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Volumn 13, Issue 11, 2003, Pages 897-901

An FTIR spectroscopy study of the interaction between α s-casein-bound phosphoryl groups and chitosan

Author keywords

Casein chitosan complex; Chitosan; FTIR; Phosphate stretching; casein

Indexed keywords


EID: 0142198448     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-6946(03)00115-8     Document Type: Article
Times cited : (22)

References (20)
  • 1
    • 0027987495 scopus 로고
    • Structure and thermal denaturation of crystalline and non-crystalline cytochrome oxidase as studied by infrared spectroscopy
    • Arrondo, J. L. R., Castresana, J. J. M., Valpuesta, J. M., & Goñi, F. M. (1994). Structure and thermal denaturation of crystalline and non-crystalline cytochrome oxidase as studied by infrared spectroscopy. Biochemistry, 33, 11650-11655.
    • (1994) Biochemistry , vol.33 , pp. 11650-11655
    • Arrondo, J.L.R.1    Castresana, J.J.M.2    Valpuesta, J.M.3    Goñi, F.M.4
  • 4
    • 0036914043 scopus 로고    scopus 로고
    • Growth of milk fermentative bacteria in the presence of chitosan for potential use in cheese making
    • Ausar, S. F., Passalacqua, N., Castagna, L. F., Bianco, I. D., & Beltramo, D. M. (2002). Growth of milk fermentative bacteria in the presence of chitosan for potential use in cheese making. International Dairy Journal, 12, 899-906.
    • (2002) International Dairy Journal , vol.12 , pp. 899-906
    • Ausar, S.F.1    Passalacqua, N.2    Castagna, L.F.3    Bianco, I.D.4    Beltramo, D.M.5
  • 5
    • 0033529630 scopus 로고    scopus 로고
    • 2+-ATPase. Molecular interpretation of infrared difference spectra
    • 2+-ATPase. Molecular interpretation of infrared difference spectra. Journal of Biological Chemistry, 274, 22170-22175.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 22170-22175
    • Barth, A.1
  • 6
    • 0000942193 scopus 로고
    • Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein
    • Byler, D. M., & Farrell Jr., H. M. , (1989). Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein. Journal of Dairy Science, 72, 1719-1723.
    • (1989) Journal of Dairy Science , vol.72 , pp. 1719-1723
    • Byler, D.M.1    Farrell H.M., Jr.2
  • 7
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - A 25 year update
    • Cohen, P. (2000). The regulation of protein function by multisite phosphorylation-a 25 year update. Trends in Biochemical Sciences, 25, 596-601.
    • (2000) Trends in Biochemical Sciences , vol.25 , pp. 596-601
    • Cohen, P.1
  • 8
    • 0032246954 scopus 로고    scopus 로고
    • Changes in the secondary structure of bovine casein by Fourier transform infrared spectroscopy: Effects of calcium and temperature
    • Curley, D. M., Kumosinski, T. F., Unruh, J. J., & Farrell Jr., H. M., (1998). Changes in the secondary structure of bovine casein by Fourier transform infrared spectroscopy: Effects of calcium and temperature. Journal of Dairy Science, 81, 3154-3162.
    • (1998) Journal of Dairy Science , vol.81 , pp. 3154-3162
    • Curley, D.M.1    Kumosinski, T.F.2    Unruh, J.J.3    Farrell H.M., Jr.4
  • 10
    • 0027959395 scopus 로고
    • Use of photoacoustic Fourier-transform infrared spectroscopy to study phosphates in proteins
    • Graves, D. J., & Luo, S. (1994). Use of photoacoustic Fourier-transform infrared spectroscopy to study phosphates in proteins. Biochemical and Biophysical Research Communications, 205, 618-624.
    • (1994) Biochemical and Biophysical Research Communications , vol.205 , pp. 618-624
    • Graves, D.J.1    Luo, S.2
  • 11
    • 0033311821 scopus 로고    scopus 로고
    • Chitosan-polyelectrolyte complexation for the preparation of gel beads and controlled release of anticancer drug. I. Effect of phosphorous polyelectrolyte complex and enzymatic hydrolysis of polymer
    • Mi, F. L., Shyu, S. S., Kuan, C. Y., Lee, S. T., Lu, K. T., & Jang S. F. (1999). Chitosan-polyelectrolyte complexation for the preparation of gel beads and controlled release of anticancer drug. I. Effect of phosphorous polyelectrolyte complex and enzymatic hydrolysis of polymer. Journal of Applied Polymer Science, 74, 1868-1879.
    • (1999) Journal of Applied Polymer Science , vol.74 , pp. 1868-1879
    • Mi, F.L.1    Shyu, S.S.2    Kuan, C.Y.3    Lee, S.T.4    Lu, K.T.5    Jang, S.F.6
  • 12
    • 0034730575 scopus 로고    scopus 로고
    • Partly folded states of bovine carbonic anhydrase interact with zwitterionic and anionic lipid membranes
    • Montich, G. G. (2000). Partly folded states of bovine carbonic anhydrase interact with zwitterionic and anionic lipid membranes. Biochimica et Biophysica Acta, 1468, 115-126.
    • (2000) Biochimica et Biophysica Acta , vol.1468 , pp. 115-126
    • Montich, G.G.1
  • 14
  • 15
    • 0024276839 scopus 로고
    • A Fourier-transform spectroscopic study of the phosphoserine residues in hen egg phosvitin and ovalbumin
    • Sanchez-Ruiz, J. M., & Martinez-Carrion, M. (1988). A Fourier-transform spectroscopic study of the phosphoserine residues in hen egg phosvitin and ovalbumin. Biochemistry, 27, 3338-3342.
    • (1988) Biochemistry , vol.27 , pp. 3338-3342
    • Sanchez-Ruiz, J.M.1    Martinez-Carrion, M.2
  • 16
    • 0027504517 scopus 로고
    • Relation between the physicochemical characteristics of collagen and its interactions with chitosan: I
    • Taravel, M. N., & Domard, A. (1993). Relation between the physicochemical characteristics of collagen and its interactions with chitosan: I. Biomaterials, 14, 930-938.
    • (1993) Biomaterials , vol.14 , pp. 930-938
    • Taravel, M.N.1    Domard, A.2
  • 17
    • 0029029479 scopus 로고
    • Collagen and its interactions with chitosan: II influence of the physicochemical characteristics of collagen
    • Taravel, M. N., & Domard, A. (1995). Collagen and its interactions with chitosan: II influence of the physicochemical characteristics of collagen. Biomaterials, 16, 865-871.
    • (1995) Biomaterials , vol.16 , pp. 865-871
    • Taravel, M.N.1    Domard, A.2
  • 18
    • 0348050182 scopus 로고    scopus 로고
    • Analysis of modified whole casein with different phosphorous contents using phosphorous-31 nuclear magnetic resonance and Fourier transform infrared spectroscopy
    • van Hekken, D. L., & Dudley, R. L. (1997). Analysis of modified whole casein with different phosphorous contents using phosphorous-31 nuclear magnetic resonance and Fourier transform infrared spectroscopy. Journal of Dairy Science, 80, 2751-2759.
    • (1997) Journal of Dairy Science , vol.80 , pp. 2751-2759
    • Van Hekken, D.L.1    Dudley, R.L.2
  • 19
    • 0345810450 scopus 로고    scopus 로고
    • Rheology and microstructure of chemically superphosphorylated whole casein
    • van Hekken, D. L., & Strange, E. D. (1997). Rheology and microstructure of chemically superphosphorylated whole casein. Journal of Dairy Science, 80, 2740-2750.
    • (1997) Journal of Dairy Science , vol.80 , pp. 2740-2750
    • Van Hekken, D.L.1    Strange, E.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.