biotechnol. 2007, 27, 129-145.
    • (2007) Crit. Rev. Biotechnol. , vol.27 , pp. 129-145
    • Ricca, E.1    Calabrò, V.2    Curcio, S.3    Iorio, G.4
  • 8
    • 34548557545 scopus 로고    scopus 로고
    • Production of high fructose syrup from Asparagus inulin using immobilized exoinulinase from Kluyveromyces marxianus YS-1
    • Singh, R. S., Dhaliwal, R., Puri, M., Production of high fructose syrup from Asparagus inulin using immobilized exoinulinase from Kluyveromyces marxianus YS-1. J. Ind. Microbiol. Biotechnol. 2007, 34, 649-655.
    • (2007) J. Ind. Microbiol. Biotechnol. , vol.34 , pp. 649-655
    • Singh, R.S.1    Dhaliwal, R.2    Puri, M.3
  • 9
    • 56849097325 scopus 로고    scopus 로고
    • Purification and characterization of extracellular inulinase from a marine yeast Pichia guilliermondii and inulin hydrolysis by the purified inulinase
    • Gong, F., Zhang, T., Chi, Z. M., Sheng, J. et al., Purification and characterization of extracellular inulinase from a marine yeast Pichia guilliermondii and inulin hydrolysis by the purified inulinase. Biotech. Bioproc. Bioeng. 2008, 13, 511-517.
    • (2008) Biotech. Bioproc. Bioeng. , vol.13 , pp. 511-517
    • Gong, F.1    Zhang, T.2    Chi, Z.M.3    Sheng, J.4
  • 10
    • 33745201646 scopus 로고    scopus 로고
    • Inulinase production using garlic (Allium sativum) powder as potential substrate in Streptomyces sp
    • Sharma, A. D., Kainth, S., Gill, P. K., Inulinase production using garlic (Allium sativum) powder as potential substrate in Streptomyces sp. J. Food Eng. 2006, 77, 486-491.
    • (2006) J. Food Eng. , vol.77 , pp. 486-491
    • Sharma, A.D.1    Kainth, S.2    Gill, P.K.3
  • 11
    • 31844441344 scopus 로고    scopus 로고
    • Design and characterization of an enzyme system for inulin hydrolysis
    • Rocha, J. R., Catana, R., Ferreira, B. S., Cabral, J. M. S., Fenandes, P., Design and characterization of an enzyme system for inulin hydrolysis. Food Chem. 2006, 95, 77-82.
    • (2006) Food Chem. , vol.95 , pp. 77-82
    • Rocha, J.R.1    Catana, R.2    Ferreira, B.S.3    Cabral, J.M.S.4    Fenandes, P.5
  • 12
    • 23744514161 scopus 로고    scopus 로고
    • Adsorption of the inulinase from Kluyveromyces marxianus NRRL Y-7571 on Streamline DEAE resin
    • Makino, Y., Lima, P. S. C., Filho, F. M., Rodrigues, M. I., Adsorption of the inulinase from Kluyveromyces marxianus NRRL Y-7571 on Streamline DEAE resin. Braz. J. Chem. Eng. 2005, 22, 539-545.
    • (2005) Braz. J. Chem. Eng. , vol.22 , pp. 539-545
    • Makino, Y.1    Lima, P.S.C.2    Filho, F.M.3    Rodrigues, M.I.4
  • 13
    • 67349160166 scopus 로고    scopus 로고
    • Technical viability of the production, partial purification and characterisation of inulinase using pretreated agroindustrial residues
    • Treichel, H., Mazutti, M. A., Filho, F. M., Rodrigues, M. I., Technical viability of the production, partial purification and characterisation of inulinase using pretreated agroindustrial residues. Bioprocess Biosyst. Eng. 2009, 32, 425-433.
    • (2009) Bioprocess Biosyst. Eng. , vol.32 , pp. 425-433
    • Treichel, H.1    Mazutti, M.A.2    Filho, F.M.3    Rodrigues, M.I.4
  • 14
    • 0031459396 scopus 로고    scopus 로고
    • Production, purification and properties of an endo-inulinase from Penicillium sp. TN-88
    • Nakamura, T., Shitara, A., Matsuda, S., Matsuo, T. et al., Production, purification and properties of an endo-inulinase from Penicillium sp. TN-88. J. Ferment. Bioeng. 1997, 84, 313-318.
    • (1997) J. Ferment. Bioeng. , vol.84 , pp. 313-318
    • Nakamura, T.1    Shitara, A.2    Matsuda, S.3    Matsuo, T.4
  • 15
    • 44649107069 scopus 로고    scopus 로고
    • Purification and characterization of extracellular inulinase from a marine yeast Cryptococcus aureus G7a and inulin hydrolysis by the purified inulinase
    • Sheng, J., Chi, Z. M., Gong, F., Li, J., Purification and characterization of extracellular inulinase from a marine yeast Cryptococcus aureus G7a and inulin hydrolysis by the purified inulinase. Appl. Biochem. Biotechnol. 2008, 144, 111-121.
    • (2008) Appl. Biochem. Biotechnol. , vol.144 , pp. 111-121
    • Sheng, J.1    Chi, Z.M.2    Gong, F.3    Li, J.4
  • 16
    • 0033754941 scopus 로고    scopus 로고
    • Production, purification and characterization of an extracellular inulinase from Kluyveromyces marxianus var. Bulgaricus
    • Kushi, R. T., Monti, R., Contiero, J., Production, purification and characterization of an extracellular inulinase from Kluyveromyces marxianus var. Bulgaricus. J. Ind. Microbiol. Biotechnol. 2000, 25, 63-69.
    • (2000) J. Ind. Microbiol. Biotechnol. , vol.25 , pp. 63-69
    • Kushi, R.T.1    Monti, R.2    Contiero, J.3
  • 17
    • 63049113629 scopus 로고    scopus 로고
    • Purification and characterisation of exo- and endo-inulinase from Aspergillus ficuum JNSP5-06
    • Chen, H. Q., Chen, X. M., Li, Y., Wang, J. et al., Purification and characterisation of exo- and endo-inulinase from Aspergillus ficuum JNSP5-06. Food Chem. 2009, 115, 1206-1212.
    • (2009) Food Chem. , vol.115 , pp. 1206-1212
    • Chen, H.Q.1    Chen, X.M.2    Li, Y.3    Wang, J.4
  • 18
    • 0031281935 scopus 로고    scopus 로고
    • Three phase partitioning: concentration and purification of proteins
    • Dennison, C., Lovrien, R., Three phase partitioning: concentration and purification of proteins. Protein Expr. Purif. 1997, 11, 149-161.
    • (1997) Protein Expr. Purif. , vol.11 , pp. 149-161
    • Dennison, C.1    Lovrien, R.2
  • 19
    • 77952322892 scopus 로고    scopus 로고
    • Three-phase partitioning of protease from Calotropis procera latex
    • Rawdkuena, S., Chaiwut, P., Pintathong, P., Benjakulc, S., Three-phase partitioning of protease from Calotropis procera latex. Biochem. Eng. J. 2010, 50, 145-149.
    • (2010) Biochem. Eng. J. , vol.50 , pp. 145-149
    • Rawdkuena, S.1    Chaiwut, P.2    Pintathong, P.3    Benjakulc, S.4
  • 21
    • 57649149329 scopus 로고    scopus 로고
    • Three-phase partitioning of a-galactosidase from fermented media of Aspergillus oryzae and comparison with conventional purification techniques
    • Dhananjay, S. K., Mulimani, V. H., Three-phase partitioning of a-galactosidase from fermented media of Aspergillus oryzae and comparison with conventional purification techniques. J. Ind. Microbiol. Biotechnol. 2009, 36, 123-128.
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 123-128
    • Dhananjay, S.K.1    Mulimani, V.H.2
  • 22
    • 79960866839 scopus 로고    scopus 로고
    • Application of Response Surface Methodology to Optimize Three Phase Partitioning for Purification of Laccase from Pleurotus Ostreatus
    • Kumar, V. V., Sathyaselvabala, V., Kirupha, S. D., Murugesan, A. et al., Application of Response Surface Methodology to Optimize Three Phase Partitioning for Purification of Laccase from Pleurotus Ostreatus. Sep. Sci. Technol. 2011, 46, pp. 1922-1930.
    • (2011) Sep. Sci. Technol. , vol.46 , pp. 1922-1930
    • Kumar, V.V.1    Sathyaselvabala, V.2    Kirupha, S.D.3    Murugesan, A.4
  • 23
    • 0033775993 scopus 로고    scopus 로고
    • Purification of alkaline phosphatase from chicken intestine by three-phase partitioning and use of phenyl-Sepharose 6B in the batch mode
    • Sharma, A., Sharma, S., Gupta, M. N., Purification of alkaline phosphatase from chicken intestine by three-phase partitioning and use of phenyl-Sepharose 6B in the batch mode. Biosepartion 2000, 9, 155-161.
    • (2000) Biosepartion , vol.9 , pp. 155-161
    • Sharma, A.1    Sharma, S.2    Gupta, M.N.3
  • 24
    • 0035717688 scopus 로고    scopus 로고
    • Purification of phospholipase D from Dacus carota by three-phase partitioning and its characterization
    • Sharma, S., Gupta, M. N., Purification of phospholipase D from Dacus carota by three-phase partitioning and its characterization. Protein Expres. Purif. 2001, 21, 310-316.
    • (2001) Protein Expres. Purif. , vol.21 , pp. 310-316
    • Sharma, S.1    Gupta, M.N.2
  • 25
    • 58149199032 scopus 로고    scopus 로고
    • Extraction and purification of Ipomoea peroxidase employing three-phase partitioning
    • Narayan, A. V., Madhusudhan, M. C., Raghavarao, K. S. M. S., Extraction and purification of Ipomoea peroxidase employing three-phase partitioning. Appl. Biochem. Biotechnol. 2008, 151, 263-272.
    • (2008) Appl. Biochem. Biotechnol. , vol.151 , pp. 263-272
    • Narayan, A.V.1    Madhusudhan, M.C.2    Raghavarao, K.S.M.S.3
  • 26
    • 43049136627 scopus 로고    scopus 로고
    • Characterization of three-phase partitioned exo polygalacturonase from Aspergillus sojae with unique properties
    • Dogan, N., Tari, C., Characterization of three-phase partitioned exo polygalacturonase from Aspergillus sojae with unique properties. Biochem. Eng. J. 2008, 39, 43-50.
    • (2008) Biochem. Eng. J. , vol.39 , pp. 43-50
    • Dogan, N.1    Tari, C.2
  • 27
    • 79952703035 scopus 로고    scopus 로고
    • Induction and purification by three-phase partitioning of aryl alcohol oxidase (AAO) from Pleurotus ostreatus
    • Kumar, V. V., Rapheal, V. S., Induction and purification by three-phase partitioning of aryl alcohol oxidase (AAO) from Pleurotus ostreatus. Appl. Biochem. Biotechnol. 2010, 163, 423-432.
    • (2010) Appl. Biochem. Biotechnol. , vol.163 , pp. 423-432
    • Kumar, V.V.1    Rapheal, V.S.2
  • 28
    • 33847300062 scopus 로고    scopus 로고
    • Three phase partitioning as a novel method for purification of ragi (Eleusine coracana) bifunctional amylase/protease inhibitor
    • Saxena, L., Iyer, B. K., Ananthanarayan, L., Three phase partitioning as a novel method for purification of ragi (Eleusine coracana) bifunctional amylase/protease inhibitor. Process Biochem. 2007, 42, 491-495.
    • (2007) Process Biochem. , vol.42 , pp. 491-495
    • Saxena, L.1    Iyer, B.K.2    Ananthanarayan, L.3
  • 29
    • 77952242120 scopus 로고    scopus 로고
    • Three-phase partitioning as a rapid and efficient method for purification of invertase from tomato
    • Ozer, B., Akardere, E., Celem, E. B., Onal, S., Three-phase partitioning as a rapid and efficient method for purification of invertase from tomato. Biochem. Eng. J. 2010, 50, 110-115.
    • (2010) Biochem. Eng. J. , vol.50 , pp. 110-115
    • Ozer, B.1    Akardere, E.2    Celem, E.B.3    Onal, S.4
  • 30
    • 33747333106 scopus 로고
    • Use of Dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L., Use of Dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31, 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, 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
    • Laemmli, U.K.1
  • 34
    • 83755200607 scopus 로고    scopus 로고
    • Sadasivam, S., Manickam, A. (Ed.), New Age International (p) Limited
    • Sadasivam, S., Manickam, A. (Ed.), Biochemical Methods, New Age International (p) Limited, 2004, 246-250.
    • (2004) Biochemical Methods , pp. 246-250
  • 35
    • 33645278952 scopus 로고    scopus 로고
    • Purification and properties of extracellular endoinulinase from Aspergillus niger 20 OSM
    • Skowronek, M., Fiedurek, J., Purification and properties of extracellular endoinulinase from Aspergillus niger 20 OSM. Food Technol. Biotechnol. 2006, 44, 53-55.
    • (2006) Food Technol. Biotechnol. , vol.44 , pp. 53-55
    • Skowronek, M.1    Fiedurek, J.2
  • 36
    • 24944499709 scopus 로고    scopus 로고
    • Comparative analysis of thermostability of extracellular inulinase activity from Aspergillus fumigatus with commercially available (Novozyme) inulinase
    • Gill, P. K., Manhas, R. K., Singh, P., Comparative analysis of thermostability of extracellular inulinase activity from Aspergillus fumigatus with commercially available (Novozyme) inulinase. Biores. Technol. 2006, 97, 355-358.
    • (2006) Biores. Technol. , vol.97 , pp. 355-358
    • Gill, P.K.1    Manhas, R.K.2    Singh, P.3
  • 37
    • 58349116668 scopus 로고    scopus 로고
    • Inulinase overproduction by a mutant of the marine yeast Pichia guilliermondii using surface response methodology and inulin hydrolysis
    • Yu, X., Guo, N., Chi, Z., Gong, F. et al., Inulinase overproduction by a mutant of the marine yeast Pichia guilliermondii using surface response methodology and inulin hydrolysis. Biochem. Eng. J. 2009, 43, 266-271.
    • (2009) Biochem. Eng. J. , vol.43 , pp. 266-271
    • Yu, X.1    Guo, N.2    Chi, Z.3    Gong, F.4
  • 38
    • 36049047602 scopus 로고    scopus 로고
    • Purification and properties of exo-inulinases from Penicillium janczewskii growing on distinct carbon sources
    • Pessoni, R. A. B., Figueiredo, R., Braga, M. R., Purification and properties of exo-inulinases from Penicillium janczewskii growing on distinct carbon sources. Mycologia 2007, 99, 493-503.
    • (2007) Mycologia , vol.99 , pp. 493-503
    • Pessoni, R.A.B.1    Figueiredo, R.2    Braga, M.R.3
  • 39
    • 0026488501 scopus 로고
    • General properties of extracellular bacterial inulinase
    • Elyachloui, M., Hornez, J. P., Tailllez, R., General properties of extracellular bacterial inulinase. J. Appl. Bacteriol. 1992, 73, 514-519.
    • (1992) J. Appl. Bacteriol. , vol.73 , pp. 514-519
    • Elyachloui, M.1    Hornez, J.P.2    Tailllez, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.