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Volumn 59, Issue 1, 2011, Pages 241-248

Conformational study of red kidney bean (Phaseolus vulgaris L.) protein isolate (KPI) by tryptophan fluorescence and differential scanning calorimetry

Author keywords

conformational properties; DSC; fluorescence quenching; Red kidney bean protein isolate (KPI); tryptophan fluorescence

Indexed keywords

CONFORMATIONAL PROPERTIES; DSC; FLUORESCENCE QUENCHING; RED KIDNEY BEAN; TRYPTOPHAN FLUORESCENCE;

EID: 78651068611     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf1027608     Document Type: Article
Times cited : (30)

References (46)
  • 1
    • 78651078893 scopus 로고    scopus 로고
    • Food and Agricultural Organization of the United Nations. [Online database] Agriculture Bulletin Board on Data Collection, Dissemination and Quality of Statistics, URL (August 1)
    • Food and Agricultural Organization of the United Nations. [Online database] Agriculture Bulletin Board on Data Collection, Dissemination and Quality of Statistics, URL http//apps.fao.org/cgi-bin/nph-db.pI-subset= agriculture (August 1, 2002).
    • (2002)
  • 2
    • 0002838268 scopus 로고
    • Proteins of some legume seeds: Soybean, pea, fababean and lupin
    • Hudson, F. J. B., Ed. Chapman and Hall: London, U.K
    • Gueguen, I. and Cerletti, P. Proteins of some legume seeds: soybean, pea, fababean and lupin. In New and Developing Sources of Food Proteins; Hudson, F. J. B., Ed.; Chapman and Hall: London, U.K., 1994; pp 145 - 193.
    • (1994) New and Developing Sources of Food Proteins , pp. 145-193
    • Gueguen, I.1    Cerletti, P.2
  • 3
    • 0035990272 scopus 로고    scopus 로고
    • Dry bean protein functionality
    • Sathe, S. K. Dry bean protein functionality Crit. Rev. Biotechnol. 2002, 22, 175-223
    • (2002) Crit. Rev. Biotechnol. , vol.22 , pp. 175-223
    • Sathe, S.K.1
  • 4
    • 33751386004 scopus 로고
    • Thermal and surface active properties of citric acid-extracted and alkali-extracted proteins from Phaseolus beans
    • Di Lollo, A.; Alli, I.; Biliarderis, C.; Barthakuri, N. Thermal and surface active properties of citric acid-extracted and alkali-extracted proteins from Phaseolus beans J. Agric. Food Chem. 1993, 41, 24-29
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 24-29
    • Di Lollo, A.1    Alli, I.2    Biliarderis, C.3    Barthakuri, N.4
  • 6
    • 43449126795 scopus 로고    scopus 로고
    • Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: Effect of high-pressure treatment
    • Yin, S. W.; Tang, C. H.; Wen, Q. B.; Yang, X. Q.; Li, L. Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: effect of high-pressure treatment Food Chem. 2008, 110, 938-945
    • (2008) Food Chem. , vol.110 , pp. 938-945
    • Yin, S.W.1    Tang, C.H.2    Wen, Q.B.3    Yang, X.Q.4    Li, L.5
  • 7
    • 0001719005 scopus 로고
    • Heritable variation in a polypeptide subunit of the major storage protein of the bean, Phaseolus vulgaris L
    • Romero, J.; Sun, S. M.; McLeester, R. C.; Bliss, F. A.; Hall, T. C. Heritable variation in a polypeptide subunit of the major storage protein of the bean, Phaseolus vulgaris L Plant Physiol. 1975, 56, 776-779
    • (1975) Plant Physiol. , vol.56 , pp. 776-779
    • Romero, J.1    Sun, S.M.2    McLeester, R.C.3    Bliss, F.A.4    Hall, T.C.5
  • 8
    • 76749106479 scopus 로고    scopus 로고
    • Functional and conformational properties of phaseolin (Phaseolus vulgris L.) and kidney bean protein isolate: A comparative study
    • Yin, S. W.; Tang, C. H.; Wen, Q. B.; Yang, X. Q.; Li, L. Functional and conformational properties of phaseolin (Phaseolus vulgris L.) and kidney bean protein isolate: a comparative study J. Sci. Food Agric. 2010, 90, 599-607
    • (2010) J. Sci. Food Agric. , vol.90 , pp. 599-607
    • Yin, S.W.1    Tang, C.H.2    Wen, Q.B.3    Yang, X.Q.4    Li, L.5
  • 9
    • 33846291896 scopus 로고    scopus 로고
    • Thermal properties of buckwheat proteins as related to their lipid contents
    • Tang, C. H. Thermal properties of buckwheat proteins as related to their lipid contents Food Res. Int. 2007, 40, 381-387
    • (2007) Food Res. Int. , vol.40 , pp. 381-387
    • Tang, C.H.1
  • 10
    • 58149333536 scopus 로고    scopus 로고
    • Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and French bean with those of soybean - French bean 7S globulin exhibits excellent properties
    • Kimura, A.; Fukuda, T.; Zhang, M.; Motoyama, S.; Maruyama, N.; Utsumi, S. Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and French bean with those of soybean - French bean 7S globulin exhibits excellent properties J. Agric. Food Chem. 2008, 56, 10273-10279
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 10273-10279
    • Kimura, A.1    Fukuda, T.2    Zhang, M.3    Motoyama, S.4    Maruyama, N.5    Utsumi, S.6
  • 11
    • 76349104429 scopus 로고    scopus 로고
    • The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates
    • Yin, S. W.; Tang, C. H.; Wen, Q. B.; Yang, X. Q.; Yuan, D. B. The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates Food Res. Int. 2010, 43, 730-738
    • (2010) Food Res. Int. , vol.43 , pp. 730-738
    • Yin, S.W.1    Tang, C.H.2    Wen, Q.B.3    Yang, X.Q.4    Yuan, D.B.5
  • 12
    • 70449491023 scopus 로고    scopus 로고
    • Effects of acylation on the functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate
    • Yin, S. W.; Tang, C. H.; Wen, Q. B.; Yang, X. Q. Effects of acylation on the functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate J. Food Sci. 2009, 74, E488-494
    • (2009) J. Food Sci. , vol.74 , pp. 488-494
    • Yin, S.W.1    Tang, C.H.2    Wen, Q.B.3    Yang, X.Q.4
  • 13
    • 0031841737 scopus 로고    scopus 로고
    • Methods to monitor process-induced changes in food proteins. An overview
    • Shahidi F., Ho C.T., Chuyen N. Eds.; Plenum Press: New York
    • Li-Chan, E. C. Y. Methods to monitor process-induced changes in food proteins. An overview. In Process-Induced Chemical Changes in Foods; Shahidi, F.; Ho, C. T.; Chuyen, N., Eds.; Plenum Press: New York, 1998; pp 5 - 23.
    • (1998) Process-Induced Chemical Changes in Foods , pp. 5-23
    • Li-Chan, E.C.Y.1
  • 16
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • Pallarès, I.; Vendrell, J.; Avilès, F. X.; Ventura, S. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin J. Mol. Biol. 2004, 342, 321-331
    • (2004) J. Mol. Biol. , vol.342 , pp. 321-331
    • Pallarès, I.1    Vendrell, J.2    Avilès, F.X.3    Ventura, S.4
  • 17
    • 84985232976 scopus 로고
    • Study of thermal properties of oat globulin by differential scanning calorimetry
    • Harwalkar, V. R.; Ma, C. Y. Study of thermal properties of oat globulin by differential scanning calorimetry J. Food Sci. 1987, 52, 394-398
    • (1987) J. Food Sci. , vol.52 , pp. 394-398
    • Harwalkar, V.R.1    Ma, C.Y.2
  • 18
    • 84987277514 scopus 로고
    • Studies of thermal denaturation of oat globulin by differential scanning calorimetry
    • Ma, C. Y.; Harwalkar, V. R. Studies of thermal denaturation of oat globulin by differential scanning calorimetry J. Food Sci. 1988, 53, 531-534
    • (1988) J. Food Sci. , vol.53 , pp. 531-534
    • Ma, C.Y.1    Harwalkar, V.R.2
  • 19
    • 0001441156 scopus 로고    scopus 로고
    • Calorimetric study of soybean protein isolates: Effect of calcium and thermal treatments
    • Scilingo, A. A.; Añón, M. C. Calorimetric study of soybean protein isolates: effect of calcium and thermal treatments J. Agric. Food Chem. 1996, 44, 3751-3756
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 3751-3756
    • Scilingo, A.A.1    Añón, M.C.2
  • 20
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study
    • Boye, J. I.; Alli, I. Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study Food Res. Int. 2000, 33, 673-682
    • (2000) Food Res. Int. , vol.33 , pp. 673-682
    • Boye, J.I.1    Alli, I.2
  • 21
    • 0035036512 scopus 로고    scopus 로고
    • Thermal properties of Phaseolus angularis (red bean) globulin
    • Meng, G. T.; Ma, C. Y. Thermal properties of Phaseolus angularis (red bean) globulin Food Chem. 2001, 23, 453-460
    • (2001) Food Chem. , vol.23 , pp. 453-460
    • Meng, G.T.1    Ma, C.Y.2
  • 22
    • 0036265114 scopus 로고    scopus 로고
    • Thermal analysis of flaxseed (Linum usitatissimum) proteins by differential scanning calorimetry
    • Li-Chan, E. C. Y.; Ma, C. Y. Thermal analysis of flaxseed (Linum usitatissimum) proteins by differential scanning calorimetry Food Chem. 2002, 77, 495-502
    • (2002) Food Chem. , vol.77 , pp. 495-502
    • Li-Chan, E.C.Y.1    Ma, C.Y.2
  • 23
    • 28844481346 scopus 로고    scopus 로고
    • Thermal properties of globulin from rice (Oryza sativa) seeds
    • Ellepola, S. W.; Ma, C. Y. Thermal properties of globulin from rice (Oryza sativa) seeds Food Res. Int. 2006, 39, 257-264
    • (2006) Food Res. Int. , vol.39 , pp. 257-264
    • Ellepola, S.W.1    Ma, C.Y.2
  • 24
    • 27144501099 scopus 로고    scopus 로고
    • Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry
    • Choi, S. M.; Ma, C. Y. Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry J. Agric. Food Chem. 2005, 53, 8046-8053
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 8046-8053
    • Choi, S.M.1    Ma, C.Y.2
  • 25
    • 0041990959 scopus 로고    scopus 로고
    • Metal-enhanced fluorescence
    • Geddes, C. D.; Lakowicz, J. R. Metal-enhanced fluorescence J. Fluoresc. 2002, 12, 121-129
    • (2002) J. Fluoresc. , vol.12 , pp. 121-129
    • Geddes, C.D.1    Lakowicz, J.R.2
  • 26
    • 0028180075 scopus 로고
    • High-pressure effects of β-lactoglobulin interactions with ligands studied by fluorescence
    • Dufour, E.; Hoa, G. H.; Haertlé, T. High-pressure effects of β-lactoglobulin interactions with ligands studied by fluorescence Biochim. Biophys. Acta 1994, 1206, 166-172
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 166-172
    • Dufour, E.1    Hoa, G.H.2    Haertlé, T.3
  • 27
    • 0025827792 scopus 로고
    • Denaturation behavior of phaseolin in urea, guanidine hydrochloride, and sodium dodecyl sulfate solutions
    • Deshpande, S. S.; Damodaran, S. Denaturation behavior of phaseolin in urea, guanidine hydrochloride, and sodium dodecyl sulfate solutions J. Protein Chem. 1991, 10, 103-115
    • (1991) J. Protein Chem. , vol.10 , pp. 103-115
    • Deshpande, S.S.1    Damodaran, S.2
  • 28
    • 0037446864 scopus 로고    scopus 로고
    • The hydration structure of guanidinium and thiocyanate ions: Implications for protein stability in dilute solution
    • Mason, P. E.; Neilson, G. W.; Dempsey, C. E.; Barnes, A. C.; Cruickshank, J. M. The hydration structure of guanidinium and thiocyanate ions: Implications for protein stability in dilute solution Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 4557-4561
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4557-4561
    • Mason, P.E.1    Neilson, G.W.2    Dempsey, C.E.3    Barnes, A.C.4    Cruickshank, J.M.5
  • 29
    • 0036403888 scopus 로고    scopus 로고
    • Use of fluorescence methods to monitor unfolding transitions in β-lactoglobulin
    • Busti, P.; Scarpeci, S.; Gatti, C.; Delorenzi, N. Use of fluorescence methods to monitor unfolding transitions in β-lactoglobulin Food Res. Int. 2002, 35, 871-877
    • (2002) Food Res. Int. , vol.35 , pp. 871-877
    • Busti, P.1    Scarpeci, S.2    Gatti, C.3    Delorenzi, N.4
  • 30
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink, M. R.; Ghiron, C. A. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies Biochemistry 1976, 15, 672-680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 32
    • 3543146731 scopus 로고    scopus 로고
    • Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin
    • Silva, D.; Cortez, C. M.; Louro, S. R. W. Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin Braz. J. Med. Res. 2004, 37, 963-968
    • (2004) Braz. J. Med. Res. , vol.37 , pp. 963-968
    • Silva, D.1    Cortez, C.M.2    Louro, S.R.W.3
  • 33
    • 0023323198 scopus 로고
    • Studies on tryptophan residues of Abrus agglutinin; Stopped-flow kinetics of modification and fluorescence quenching studies
    • Patanjali, S. R.; Swamy, J. M.; Surolia, A. Studies on tryptophan residues of Abrus agglutinin; stopped-flow kinetics of modification and fluorescence quenching studies Biochem. J. 1987, 243, 79-86
    • (1987) Biochem. J. , vol.243 , pp. 79-86
    • Patanjali, S.R.1    Swamy, J.M.2    Surolia, A.3
  • 34
    • 0031687227 scopus 로고    scopus 로고
    • Fluorescence quenching and timeresolved fluorescence studies on Momordica charantia (bitter gourd) seed lectin
    • Padma, P.; Komath, S. S.; Swamy, M. J. Fluorescence quenching and timeresolved fluorescence studies on Momordica charantia (bitter gourd) seed lectin Biochem. Mol. Biol. Int. 1998, 45, 911-922
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 911-922
    • Padma, P.1    Komath, S.S.2    Swamy, M.J.3
  • 35
    • 0038793591 scopus 로고    scopus 로고
    • Surface changes and role of buried water molecules during the sulfane sulfur transfer in Rhodanese from Azotobactor vinelandii: A fluorescence quenching and nuclear magnetic relaxation dispersion spectroscopic study
    • Fasano, M.; Orsale, M.; Melino, S.; Nicolai, E.; Forlani, F.; Rosato, N.; Cicero, D.; Pagani, S.; Paci, M. Surface changes and role of buried water molecules during the sulfane sulfur transfer in Rhodanese from Azotobactor vinelandii: a fluorescence quenching and nuclear magnetic relaxation dispersion spectroscopic study Biochemistry 2003, 42, 8550-8557
    • (2003) Biochemistry , vol.42 , pp. 8550-8557
    • Fasano, M.1    Orsale, M.2    Melino, S.3    Nicolai, E.4    Forlani, F.5    Rosato, N.6    Cicero, D.7    Pagani, S.8    Paci, M.9
  • 36
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • Arakawa, J.; Timasheff, S. N. Preferential interactions of proteins with salts in concentrated solutions Biochemistry 1982, 24, 6545-6552
    • (1982) Biochemistry , vol.24 , pp. 6545-6552
    • Arakawa, J.1    Timasheff, S.N.2
  • 37
    • 70149121260 scopus 로고    scopus 로고
    • Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry
    • Haug, I. J.; Skar, H. M.; Vegarud, G. E.; Langsrud, T.; Draget, K. I. Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry Food Hydrocolloids 2009, 23, 2287-2293
    • (2009) Food Hydrocolloids , vol.23 , pp. 2287-2293
    • Haug, I.J.1    Skar, H.M.2    Vegarud, G.E.3    Langsrud, T.4    Draget, K.I.5
  • 38
    • 0002207547 scopus 로고
    • Relationship between structure and functional properties of food proteins
    • Fox P.F., Cowden J.J. Eds.; Applied Science Publisher: London, U.K
    • Kinsella, J. E. Relationship between structure and functional properties of food proteins. In Food Proteins; Fox, P. F.; Cowden, J. J., Eds.; Applied Science Publisher: London, U.K., 1982; pp 51 - 103.
    • (1982) Food Proteins , pp. 51-103
    • Kinsella, J.E.1
  • 39
    • 0016537698 scopus 로고
    • The role of solvent interactions in protein conformation
    • Franks, F.; England, D. The role of solvent interactions in protein conformation CRC Crit. Rev. Biochem. 1975, 3, 165-21
    • (1975) CRC Crit. Rev. Biochem. , vol.3 , pp. 165-21
    • Franks, F.1    England, D.2
  • 40
    • 37549043949 scopus 로고    scopus 로고
    • Interaction of urea with amino acids: Implications for urea-induced protein denaturation
    • Stumpe, M. C.; Grubmüller, H. Interaction of urea with amino acids: implications for urea-induced protein denaturation J. Am. Chem. Soc. 2007, 129, 16126-16131
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 16126-16131
    • Stumpe, M.C.1    Grubmüller, H.2
  • 41
    • 0015143060 scopus 로고
    • Thermodynamic analysis of thermal transition in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease and myoglobin
    • Privalov, P. L.; Khechinashvili, N. N.; Atanssaov, B. P. Thermodynamic analysis of thermal transition in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease and myoglobin Biopolymers 1971, 10, 1865-1890
    • (1971) Biopolymers , vol.10 , pp. 1865-1890
    • Privalov, P.L.1    Khechinashvili, N.N.2    Atanssaov, B.P.3
  • 42
    • 77950665176 scopus 로고    scopus 로고
    • Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins
    • Colombo, A.; Ribotta, P. D.; León, A. E. Differential scanning calorimetry (DSC) studies on the thermal properties of peanut proteins J. Agric. Food Chem. 2010, 58, 4434-4439
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 4434-4439
    • Colombo, A.1    Ribotta, P.D.2    León, A.E.3
  • 43
    • 0002602653 scopus 로고
    • The nature of specific and non-specific interactions of detergent with protein: Complexing and unfolding
    • Sund H., Blauer G. Eds.; de Gruyter: Berlin, Germany
    • Steinhardt, J. The nature of specific and non-specific interactions of detergent with protein: complexing and unfolding. In Protein-Ligand Interaction; Sund, H.; Blauer, G., Eds.; de Gruyter: Berlin, Germany, 1975; pp 412 - 426.
    • (1975) Protein-Ligand Interaction , pp. 412-426
    • Steinhardt, J.1
  • 45
    • 0032126905 scopus 로고    scopus 로고
    • Influence of naturally acid-soluble proteins from beans (Phaseolus vulgaris L.) on in vitro digestibility determination
    • Genovese, M. I.; Lajol, F. M. Influence of naturally acid-soluble proteins from beans (Phaseolus vulgaris L.) on in vitro digestibility determination Food Chem. 1998, 62, 315-323
    • (1998) Food Chem. , vol.62 , pp. 315-323
    • Genovese, M.I.1    Lajol, F.M.2
  • 46
    • 77957783907 scopus 로고    scopus 로고
    • A comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes: Implications for the structureefunction relationship
    • 324
    • Tang, C. H.; Sun, X. A comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes: Implications for the structureefunction relationship. Food Hydrocolloids 2010, 25, 315 - 324.
    • (2010) Food Hydrocolloids , vol.25 , pp. 315
    • Tang, C.H.1    Sun, X.2


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