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Volumn 30, Issue 2, 2006, Pages 130-137

Optimization of chemical and physical parameters affecting the activity of pectin lyase and pectate lyase from Debaryomyces nepalensis: A statistical approach

Author keywords

Central composite design; Chemical parameters; Pectate lyase; Pectin; Pectin lyase; Physical parameters; Polygalacturonic acid; Response surface methodology; Transelimination reaction

Indexed keywords

CARBON; OPTIMIZATION; PH EFFECTS; REACTION KINETICS; STATISTICAL METHODS;

EID: 33745271337     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2006.02.014     Document Type: Article
Times cited : (25)

References (25)
  • 1
    • 0041990500 scopus 로고
    • Microbial pectolytic enzymes
    • Fogarty W.M., and Kelly C.T. (Eds), Elsevier, London
    • Whitaker J.R. Microbial pectolytic enzymes. In: Fogarty W.M., and Kelly C.T. (Eds). Microbial Enzymes and Biotechnology (1991), Elsevier, London 133-176
    • (1991) Microbial Enzymes and Biotechnology , pp. 133-176
    • Whitaker, J.R.1
  • 2
    • 0037899941 scopus 로고    scopus 로고
    • Purification and biochemical properties of microbial pectinases: a review
    • Gummadi S.N., and Panda T. Purification and biochemical properties of microbial pectinases: a review. Proc. Biochem. 38 (2003) 987-996
    • (2003) Proc. Biochem. , vol.38 , pp. 987-996
    • Gummadi, S.N.1    Panda, T.2
  • 3
    • 0035191237 scopus 로고    scopus 로고
    • Applications of pectinases in the commercial sector: a review
    • Kashyap D.R., Vohra P.K., Chopra S., and Tewari R. Applications of pectinases in the commercial sector: a review. Bioresour. Technol. 77 (2001) 215-227
    • (2001) Bioresour. Technol. , vol.77 , pp. 215-227
    • Kashyap, D.R.1    Vohra, P.K.2    Chopra, S.3    Tewari, R.4
  • 4
    • 85047679885 scopus 로고    scopus 로고
    • Production of pectolytic enzymes: a review
    • Naidu G.S.N., and Panda T. Production of pectolytic enzymes: a review. Bioproc. Eng. 19 (1998) 355-361
    • (1998) Bioproc. Eng. , vol.19 , pp. 355-361
    • Naidu, G.S.N.1    Panda, T.2
  • 5
    • 0021522222 scopus 로고
    • Application of cellulase and pectinases from fungal origin for the liquefaction and sachharification of biomass
    • Beldman G., Rombouts F.M., Voragen A.G.J., and Pilnik W. Application of cellulase and pectinases from fungal origin for the liquefaction and sachharification of biomass. Enzyme Microbial. Technol. 6 (1984) 503-507
    • (1984) Enzyme Microbial. Technol. , vol.6 , pp. 503-507
    • Beldman, G.1    Rombouts, F.M.2    Voragen, A.G.J.3    Pilnik, W.4
  • 6
    • 0028319223 scopus 로고
    • Pectolytic enzymes from Actinomycetes for the degumming of ramie bast fibres
    • Bruhlmann F., Kim K.S., Zimmerman W., and Fiechter A. Pectolytic enzymes from Actinomycetes for the degumming of ramie bast fibres. Appl. Environ. Microbiol. 60 (1994) 2107-2112
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2107-2112
    • Bruhlmann, F.1    Kim, K.S.2    Zimmerman, W.3    Fiechter, A.4
  • 8
    • 21144449971 scopus 로고    scopus 로고
    • Microbial pectic transeliminases
    • Gummadi S.N., and Kumar D.S. Microbial pectic transeliminases. Biotechnol. Lett. 27 (2005) 451-458
    • (2005) Biotechnol. Lett. , vol.27 , pp. 451-458
    • Gummadi, S.N.1    Kumar, D.S.2
  • 11
    • 14944351939 scopus 로고    scopus 로고
    • Pectinolytic systems of two aerobic sporogenous bacterial strains with high activity on pectin
    • Soriano M., Diaz P., and Pastor F.I.J. Pectinolytic systems of two aerobic sporogenous bacterial strains with high activity on pectin. Curr. Microbiol. 50 (2005) 114-118
    • (2005) Curr. Microbiol. , vol.50 , pp. 114-118
    • Soriano, M.1    Diaz, P.2    Pastor, F.I.J.3
  • 12
    • 0025118070 scopus 로고
    • Production of pectolytic enzymes by Aspergillus niger: effect of inoculum size and potassium hexacyanoferrate II-trihydrate
    • Friedrich J., Cimermann A., and Steiner W. Production of pectolytic enzymes by Aspergillus niger: effect of inoculum size and potassium hexacyanoferrate II-trihydrate. Appl. Microbiol. Biotechnol. 33 (1990) 377-381
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 377-381
    • Friedrich, J.1    Cimermann, A.2    Steiner, W.3
  • 13
    • 0030855808 scopus 로고    scopus 로고
    • Biochemical characterization of pectate lyase produced by fluorescent Pseudomonads associated with spoilage of fruits and vegetables
    • Liao C.H., Sullivan J., Grady J., and Wong L.C. Biochemical characterization of pectate lyase produced by fluorescent Pseudomonads associated with spoilage of fruits and vegetables. J. Appl. Microbiol. 83 (1997) 10-16
    • (1997) J. Appl. Microbiol. , vol.83 , pp. 10-16
    • Liao, C.H.1    Sullivan, J.2    Grady, J.3    Wong, L.C.4
  • 14
    • 85047678867 scopus 로고    scopus 로고
    • Parameters optimization of chitin hydrolysis by Trichoderma harzianum chitinase under assay conditions
    • Kapat A., Rakshit S.K., and Panda T. Parameters optimization of chitin hydrolysis by Trichoderma harzianum chitinase under assay conditions. Bioproc. Eng. 14 (1996) 275-279
    • (1996) Bioproc. Eng. , vol.14 , pp. 275-279
    • Kapat, A.1    Rakshit, S.K.2    Panda, T.3
  • 15
    • 14644413617 scopus 로고    scopus 로고
    • Hydrolysis of starch by amylase from Bacillus sp. KCA102: a statistical approach
    • Agrawal M., Pradeep S., Chandraraj K., and Gummadi S.N. Hydrolysis of starch by amylase from Bacillus sp. KCA102: a statistical approach. Proc. Biochem. 40 (2005) 2499-2507
    • (2005) Proc. Biochem. , vol.40 , pp. 2499-2507
    • Agrawal, M.1    Pradeep, S.2    Chandraraj, K.3    Gummadi, S.N.4
  • 16
    • 0033054494 scopus 로고    scopus 로고
    • Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: a statistical approach
    • Naidu G.S.N., and Panda T. Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: a statistical approach. Enzyme Microbial. Technol. 25 (1999) 116-124
    • (1999) Enzyme Microbial. Technol. , vol.25 , pp. 116-124
    • Naidu, G.S.N.1    Panda, T.2
  • 17
    • 77957002524 scopus 로고
    • Pectin lyase from fungi
    • Albersheim P. Pectin lyase from fungi. Methods Enzymol. 8 (1966) 628-631
    • (1966) Methods Enzymol. , vol.8 , pp. 628-631
    • Albersheim, P.1
  • 20
    • 0000532112 scopus 로고
    • Multi-factor experimental designs for exploring response surfaces
    • Box G.E.P., and Hunter J.S. Multi-factor experimental designs for exploring response surfaces. Ann. Math. Stat. 28 (1957) 195-241
    • (1957) Ann. Math. Stat. , vol.28 , pp. 195-241
    • Box, G.E.P.1    Hunter, J.S.2
  • 21
    • 0009481843 scopus 로고
    • On the experimental designs for exploring response surfaces
    • Box G.E.P., and Wilson K.B. On the experimental designs for exploring response surfaces. Ann. Math. Stat. 13 (1951) 1-45
    • (1951) Ann. Math. Stat. , vol.13 , pp. 1-45
    • Box, G.E.P.1    Wilson, K.B.2
  • 24
    • 0021962644 scopus 로고
    • Location and characteristics of enzymes involved in the breakdown of polygalacturonic acid by Bacteroides thetaiotaomicron
    • McCarthy R.E., Kotarski S.F., and Salyers A.A. Location and characteristics of enzymes involved in the breakdown of polygalacturonic acid by Bacteroides thetaiotaomicron. J. Bacteriol. 161 (1985) 493-499
    • (1985) J. Bacteriol. , vol.161 , pp. 493-499
    • McCarthy, R.E.1    Kotarski, S.F.2    Salyers, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.