메뉴 건너뛰기




Volumn 99, Issue 4, 2008, Pages 874-881

Batch and fed batch production of pectin lyase and pectate lyase by novel strain Debaryomyces nepalensis in bioreactor

Author keywords

Bioreactor; Debaryomyces nepalensis; Fed batch culture; Pectate lyase; Pectin lyase

Indexed keywords

BIOREACTORS; PARAMETER ESTIMATION; PH EFFECTS; STRAIN;

EID: 36048933009     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2007.01.022     Document Type: Article
Times cited : (27)

References (42)
  • 1
    • 0022778815 scopus 로고
    • Application of fed-batch cultures in the production of extracellular pectinases by Aspergillus sp
    • Aguilar G., and Huitron C. Application of fed-batch cultures in the production of extracellular pectinases by Aspergillus sp. Enzyme Microb. Technol. 8 (1986) 541-545
    • (1986) Enzyme Microb. Technol. , vol.8 , pp. 541-545
    • Aguilar, G.1    Huitron, C.2
  • 3
    • 0025514206 scopus 로고
    • Endopolygalacturonase production from Kluyveromyces marxianus. I. Resolution, purification, and partial characterization of the enzyme
    • Barnby F.M., Morpeth F.F., and Pyle D.L. Endopolygalacturonase production from Kluyveromyces marxianus. I. Resolution, purification, and partial characterization of the enzyme. Enzyme Microb. Technol. 12 (1990) 891-897
    • (1990) Enzyme Microb. Technol. , vol.12 , pp. 891-897
    • Barnby, F.M.1    Morpeth, F.F.2    Pyle, D.L.3
  • 4
    • 0033845456 scopus 로고    scopus 로고
    • Production and characterization of thermostable xylanase and pectinase from a Streptomyces sp. QG-11-3
    • Beg Q.K., Bhushan K., Kapoor M., and Hoondal G.S. Production and characterization of thermostable xylanase and pectinase from a Streptomyces sp. QG-11-3. J. Ind. Microbiol. Biotechnol. 24 (2000) 396-402
    • (2000) J. Ind. Microbiol. Biotechnol. , vol.24 , pp. 396-402
    • Beg, Q.K.1    Bhushan, K.2    Kapoor, M.3    Hoondal, G.S.4
  • 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 Microb. Technol. 6 (1984) 503-507
    • (1984) Enzyme Microb. Technol. , vol.6 , pp. 503-507
    • Beldman, G.1    Rombouts, F.M.2    Voragen, A.G.J.3    Pilnik, W.4
  • 7
    • 0031003024 scopus 로고    scopus 로고
    • Genetic determination of polygalacturonase production in wild type and laboratory strains of Saccharomyces cerevisiae
    • Blanco P., Sieiro C., Reboredo N.M., and Villa T.G. Genetic determination of polygalacturonase production in wild type and laboratory strains of Saccharomyces cerevisiae. Arch. Microbiol. 167 (1997) 284-288
    • (1997) Arch. Microbiol. , vol.167 , pp. 284-288
    • Blanco, P.1    Sieiro, C.2    Reboredo, N.M.3    Villa, T.G.4
  • 8
    • 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
  • 9
    • 6544229829 scopus 로고
    • A study of the conditions and mechanisms of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid
    • Burton K. A study of the conditions and mechanisms of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. J. Biochem. 62 (1956) 315-323
    • (1956) J. Biochem. , vol.62 , pp. 315-323
    • Burton, K.1
  • 10
    • 0024450730 scopus 로고
    • Submerged production of pectolytic enzymes by Aspergillus niger: effect of different aeration/agitation regimes
    • Friedrich J., Cimermenm A., and Steiner W. Submerged production of pectolytic enzymes by Aspergillus niger: effect of different aeration/agitation regimes. Appl. Microbiol. Biotechnol. 31 (1989) 490-494
    • (1989) Appl. Microbiol. Biotechnol. , vol.31 , pp. 490-494
    • Friedrich, J.1    Cimermenm, A.2    Steiner, W.3
  • 11
    • 0027091573 scopus 로고
    • Production of pectolytic enzymes by Aspergillus niger on sucrose
    • Friedrich J., Cimermenm A., and Steiner W. Production of pectolytic enzymes by Aspergillus niger on sucrose. Food Biotechnol. 6 (1992) 207-216
    • (1992) Food Biotechnol. , vol.6 , pp. 207-216
    • Friedrich, J.1    Cimermenm, A.2    Steiner, W.3
  • 12
    • 0028483110 scopus 로고
    • Concomitant biosynthesis of Aspergillus niger pectolytic enzymes and citric acid on sucrose
    • Friedrich J., Cimermenm A., and Steiner W. Concomitant biosynthesis of Aspergillus niger pectolytic enzymes and citric acid on sucrose. Enzyme Microb. Technol. 16 (1994) 703-707
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 703-707
    • Friedrich, J.1    Cimermenm, A.2    Steiner, W.3
  • 13
    • 36048930522 scopus 로고
    • Physiology of polygalacturonases formation by Aspergillus aculeatus and Mucor pusillus
    • Foda M.S., Hussein M.F., Gibriel A.Y., Rizk L.R.S., and Basha S.I. Physiology of polygalacturonases formation by Aspergillus aculeatus and Mucor pusillus. Egypt J. Microbiol. 19 (1984) 181-185
    • (1984) Egypt J. Microbiol. , vol.19 , pp. 181-185
    • Foda, M.S.1    Hussein, M.F.2    Gibriel, A.Y.3    Rizk, L.R.S.4    Basha, S.I.5
  • 14
    • 0344616527 scopus 로고
    • Detection of polygalacturonase, pectin-lyase, and pectin-esterase activities in a Saccharomyces cerevisiae strain
    • Gainvors A., Frezier V., Lemaresquier H., Lequart C., Aigle M., and Belarbi A. Detection of polygalacturonase, pectin-lyase, and pectin-esterase activities in a Saccharomyces cerevisiae strain. Yeast 11 (1994) 1493-1499
    • (1994) Yeast , vol.11 , pp. 1493-1499
    • Gainvors, A.1    Frezier, V.2    Lemaresquier, H.3    Lequart, C.4    Aigle, M.5    Belarbi, A.6
  • 15
    • 0001000535 scopus 로고
    • Studies on the simultaneous production of single cell protein and polygalacturonase from Kluyveromyces fragilis
    • Garcia-Garibay M., Goèmez-Ruiz L., and Baèrzana E. Studies on the simultaneous production of single cell protein and polygalacturonase from Kluyveromyces fragilis. Biotechnol. Lett. 9 (1987) 411-416
    • (1987) Biotechnol. Lett. , vol.9 , pp. 411-416
    • Garcia-Garibay, M.1    Goèmez-Ruiz, L.2    Baèrzana, E.3
  • 16
    • 4243553322 scopus 로고
    • Production of industrial enzymes and some applications in fermented foods
    • Wood B.J.B. (Ed), Elsevier, London
    • Godfrey A. Production of industrial enzymes and some applications in fermented foods. In: Wood B.J.B. (Ed). Microbiology Fermented Foods vol. 1 (1985), Elsevier, London 345-371
    • (1985) Microbiology Fermented Foods , vol.1 , pp. 345-371
    • Godfrey, A.1
  • 17
    • 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
  • 18
    • 34249093490 scopus 로고    scopus 로고
    • Pectin lyase and pectate lyase from Debaryomyces nepalensis isolated from apple
    • Gummadi S.N., and Kumar D.S. Pectin lyase and pectate lyase from Debaryomyces nepalensis isolated from apple. Res. J. Microbiol. 1 (2006) 152-159
    • (2006) Res. J. Microbiol. , vol.1 , pp. 152-159
    • Gummadi, S.N.1    Kumar, D.S.2
  • 19
    • 36048948372 scopus 로고    scopus 로고
    • Enhanced production of pectin lyase and pectate lyase by Debaryomyces nepalensis in submerged fermentation by statistical methods
    • Gummadi S.N., and Kumar D.S. Enhanced production of pectin lyase and pectate lyase by Debaryomyces nepalensis in submerged fermentation by statistical methods. Am. J. Food Technol. 1 (2006) 19-33
    • (2006) Am. J. Food Technol. , vol.1 , pp. 19-33
    • Gummadi, S.N.1    Kumar, D.S.2
  • 20
    • 33745271337 scopus 로고    scopus 로고
    • Optimization of chemical and physical parameters affecting the activity of pectin lyase and pectate lyase from Debaryomyces nepalensis: a statistical approach
    • Gummadi S.N., and Kumar D.S. Optimization of chemical and physical parameters affecting the activity of pectin lyase and pectate lyase from Debaryomyces nepalensis: a statistical approach. Biochem. Eng. J. 30 (2006) 130-137
    • (2006) Biochem. Eng. J. , vol.30 , pp. 130-137
    • Gummadi, S.N.1    Kumar, D.S.2
  • 23
    • 0001884169 scopus 로고
    • Enzymes and their uses in the processed apple industry: a review
    • Kilara A. Enzymes and their uses in the processed apple industry: a review. Process Biochem. 23 (1982) 35-41
    • (1982) Process Biochem. , vol.23 , pp. 35-41
    • Kilara, A.1
  • 24
    • 0346767626 scopus 로고
    • Temprature and pH influence on pectinolytic activities of some fungi cultured in solid state medium
    • Loudiere S., Durand A., and Grajek W. Temprature and pH influence on pectinolytic activities of some fungi cultured in solid state medium. J. Eur. Cong-Biotechnol. 3 (1987) 258-263
    • (1987) J. Eur. Cong-Biotechnol. , vol.3 , pp. 258-263
    • Loudiere, S.1    Durand, A.2    Grajek, W.3
  • 26
    • 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
  • 27
    • 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. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 28
    • 0026680868 scopus 로고
    • Production of yeast polygalacturonases in dairy wastes
    • Murad H.A., and Foda M.S. Production of yeast polygalacturonases in dairy wastes. Bioresour. Technol. 41 (1992) 247-250
    • (1992) Bioresour. Technol. , vol.41 , pp. 247-250
    • Murad, H.A.1    Foda, M.S.2
  • 29
    • 85047679885 scopus 로고    scopus 로고
    • Production of pectolytic enzymes - a review
    • Naidu G.S.N., and Panda T. Production of pectolytic enzymes - a review. Bioprocess Eng. 19 (1998) 355-361
    • (1998) Bioprocess Eng. , vol.19 , pp. 355-361
    • Naidu, G.S.N.1    Panda, T.2
  • 31
    • 0033868361 scopus 로고    scopus 로고
    • Rotating simplex method of optimization of physical parameters for higher production of pectinases in bioreactor
    • Panda T., and Naidu G.S.N. Rotating simplex method of optimization of physical parameters for higher production of pectinases in bioreactor. Bioprocess Eng. 23 (2000) 47-49
    • (2000) Bioprocess Eng. , vol.23 , pp. 47-49
    • Panda, T.1    Naidu, G.S.N.2
  • 32
    • 0037474394 scopus 로고    scopus 로고
    • Influence of different mixing and aeration regimes on pectin lyase production by Penicillium griseoroseum
    • Piccoli-Valle R.H., Passos F.J.V., Brandi I.V., Peternelli L.A., and Silva D.O. Influence of different mixing and aeration regimes on pectin lyase production by Penicillium griseoroseum. Process Biochem. 38 (2003) 849-854
    • (2003) Process Biochem. , vol.38 , pp. 849-854
    • Piccoli-Valle, R.H.1    Passos, F.J.V.2    Brandi, I.V.3    Peternelli, L.A.4    Silva, D.O.5
  • 34
    • 0034135689 scopus 로고    scopus 로고
    • Pectinase in papermaking: Solving retention problems in mechanical pulp, bleached with hydrogen peroxide
    • Reid I., and Ricard M. Pectinase in papermaking: Solving retention problems in mechanical pulp, bleached with hydrogen peroxide. Enzyme Microb. Technol. 26 (2000) 115-123
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 115-123
    • Reid, I.1    Ricard, M.2
  • 36
    • 36048978754 scopus 로고    scopus 로고
    • Salazar, L., Jayasinghe, U., 1999. Fundamentals of purification of plant viruses. In: Techniques in Plant Virology. CIP Training Manual 5.0, Virus purification, International Potato Center, Peru, pp. 1-10.
  • 37
    • 33644642851 scopus 로고    scopus 로고
    • Effect of nitrogen limitation on the ergosterol production by fed-batch culture of Saccharomyces cerevisia
    • Shang F., Wen S., Wang X., and Tan T. Effect of nitrogen limitation on the ergosterol production by fed-batch culture of Saccharomyces cerevisia. J. Biotechnol. 122 (2006) 285-292
    • (2006) J. Biotechnol. , vol.122 , pp. 285-292
    • Shang, F.1    Wen, S.2    Wang, X.3    Tan, T.4
  • 38
    • 0033179810 scopus 로고    scopus 로고
    • Exopolygalacturonate lyase from a thermophilic Bacillus sp
    • Singh S.A., Plattnera H., and Diekmann H. Exopolygalacturonate lyase from a thermophilic Bacillus sp. Enzyme Microb. Technol. 25 (1999) 420-425
    • (1999) Enzyme Microb. Technol. , vol.25 , pp. 420-425
    • Singh, S.A.1    Plattnera, H.2    Diekmann, H.3
  • 39
    • 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
  • 40
    • 84963043384 scopus 로고
    • Isolation of tobacco mesophyll cells in intact and active state
    • Takebe I., Otsuki Y., and Aoki S. Isolation of tobacco mesophyll cells in intact and active state. Plant Cell Physiol. 9 (1968) 115-124
    • (1968) Plant Cell Physiol. , vol.9 , pp. 115-124
    • Takebe, I.1    Otsuki, Y.2    Aoki, S.3
  • 42
    • 0017850958 scopus 로고
    • Pectinolytic activity of Saccharomyces fragilis cultured in controlled environments
    • Wimborne M.P., and Rickard P.A.D. Pectinolytic activity of Saccharomyces fragilis cultured in controlled environments. Biotechnol. Bioeng. 20 (1978) 231-242
    • (1978) Biotechnol. Bioeng. , vol.20 , pp. 231-242
    • Wimborne, M.P.1    Rickard, P.A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.