메뉴 건너뛰기




Volumn 99, Issue 18, 2008, Pages 8662-8666

Immobilization of Neocallimastix patriciarum xylanase on artificial oil bodies and statistical optimization of enzyme activity

Author keywords

Artificial oil body; Immobilization; Neocallimastix patriciarum; Xylanase

Indexed keywords

CENTRIFUGATION; CHARGE COUPLED DEVICES; ENZYME IMMOBILIZATION; ESCHERICHIA COLI; FOOD ADDITIVES; FOOD PROCESSING; OILS AND FATS; OPTIMIZATION; REGRESSION ANALYSIS;

EID: 50649089598     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2008.04.017     Document Type: Article
Times cited : (34)

References (27)
  • 1
    • 50649084584 scopus 로고    scopus 로고
    • Akhnazarova, S., Kafarov, V., 1982. Experiment Optimization in Chemistry and Chemical Engineering. Mir, Moscow.
    • Akhnazarova, S., Kafarov, V., 1982. Experiment Optimization in Chemistry and Chemical Engineering. Mir, Moscow.
  • 2
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim H.C., and Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7 (1979) 1513-1517
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1517
    • Birnboim, H.C.1    Doly, J.2
  • 3
    • 0002363078 scopus 로고
    • On the experimental attainment of optimum conditions
    • Box G.E.P., and Wilson K.B. On the experimental attainment of optimum conditions. J. R. Stat. Soc. 13 (1951) 1-45
    • (1951) J. R. Stat. Soc. , vol.13 , pp. 1-45
    • Box, G.E.P.1    Wilson, K.B.2
  • 4
    • 0035723208 scopus 로고    scopus 로고
    • Directed evolution to produce an alkalophilic variant from a Neocallimastix patriciarum xylanase
    • Chen Y.L., Tang T.Y., and Cheng K.-J. Directed evolution to produce an alkalophilic variant from a Neocallimastix patriciarum xylanase. Can. J. Microbiol. 47 (2001) 1088-1094
    • (2001) Can. J. Microbiol. , vol.47 , pp. 1088-1094
    • Chen, Y.L.1    Tang, T.Y.2    Cheng, K.-J.3
  • 5
    • 21644451024 scopus 로고    scopus 로고
    • Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli
    • Chiang C.J., Chen H.C., Chao Y.P., and Tzen J.T.C. Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli. J. Agric. Food Chem. 53 (2005) 4799-4804
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 4799-4804
    • Chiang, C.J.1    Chen, H.C.2    Chao, Y.P.3    Tzen, J.T.C.4
  • 6
    • 33745957439 scopus 로고    scopus 로고
    • A simple and effective method to prepare immobilized enzymes using artificial oil bodies
    • Chiang C.J., Chen H.C., Kuo H.F., Chao Y.P., and Tzen J.T.C. A simple and effective method to prepare immobilized enzymes using artificial oil bodies. Enzyme Microb. Technol. 39 (2006) 1152-1158
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 1152-1158
    • Chiang, C.J.1    Chen, H.C.2    Kuo, H.F.3    Chao, Y.P.4    Tzen, J.T.C.5
  • 7
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T., Gerday C., and Feller G. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 29 (2005) 3-23
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 9
    • 33745213542 scopus 로고    scopus 로고
    • Statistical optimization of thermo-tolerant xylanase activity from Amazon isolated Bacillus circulans on solid-state cultivation
    • Heck J.X., Flôres S.H., Hertz P.F., and Ayub M.A.Z. Statistical optimization of thermo-tolerant xylanase activity from Amazon isolated Bacillus circulans on solid-state cultivation. Bioresour. Technol. 97 (2006) 1902-1906
    • (2006) Bioresour. Technol. , vol.97 , pp. 1902-1906
    • Heck, J.X.1    Flôres, S.H.2    Hertz, P.F.3    Ayub, M.A.Z.4
  • 10
    • 27544472308 scopus 로고    scopus 로고
    • Methodology for the immobilization of enzymes onto mesoporous materials
    • Hudson S., Magner E., Cooney J., and Hodnett B.K. Methodology for the immobilization of enzymes onto mesoporous materials. J. Phys. Chem. B 109 (2005) 19496-19506
    • (2005) J. Phys. Chem. B , vol.109 , pp. 19496-19506
    • Hudson, S.1    Magner, E.2    Cooney, J.3    Hodnett, B.K.4
  • 11
    • 0036051173 scopus 로고    scopus 로고
    • Determination of xylanase, β-glucanase, and cellulase activity
    • Konig J., Grasser R., Pikor H., and Vogel K. Determination of xylanase, β-glucanase, and cellulase activity. Anal. Bioanal. Chem. 374 (2002) 80-87
    • (2002) Anal. Bioanal. Chem. , vol.374 , pp. 80-87
    • Konig, J.1    Grasser, R.2    Pikor, H.3    Vogel, K.4
  • 12
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • Kulkarni N., Shendye A., and Rao M. Molecular and biotechnological aspects of xylanases. FEMS Microbiol. Rev. 23 (1999) 411-456
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye, A.2    Rao, M.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophate T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophate T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 33845740350 scopus 로고    scopus 로고
    • Characterization and immobilization of liposome-bound cellulase for hydrolysis of insoluble cellulose
    • Li C., Yoshimoto M., Fukunaga K., and Nakao K. Characterization and immobilization of liposome-bound cellulase for hydrolysis of insoluble cellulose. Bioresour. Technol. 98 (2007) 1366-1372
    • (2007) Bioresour. Technol. , vol.98 , pp. 1366-1372
    • Li, C.1    Yoshimoto, M.2    Fukunaga, K.3    Nakao, K.4
  • 15
    • 0000450509 scopus 로고    scopus 로고
    • Plant seed oil-bodies as an immobilization matrix for a recombinant xylanase from the rumen fungus Neocallimastix patriciarum
    • Liu J.H., Selinger L.B., Cheng K.-J., Beauchemin K.A., and Moloney M.M. Plant seed oil-bodies as an immobilization matrix for a recombinant xylanase from the rumen fungus Neocallimastix patriciarum. Mol. Breeding 3 (1997) 463-470
    • (1997) Mol. Breeding , vol.3 , pp. 463-470
    • Liu, J.H.1    Selinger, L.B.2    Cheng, K.-J.3    Beauchemin, K.A.4    Moloney, M.M.5
  • 16
    • 32044440289 scopus 로고    scopus 로고
    • Expression of rumen microbial fibrolytic enzyme genes in probiotic Lactobacillus reuteri
    • Liu J.R., Yu B., Liu F.H., Cheng K.-J., and Zhao X. Expression of rumen microbial fibrolytic enzyme genes in probiotic Lactobacillus reuteri. Appl. Environ. Microbiol. 71 (2005) 6769-6775
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 6769-6775
    • Liu, J.R.1    Yu, B.2    Liu, F.H.3    Cheng, K.-J.4    Zhao, X.5
  • 19
    • 0011736264 scopus 로고    scopus 로고
    • Experiments with a single factor: the analysis of variance
    • Montgomery D.C. (Ed), John Wiley and Sons, New York
    • Montgomery D.C. Experiments with a single factor: the analysis of variance. In: Montgomery D.C. (Ed). Design and Analysis of Experiments (1999), John Wiley and Sons, New York 75-77
    • (1999) Design and Analysis of Experiments , pp. 75-77
    • Montgomery, D.C.1
  • 20
    • 2442480755 scopus 로고    scopus 로고
    • Method for bacterial expression and purification of sesame cystatin via artificial oil bodies
    • Peng C.C., Shyu D.J.H., Chou W.M., Chen M.J., and Tzen J.T.C. Method for bacterial expression and purification of sesame cystatin via artificial oil bodies. J. Agric. Food Chem. 52 (2004) 3115-3119
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 3115-3119
    • Peng, C.C.1    Shyu, D.J.H.2    Chou, W.M.3    Chen, M.J.4    Tzen, J.T.C.5
  • 21
    • 0038182311 scopus 로고    scopus 로고
    • Immobilization of xylan-degrading enzymes from Melanocarpus albomyces IIS 68 on the smart polymer Eudragit L-100
    • Roy I., Gupta A., Khare S.K., Bisaria V.S., and Gupta M.N. Immobilization of xylan-degrading enzymes from Melanocarpus albomyces IIS 68 on the smart polymer Eudragit L-100. Appl. Microbiol. Biotechnol. 61 (2003) 309-313
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 309-313
    • Roy, I.1    Gupta, A.2    Khare, S.K.3    Bisaria, V.S.4    Gupta, M.N.5
  • 23
    • 50649099102 scopus 로고    scopus 로고
    • Statistical Analysis System Institute, 1998. SAS User's Guide: Statistics. SAS Institute Inc., Cary, N.C.
    • Statistical Analysis System Institute, 1998. SAS User's Guide: Statistics. SAS Institute Inc., Cary, N.C.
  • 24
    • 0036210191 scopus 로고    scopus 로고
    • Biotechnology of microbial xylanases: enzymology, molecular biology, and application
    • Subramaniyan S., and Prema P. Biotechnology of microbial xylanases: enzymology, molecular biology, and application. Crit. Rev. Biotechnol. 22 (2002) 33-64
    • (2002) Crit. Rev. Biotechnol. , vol.22 , pp. 33-64
    • Subramaniyan, S.1    Prema, P.2
  • 25
    • 34848914559 scopus 로고    scopus 로고
    • Production of xylobiose from the autohydrolysis explosion liquor of corncob using Thermotoga maritima xylanase B (XynB) immobilized on nickel-chelated Eupergit C
    • Tan S.S., Li D.Y., Jiang Z.Q., Zhu Y.P., Shi B., and Li L.T. Production of xylobiose from the autohydrolysis explosion liquor of corncob using Thermotoga maritima xylanase B (XynB) immobilized on nickel-chelated Eupergit C. Bioresour. Technol. 99 (2008) 200-204
    • (2008) Bioresour. Technol. , vol.99 , pp. 200-204
    • Tan, S.S.1    Li, D.Y.2    Jiang, Z.Q.3    Zhu, Y.P.4    Shi, B.5    Li, L.T.6
  • 26
    • 33144488261 scopus 로고    scopus 로고
    • Immobilization of β-glucosidase on Eupergit C for lignocellulose hydrolysis
    • Tu M., Zhang X., Kurabi A., Gilkes N., Mabee W., and Saddler J. Immobilization of β-glucosidase on Eupergit C for lignocellulose hydrolysis. Biotechnol. Lett. 28 (2006) 151-156
    • (2006) Biotechnol. Lett. , vol.28 , pp. 151-156
    • Tu, M.1    Zhang, X.2    Kurabi, A.3    Gilkes, N.4    Mabee, W.5    Saddler, J.6
  • 27
    • 33749835413 scopus 로고    scopus 로고
    • Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific
    • Wu S., Liu B., and Zhang X. Characterization of a recombinant thermostable xylanase from deep-sea thermophilic Geobacillus sp. MT-1 in East Pacific. Appl. Microbiol. Biotechnol. 72 (2006) 1210-1216
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 1210-1216
    • Wu, S.1    Liu, B.2    Zhang, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.