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Volumn 63, Issue 3, 2008, Pages 706-709

A study of cell disruption of Candida mogii by glass bead mill for the recovery of xylose reductase

Author keywords

Candida mogii; Cell disruption; Experimental design; Glass beads mill; Xylose reductase

Indexed keywords

CELLS; CONCENTRATION (PROCESS); CONCRETES; EXPERIMENTS; GLASS; GRANULAR MATERIALS; STATISTICS;

EID: 54049114610     PISSN: 13835866     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.seppur.2008.06.019     Document Type: Article
Times cited : (13)

References (16)
  • 1
    • 33846220739 scopus 로고    scopus 로고
    • Chemical disruption of yeast cells for the isolation of carotenoid pigments
    • Park P.K., Kima E.Y., and Chub K.H. Chemical disruption of yeast cells for the isolation of carotenoid pigments. Sep. Purif. Technol. 53 (2007) 148-152
    • (2007) Sep. Purif. Technol. , vol.53 , pp. 148-152
    • Park, P.K.1    Kima, E.Y.2    Chub, K.H.3
  • 2
    • 0028801947 scopus 로고
    • Process-scale disruption of microorganisms
    • Middelberg A.P.J. Process-scale disruption of microorganisms. Biotechnol. Adv. 13 (1995) 491-551
    • (1995) Biotechnol. Adv. , vol.13 , pp. 491-551
    • Middelberg, A.P.J.1
  • 3
    • 11444256579 scopus 로고    scopus 로고
    • A simplified strategy for the release and primary recovery of c-phycocyanin produced by Spirulinamaxima
    • Cisneros M., and Rito-Palomares M. A simplified strategy for the release and primary recovery of c-phycocyanin produced by Spirulinamaxima. Chem. Biochem. Eng. Q. 18 (2004) 385-390
    • (2004) Chem. Biochem. Eng. Q. , vol.18 , pp. 385-390
    • Cisneros, M.1    Rito-Palomares, M.2
  • 4
    • 0000157540 scopus 로고
    • A new model for the disruption of Escherichia coli by high-pressure homogenization. Part I. Model development and verification
    • (Part C)
    • Middelberg A.P.J., O'Neil B.K., and Bogle I.D.L. A new model for the disruption of Escherichia coli by high-pressure homogenization. Part I. Model development and verification. Trans. IchemE 70 (1992) 205-211 (Part C)
    • (1992) Trans. IchemE , vol.70 , pp. 205-211
    • Middelberg, A.P.J.1    O'Neil, B.K.2    Bogle, I.D.L.3
  • 5
    • 36949081532 scopus 로고
    • Metabolism of the d-xylose by moulds
    • Chiang C., and Knight S.G. Metabolism of the d-xylose by moulds. Nature 188 (1960) 79-81
    • (1960) Nature , vol.188 , pp. 79-81
    • Chiang, C.1    Knight, S.G.2
  • 6
    • 0030950654 scopus 로고    scopus 로고
    • Xylitol production from rice straw hemicellulose hydrolysate using different yeast strains
    • Mayerhoff Z.D.V.L., Roberto I.C., and Silva S.S. Xylitol production from rice straw hemicellulose hydrolysate using different yeast strains. Biotechnol. Lett. 19 (1997) 407-409
    • (1997) Biotechnol. Lett. , vol.19 , pp. 407-409
    • Mayerhoff, Z.D.V.L.1    Roberto, I.C.2    Silva, S.S.3
  • 7
    • 0032171342 scopus 로고    scopus 로고
    • Biotechnological production of xylitol. Part 1. Interest of xylitol and fundamentals of its biosynthesis
    • Parajó J.C., Dominguez H., and Dominguez J.M. Biotechnological production of xylitol. Part 1. Interest of xylitol and fundamentals of its biosynthesis. Bioresour. Technol. 65 (1998) 191-201
    • (1998) Bioresour. Technol. , vol.65 , pp. 191-201
    • Parajó, J.C.1    Dominguez, H.2    Dominguez, J.M.3
  • 8
    • 0022514855 scopus 로고
    • Affinity purifications of aldose reductase and xylitol dehydrogenase from the xylose-fermenting yeast Pachysolen tannophilus
    • Bolen P.L., Kelly A.R., and Freer S.N. Affinity purifications of aldose reductase and xylitol dehydrogenase from the xylose-fermenting yeast Pachysolen tannophilus. Appl. Environ. Microbiol. 52 (1986) 660-664
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 660-664
    • Bolen, P.L.1    Kelly, A.R.2    Freer, S.N.3
  • 9
    • 1842491630 scopus 로고    scopus 로고
    • Extraction by reversed micelles of the intracellular enzyme xylose reductase
    • Cortez E.V., Roberto I.C., Pessoa Jr. A., and Vitolo M. Extraction by reversed micelles of the intracellular enzyme xylose reductase. Appl. Biochem. Biotechnol. 91/93 (2001) 753-759
    • (2001) Appl. Biochem. Biotechnol. , vol.91-93 , pp. 753-759
    • Cortez, E.V.1    Roberto, I.C.2    Pessoa Jr., A.3    Vitolo, M.4
  • 10
    • 0034074809 scopus 로고    scopus 로고
    • Effects of environmental conditions on xylose reductase and xylitol dehydrogenase production by Candida guilliermondii
    • Sene L., Vitolo M., Felipe M.G.A., and Silva S.S. Effects of environmental conditions on xylose reductase and xylitol dehydrogenase production by Candida guilliermondii. Appl. Biochem. Biotechnol. 84/86 (2000) 371-380
    • (2000) Appl. Biochem. Biotechnol. , vol.84-86 , pp. 371-380
    • Sene, L.1    Vitolo, M.2    Felipe, M.G.A.3    Silva, S.S.4
  • 11
    • 84985666837 scopus 로고
    • Release of protein from bakers' yeast (Saccharomyces cerevisiae) by disruption in an industrial agitator Mill
    • Currie J.A., Dunnill P., and Lilly M.D. Release of protein from bakers' yeast (Saccharomyces cerevisiae) by disruption in an industrial agitator Mill. Biotechnol. Bioeng. 14 (1972) 725-736
    • (1972) Biotechnol. Bioeng. , vol.14 , pp. 725-736
    • Currie, J.A.1    Dunnill, P.2    Lilly, M.D.3
  • 12
    • 0035021951 scopus 로고    scopus 로고
    • Activity of xylose reductase from Candida mogii grown in media containing different concentrations of rice straw hydrolysate
    • Mayerhoff Z.D.V.L., Roberto I.C., and Franco T.T. Activity of xylose reductase from Candida mogii grown in media containing different concentrations of rice straw hydrolysate. Appl. Biochem. Biotechnol. 91-93 (2001) 729-737
    • (2001) Appl. Biochem. Biotechnol. , vol.91-93 , pp. 729-737
    • Mayerhoff, Z.D.V.L.1    Roberto, I.C.2    Franco, T.T.3
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0021699836 scopus 로고
    • Xylose metabolism in Pachysolen tannophilus: purification and properties of xylose reductase
    • Ditzelmüller G., Kubicek C.P., Wöhrer W., and Röhr M. Xylose metabolism in Pachysolen tannophilus: purification and properties of xylose reductase. Can. J. Microbiol. 30 (1984) 1330-1336
    • (1984) Can. J. Microbiol. , vol.30 , pp. 1330-1336
    • Ditzelmüller, G.1    Kubicek, C.P.2    Wöhrer, W.3    Röhr, M.4
  • 16
    • 0031282431 scopus 로고    scopus 로고
    • In situ properties of Helicobacter pylori aspartate carbamoyltransferase
    • Burns B.P., Mendz G.L., and Hazell S.L. In situ properties of Helicobacter pylori aspartate carbamoyltransferase. Arch. Biochem. Biophys. 347 (1997) 119-125
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 119-125
    • Burns, B.P.1    Mendz, G.L.2    Hazell, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.