메뉴 건너뛰기




Volumn 3, Issue 3, 2009, Pages 2770-2777

Characterization of a polygalacturonase from trichoderma harzianum grown on citrus peel with application for apple juice

Author keywords

Apple juice; Mandarin citrus peel; Polygalacturonase; Properties; Purification; Trichoderma harzianum

Indexed keywords


EID: 77952264872     PISSN: 19918178     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (34)
  • 3
    • 0008677041 scopus 로고    scopus 로고
    • Partial purification and characterization of exopolygalacturonase II and III of Penicillium frequentans
    • Barense, R.I., M.A.D.S.C. Chellegatti, M.J.V. Fonseca, S. Said, 2001. Partial purification and characterization of exopolygalacturonase II and III of Penicillium frequentans. Brazilian J. Microbiol., 32: 327-330.
    • (2001) Brazilian J. Microbiol , vol.32 , pp. 327-330
    • Barense, R.I.1    Chellegatti, M.A.D.S.C.2    Fonseca, M.J.V.3    Said, S.4
  • 4
    • 78651031122 scopus 로고
    • Enzymes of starch degradation and synthesis
    • Bernfeld, P., 1951. Enzymes of starch degradation and synthesis. Adv. Enzymol., 12: 379-428.
    • (1951) Adv. Enzymol , vol.12 , pp. 379-428
    • Bernfeld, P.1
  • 5
    • 33746533208 scopus 로고    scopus 로고
    • Studies on kinetics and thermostability of a novel acid invertase from Fusarium solani
    • Bhatti, H.N., M. Asgher, A. Abbas, R. Nawaz, M.A. Sheikh, 2006. Studies on kinetics and thermostability of a novel acid invertase from Fusarium solani. J. Agricult. Food Chem., 54: 4617-4623.
    • (2006) J. Agricult. Food Chem , vol.54 , pp. 4617-4623
    • Bhatti, H.N.1    Asgher, M.2    Abbas, A.3    Nawaz, R.4    Sheikh, M.A.5
  • 6
    • 0017184389 scopus 로고
    • A rapid sensitive method of quantitation micro gram quantities of proteins utilizing the principles of protein-dye binding
    • Bradford, M.M., 1976. A rapid sensitive method of quantitation micro gram quantities of proteins utilizing the principles of protein-dye binding. Anal. Biochem., 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 1942424126 scopus 로고    scopus 로고
    • Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii
    • Contreras-Esquivel, J.C., C.E. Voget, 2004. Purification and partial characterization of an acidic polygalacturonase from Aspergillus kawachii. J. Biotechnol., 110: 21-28.
    • (2004) J. Biotechnol , vol.110 , pp. 21-28
    • Contreras-Esquivel, J.C.1    Voget, C.E.2
  • 9
    • 0030044882 scopus 로고    scopus 로고
    • Fractionation, purification, and preliminary characterization of polygalacturonases produced by Aspergillus carbonarius. Enzyme Microb
    • Devi, N.A., A.G. Appu Rao, 1996. Fractionation, purification, and preliminary characterization of polygalacturonases produced by Aspergillus carbonarius. Enzyme Microb. Technol., 18: 59-65.
    • (1996) Technol , vol.18 , pp. 59-65
    • Devi, N.A.1    Appu Rao, A.G.2
  • 11
    • 84981835608 scopus 로고
    • Purification de l'invertase de levure
    • Fischer, E.H., I. Kohtes, 1951. Purification de l'invertase de levure. Helvetica Chimical Acta, 34: 1123-1131.
    • (1951) Helvetica Chimical Acta , vol.34 , pp. 1123-1131
    • Fischer, E.H.1    Kohtes, I.2
  • 12
    • 0000086821 scopus 로고
    • Pectic enzymes
    • In: Fogarty W.M. (ed.), Applied Science Publishers, London
    • Fogarty, W.M., C.T. Kelly, 1983. Pectic enzymes, In: Fogarty W.M. (ed.) Microbial Enzymes and Biotechnology, Applied Science Publishers, London, 131-182.
    • (1983) Microbial Enzymes and Biotechnology , pp. 131-182
    • Fogarty, W.M.1    Kelly, C.T.2
  • 13
    • 0347297442 scopus 로고    scopus 로고
    • Purification, characterization and mode of action of an endo-polygalacturonase from the psychrophilic fungus Mucor flavus
    • Gadre, R.V., G. VanDriessche, J. Van Beeumen, Bhat, M.K., 2003: Purification, characterization and mode of action of an endo-polygalacturonase from the psychrophilic fungus Mucor flavus. Enzyme Microb. Technol., 32: 321-330.
    • (2003) Enzyme Microb. Technol , vol.32 , pp. 321-330
    • Gadre, R.V.1    Vandriessche, G.2    van Beeumen, J.3    Bhat, M.K.4
  • 14
    • 0028103131 scopus 로고
    • Characterization of an endopolygalacturonase produced by the chestnut blight fungus (Cryphonectria parasitica)
    • Gao, S., L. Shain, 1994. Characterization of an endopolygalacturonase produced by the chestnut blight fungus (Cryphonectria parasitica). Physiol. Molec. Plant Pathol., 45:169-179.
    • (1994) Physiol. Molec. Plant Pathol , vol.45 , pp. 169-179
    • Gao, S.1    Shain, L.2
  • 15
    • 0023844678 scopus 로고
    • Apple pomace as crude material for pectinase production from apple pomace in solid state cultures
    • Hours, R.A., C.E. Voget, R.J. Ertola, 1988. Apple pomace as crude material for pectinase production from apple pomace in solid state cultures. Biol. Wastes., 24: 147-157.
    • (1988) Biol. Wastes , vol.24 , pp. 147-157
    • Hours, R.A.1    Voget, C.E.2    Ertola, R.J.3
  • 16
    • 0035858606 scopus 로고    scopus 로고
    • Inhibition of polygalacturonase from Verticillium dahliae by a polygalacturonase inhibiting protein from cotton
    • James, J.T., I.A. Dubery, 2001. Inhibition of polygalacturonase from Verticillium dahliae by a polygalacturonase inhibiting protein from cotton. Phytochem., 57: 149-156.
    • (2001) Phytochem , vol.57 , pp. 149-156
    • James, J.T.1    Dubery, I.A.2
  • 17
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: A review
    • Jayani, R.S., S. Saxena, R. Gupta, 2005. Microbial pectinolytic enzymes: A review. Process Biochem., 40: 2931-2944.
    • (2005) Process Biochem , vol.40 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 18
    • 2942615497 scopus 로고    scopus 로고
    • Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile Apinis
    • Kaur, G., S. Kumar, T. Satyanarayana, 2004. Production, characterization and application of a thermostable polygalacturonase of a thermophilic mould Sporotrichum thermophile Apinis. Bioresour. Technol., 94: 239-243.
    • (2004) Bioresour. Technol , vol.94 , pp. 239-243
    • Kaur, G.1    Kumar, S.2    Satyanarayana, T.3
  • 19
    • 0035811977 scopus 로고    scopus 로고
    • Purification and properties of a high-molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus
    • Kobayashi, T., N. Higaki, A. Suzumatsu, K. Sawada, H. Hagihara, S. Kawai, S. Ito, 2001. Purification and properties of a high-molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus. Enzyme Microb. Technol., 29: 70-75.
    • (2001) Enzyme Microb. Technol , vol.29 , pp. 70-75
    • Kobayashi, T.1    Higaki, N.2    Suzumatsu, A.3    Sawada, K.4    Hagihara, H.5    Kawai, S.6    Ito, S.7
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K., 1970. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 19944386289 scopus 로고    scopus 로고
    • Influence of medium composition and pH on the production of polygalacturonases by Aspergillus oryzae
    • Malvessi, E., M.M. da Silveira, 2004. Influence of medium composition and pH on the production of polygalacturonases by Aspergillus oryzae. Brazilian Arch. Biol. Technol., 47: 693-702.
    • (2004) Brazilian Arch. Biol. Technol , vol.47 , pp. 693-702
    • Malvessi, E.1    da Silveira, M.M.2
  • 22
    • 38849119917 scopus 로고    scopus 로고
    • Fungal multienzyme production on industrial by- products of citrus-processing industry
    • Mamma, D., E. Kourtoglou, P. Christakopoulos, 2008. Fungal multienzyme production on industrial by- products of citrus-processing industry. Bioresour. Technol., 99: 2373-2383.
    • (2008) Bioresour. Technol , vol.99 , pp. 2373-2383
    • Mamma, D.1    Kourtoglou, E.2    Christakopoulos, P.3
  • 23
    • 69549090671 scopus 로고    scopus 로고
    • Partial purification and characterization of five α- amylases from a wheat local variety (Balady) during germination
    • (In press)
    • Mohamed, S.A., A.L. Al-Malki, T.A. Kumosani, 2009. Partial purification and characterization of five α- amylases from a wheat local variety (Balady) during germination. Austr. J. Basic Appl. Sci. (In press).
    • (2009) Austr. J. Basic Appl. Sci
    • Mohamed, S.A.1    Al-Malki, A.L.2    Kumosani, T.A.3
  • 24
    • 0037436551 scopus 로고    scopus 로고
    • New polygalactourinases from Trichoderma reesi: Characterization and their specificities to partially methylated and acetylated pectins
    • Mohamed, S.A., T.M.I.E. Christensin, J.D. Mikkelsen, 2003. New polygalactourinases from Trichoderma reesi: characterization and their specificities to partially methylated and acetylated pectins. Carbohydr. Res., 338: 515-524.
    • (2003) Carbohydr. Res , vol.338 , pp. 515-524
    • Mohamed, S.A.1    Christensin, T.M.I.E.2    Mikkelsen, J.D.3
  • 25
    • 33846253685 scopus 로고    scopus 로고
    • Biochemical characterization of an extracellular polygalacturonase from Trichoderma harzianum
    • Mohamed, S.A., N.M. Farid, E.N. Hossiny, R.I. Bassuiny, 2006. Biochemical characterization of an extracellular polygalacturonase from Trichoderma harzianum. J. Biotechnol., 127: 54-64.
    • (2006) J. Biotechnol , vol.127 , pp. 54-64
    • Mohamed, S.A.1    Farid, N.M.2    Hossiny, E.N.3    Bassuiny, R.I.4
  • 26
    • 0141975334 scopus 로고    scopus 로고
    • Optimizing the growth conditions for the pectinolytic activity of Kluyveromyces wickerhamii by using response surface methodology
    • Moyo, S., B.A. Gashe, E.K. Collison, S.I. Mpuchane, 2003. Optimizing the growth conditions for the pectinolytic activity of Kluyveromyces wickerhamii by using response surface methodology. J. Food Microbiol., 85: 87-100.
    • (2003) J. Food Microbiol , vol.85 , pp. 87-100
    • Moyo, S.1    Gashe, B.A.2    Collison, E.K.3    Mpuchane, S.I.4
  • 27
    • 4143141031 scopus 로고    scopus 로고
    • Purification and biochemical characterization of polygalacturoase II produced in semi-solid medium by a strain of Fusarium moniliforme
    • Niture, S.K., A. Pant, 2004. Purification and biochemical characterization of polygalacturoase II produced in semi-solid medium by a strain of Fusarium moniliforme. Microbiol. Res., 159: 305-314.
    • (2004) Microbiol. Res , vol.159 , pp. 305-314
    • Niture, S.K.1    Pant, A.2
  • 28
    • 3042825076 scopus 로고    scopus 로고
    • Kinetic properties and thermal behavior of polygalacturonase used in fruit juice clarification
    • Ortega, N., S. de Diego, M. Perez-Mateos, M.D. Busto, 2004. Kinetic properties and thermal behavior of polygalacturonase used in fruit juice clarification. Food Chem., 88: 209-217.
    • (2004) Food Chem , vol.88 , pp. 209-217
    • Ortega, N.1    de Diego, S.2    Perez-Mateos, M.3    Busto, M.D.4
  • 30
    • 26844506443 scopus 로고    scopus 로고
    • In vitro biocontrol activity of Trichoderma harzianum on Alternaria alternate in the presence of growth regulators
    • Roco, A., L.M. Pérez, 2001. In vitro biocontrol activity of Trichoderma harzianum on Alternaria alternate in the presence of growth regulators. J. Biotechnol., 4: 68-73.
    • (2001) J. Biotechnol , vol.4 , pp. 68-73
    • Roco, A.1    Pérez, L.M.2
  • 31
    • 2442446299 scopus 로고    scopus 로고
    • Purification of the extracellular pectinolytic enzyme from the fungus Rhizopus oryzae NBRC 4707
    • Saito, K., N. Takakuwa, Y. Oda, 2004. Purification of the extracellular pectinolytic enzyme from the fungus Rhizopus oryzae NBRC 4707. Microbiol. Res., 159: 83-86.
    • (2004) Microbiol. Res , vol.159 , pp. 83-86
    • Saito, K.1    Takakuwa, N.2    Oda, Y.3
  • 32
    • 0037104627 scopus 로고    scopus 로고
    • Purification and characterisation of two exopolygalacturonases from Aspergillus niger able to degrade xylogalacturonan and acetylated homogalacturonan
    • Sakamoto, T., E. Bonnin, B. Quemener, J.F. Thibault, 2002. Purification and characterisation of two exopolygalacturonases from Aspergillus niger able to degrade xylogalacturonan and acetylated homogalacturonan. Biochim. Biophys. Acta, 1572: 10-18.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 10-18
    • Sakamoto, T.1    Bonnin, E.2    Quemener, B.3    Thibault, J.F.4
  • 33
    • 46949092740 scopus 로고    scopus 로고
    • Biochemical and thermal characterization of crude exopolygalacturonae produced by Aspergillus sojae
    • Tari, C., N. Dogan, N. Gogus, 2008. Biochemical and thermal characterization of crude exopolygalacturonae produced by Aspergillus sojae. Food Chem., 111: 824-829.
    • (2008) Food Chem , vol.111 , pp. 824-829
    • Tari, C.1    Dogan, N.2    Gogus, N.3
  • 34
    • 0345567608 scopus 로고    scopus 로고
    • Carbon sources effect on pectinase production from Aspergillus japonicus 586. Brazilian
    • Teixeira, M.F.S., Lima J.L. Filho, N. Duran, 2000. Carbon sources effect on pectinase production from Aspergillus japonicus 586. Brazilian J. Microbiol., 31: 286-290.
    • (2000) J. Microbiol , vol.31 , pp. 286-290
    • Teixeira, M.F.S.1    Filho Lima, J.L.2    Duran, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.