메뉴 건너뛰기




Volumn 15, Issue 6, 2010, Pages 984-992

Statistical optimization of Bacillus alcalophilus α-amylase immobilization on iron-oxide magnetic nanoparticles

Author keywords

alkaline amylase; Bacillus alcalophilus; magnetic nanoparticles; Plackett Burman design; response surface; starch hydrolysis

Indexed keywords

BINDING PROCESS; BIOCONJUGATES; COEFFICIENT OF DETERMINATION; COST EFFECTIVE; FACTORIAL DESIGN; IMMOBILIZED ENZYME; INDUSTRIAL SECTOR; MAGNETIC NANOPARTICLES; NANO-SIZED; PLACKETT-BURMAN; PLACKETT-BURMAN DESIGNS; QUADRATIC MODELS; RESPONSE SURFACE; RESPONSE SURFACE METHODOLOGY; SCANNING ELECTRON MICROSCOPE; SPECIFIC ACTIVITY; STARCH HYDROLYSIS; STATISTICAL OPTIMIZATION; STORAGE STABILITY;

EID: 79952635234     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12257-009-3160-7     Document Type: Article
Times cited : (39)

References (20)
  • 1
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: A review
    • DOI 10.1016/S0960-8524(03)00033-6
    • Haki, G. D. and S. K. Rakshit (2003) Developments in industrially important thermostable enzymes: A review. Bioresource Technol. 89: 17-34. (Pubitemid 36379207)
    • (2003) Bioresource Technology , vol.89 , Issue.1 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 3
    • 33646461272 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh
    • Kim, S. -B., D. -W. Lee, C. -I. Cheigh, E. -A. Choe, S. -J. Lee, Y. -H. Hong, H. -J. Choi, and Y. -R. Pyun (2006) Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh. J. Ind. Microbiol. Biotechnol. 33: 436-444.
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 436-444
    • Kim, S.B.1    Lee, D.W.2    Cheigh, C.I.3    Choe, E.A.4    Lee, S.J.5    Hong, Y.H.6    Choi, H.J.7    Pyun, Y.R.8
  • 4
    • 0035128695 scopus 로고    scopus 로고
    • A novel magnetic affinity support for protein adsorption and purification
    • Tong, X. D., B. Xue, and Y. Sun (2001) A novel magnetic affinity support for protein adsorption and purification. Biotechnol. Prog. 17: 134-139.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 134-139
    • Tong, X.D.1    Xue, B.2    Sun, Y.3
  • 5
    • 0034757787 scopus 로고    scopus 로고
    • Immobilization of yeast alcohol dehydrogenase on magnetic nanoparticles for improving its stability
    • Liao, M. H. and D. H. Chen (2001) Immobilization of yeast alcohol dehydrogenase on magnetic nanoparticles for improving its stability. Biotechnol. Lett. 23: 1723-1727.
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1723-1727
    • Liao, M.H.1    Chen, D.H.2
  • 7
    • 11044222650 scopus 로고    scopus 로고
    • Synthesis and surface engineering of iron oxide nanoparticles for biomedical applications
    • DOI 10.1016/j.biomaterials.2004.10.012, PII S0142961204009317
    • Gupta, A. K. and M. Gupta (2005) Synthesis and surface engineering of iron oxide nanoparticles for biomedical applications. Biomaterials 26: 3995-4021. (Pubitemid 40044762)
    • (2005) Biomaterials , vol.26 , Issue.18 , pp. 3995-4021
    • Gupta, A.K.1    Gupta, M.2
  • 8
    • 36448940169 scopus 로고    scopus 로고
    • Surface modified superparamagnetic iron oxide nanoparticles: As a new carrier for bio-magnetically targeted therapy
    • Liang, S., Y. Wang, J. Yu, C. Zhang, J. Xia, and D. Yin (2007) Surface modified superparamagnetic iron oxide nanoparticles: as a new carrier for bio-magnetically targeted therapy. J. Mater. Sci. Mater. Med. 18: 2297-2302.
    • (2007) J. Mater. Sci. Mater. Med. , vol.18 , pp. 2297-2302
    • Liang, S.1    Wang, Y.2    Yu, J.3    Zhang, C.4    Xia, J.5    Yin, D.6
  • 9
    • 10344239868 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a thermostable, alkaliphilic, extracellular a-amylase from Bacillus subtilis DM-03, isolated from the traditional fermented food of India
    • Das, K., R. Doley, and A. K. Mukherjee (2004) Purification and biochemical characterization of a thermostable, alkaliphilic, extracellular a-amylase from Bacillus subtilis DM-03, isolated from the traditional fermented food of India. J Biotechnol. Appl. Biochem. 40: 291-298.
    • (2004) J Biotechnol. Appl. Biochem. , vol.40 , pp. 291-298
    • Das, K.1    Doley, R.2    Mukherjee, A.K.3
  • 10
    • 9944253349 scopus 로고    scopus 로고
    • Glucose oxidase-magnetite nanoparticle bioconjugate for glucose sensing
    • Rossi, L. M., A. D. Quach, and Z. Rosenzweig (2004) Glucose oxidase-magnetite nanoparticle bioconjugate for glucose sensing. Ana. Bioanal. Chem. 380: 606-613.
    • (2004) Ana. Bioanal. Chem. , vol.380 , pp. 606-613
    • Rossi, L.M.1    Quach, A.D.2    Rosenzweig, Z.3
  • 12
    • 0001131698 scopus 로고
    • The design of optimum multifactorial experiments
    • Plackett, R. L. and J. P. Burman (1946) The design of optimum multifactorial experiments. Biometrika 33: 305-325.
    • (1946) Biometrika , vol.33 , pp. 305-325
    • Plackett, R.L.1    Burman, J.P.2
  • 13
    • 34447644929 scopus 로고    scopus 로고
    • Comparison of lipopeptide biosurfactants production by Bacillus subtilis strains in submerged and solid state fermentation systems using a cheap carbon source: Some industrial applications of biosurfactants
    • Das, K. and A. K. Mukherjee (2007) Comparison of lipopeptide biosurfactants production by Bacillus subtilis strains in submerged and solid state fermentation systems using a cheap carbon source: Some industrial applications of biosurfactants. Proc. Biochem. 42: 1191-1199.
    • (2007) Proc. Biochem. , vol.42 , pp. 1191-1199
    • Das, K.1    Mukherjee, A.K.2
  • 14
    • 0003425407 scopus 로고    scopus 로고
    • A foundation for analysis in the health sciences. Hypothesis testing
    • 7th ed., W.W. Daniel (eds.). John Wiley and Sons, Inc., NY. USA
    • Daniel, W. W. (2000) A foundation for analysis in the health sciences. Hypothesis testing. 7th ed., pp. 166-167. In: W.W. Daniel (eds.). Biostatistics. John Wiley and Sons, Inc., NY. USA.
    • (2000) Biostatistics , pp. 166-167
    • Daniel, W.W.1
  • 16
    • 0036100312 scopus 로고    scopus 로고
    • Covalent cross-linking of proteins without chemical reagents
    • DOI 10.1110/ps.4390102
    • Simons, B. L., M. C. King, T. Cyr, M. A. Hefford, and H. Kaplan (2002) Covalent crosslinking of proteins without chemical reagents. Protein Sci. 11: 1558-1564. (Pubitemid 34547226)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1558-1564
    • Simons, B.L.1    King, M.C.2    Cyr, T.3    Hefford, M.A.4    Kaplan, H.5
  • 18
    • 0038039289 scopus 로고    scopus 로고
    • Direct binding and characterization of lipase onto magnetic nanoparticles
    • Huang, S. -H., M. -H. Liao, and D. -H. Chen (2003) Direct binding and characterization of lipase onto magnetic nanoparticles. Biotechnol. Prog. 19: 1095-1100.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1095-1100
    • Huang, S.H.1    Liao, M.H.2    Chen, D.H.3
  • 19
    • 37348998909 scopus 로고    scopus 로고
    • Covalent immobilization of chloroperoxidase onto magnetic beads: Catalytic properties and stability
    • Bayramoglu, G., S. Kiralp, M. Yilmaz, L. Toppare, and M. Y. Ar ca (2008) Covalent immobilization of chloroperoxidase onto magnetic beads: Catalytic properties and stability. Biochem. Eng. J. 38: 180-188.
    • (2008) Biochem. Eng. J. , vol.38 , pp. 180-188
    • Bayramoglu, G.1    Kiralp, S.2    Yilmaz, M.3    Toppare, L.4    Ar Ca, M.Y.5
  • 20
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T. and S. N. Timasheff (1985) The stabilization of proteins by osmolytes. Biophysical J. 47: 411-414.
    • (1985) Biophysical J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.