메뉴 건너뛰기




Volumn 91, Issue 6, 2011, Pages 1022-1031

Physicochemical, thermal and functional characterisation of protein isolates from Kabuli and Desi chickpea (Cicer arietinum L.): A comparative study with soy (Glycine max) and pea (Pisum sativum L.)

Author keywords

Biotype; Chickpea; Functional properties; Physicochemical; Protein isolates; Soy protein

Indexed keywords

EMULSIFYING AGENT; VEGETABLE OIL; VEGETABLE PROTEIN; WATER;

EID: 79952752991     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.4277     Document Type: Article
Times cited : (130)

References (38)
  • 1
    • 84985200965 scopus 로고
    • Chickpea protein isolates: physicochemical, functional and nutritional characterization
    • Parades-Lopez O, Ordorica-Falmir C and Olivares-Vasquez MR, Chickpea protein isolates: physicochemical, functional and nutritional characterization. J Food Sci 56: 726-729 (1991).
    • (1991) J Food Sci , vol.56 , pp. 726-729
    • Parades-Lopez, O.1    Ordorica-Falmir, C.2    Olivares-Vasquez, M.R.3
  • 3
    • 75149163816 scopus 로고    scopus 로고
    • Characterization of chickpea (Cicer arietinum L.) flours and application in low-fat pork bologna as a model system
    • Sanjeewa WGT, Wanasundara JPD, Pietrasik Z and Shand PJ, Characterization of chickpea (Cicer arietinum L.) flours and application in low-fat pork bologna as a model system. Food Res 43: 617-626 (2010).
    • (2010) Food Res , vol.43 , pp. 617-626
    • Sanjeewa, W.G.T.1    Wanasundara, J.P.D.2    Pietrasik, Z.3    Shand, P.J.4
  • 4
    • 79952754013 scopus 로고    scopus 로고
    • Physico-chemical properties of chickpea flour, starch and protein fractions and their utilization in low-fat pork bologna. MSc Thesis, University of Saskatchewan, Saskatoon
    • Sanjeewa WGT, Physico-chemical properties of chickpea flour, starch and protein fractions and their utilization in low-fat pork bologna. MSc Thesis, University of Saskatchewan, Saskatoon (2008)
    • (2008)
    • Sanjeewa, W.G.T.1
  • 5
    • 0344404404 scopus 로고    scopus 로고
    • Protein isolates from chickpea (Cicer arietinum L.): chemical composition, functional properties and protein characterization
    • Sánchez-Vioque R, Clemente A, Vioque J, Bautista J and Millán F, Protein isolates from chickpea (Cicer arietinum L.): chemical composition, functional properties and protein characterization. Food Chem 64: 237-243 (1999).
    • (1999) Food Chem , vol.64 , pp. 237-243
    • Sánchez-Vioque, R.1    Clemente, A.2    Vioque, J.3    Bautista, J.4    Millán, F.5
  • 6
    • 25444455001 scopus 로고    scopus 로고
    • Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach
    • Yu P, Protein secondary structures (α-helix and β-sheet) at a cellular level and protein fractions in relation to rumen degradation behaviours of protein: a new approach. Br J Nutr 94: 655-665 (2005).
    • (2005) Br J Nutr , vol.94 , pp. 655-665
    • Yu, P.1
  • 7
    • 33751526555 scopus 로고    scopus 로고
    • Characterization of protein isolates from different Indian chickpea (Cicer arietinum L.) cultivars
    • Kaur M and Singh N, Characterization of protein isolates from different Indian chickpea (Cicer arietinum L.) cultivars. Food Chem 102: 366-374 (2006).
    • (2006) Food Chem , vol.102 , pp. 366-374
    • Kaur, M.1    Singh, N.2
  • 9
    • 33846642594 scopus 로고    scopus 로고
    • Physicochemical and textural properties of heat-induced pea protein isolate gels
    • Shand PJ, Ya H, Pietrasik Z and Wanasundara PKJPD, Physicochemical and textural properties of heat-induced pea protein isolate gels. Food Chem 102: 1119-1130 (2007).
    • (2007) Food Chem , vol.102 , pp. 1119-1130
    • Shand, P.J.1    Ya, H.2    Pietrasik, Z.3    Wanasundara, P.K.J.P.D.4
  • 10
    • 0004202155 scopus 로고
    • AOAC, 15th edn). Association of Official Analytical Chemists, Washington, DC.
    • AOAC, Official Methods of Analysis (15th edn). Association of Official Analytical Chemists, Washington, DC (1990).
    • (1990) Official Methods of Analysis
  • 11
    • 29144487201 scopus 로고
    • Preparation of lipid extracts from tissues
    • Christie WW, Preparation of lipid extracts from tissues. Lipid Technol 5: 18-19 (1993).
    • (1993) Lipid Technol , vol.5 , pp. 18-19
    • Christie, W.W.1
  • 12
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: a method for resolving intrinsically overlapped bands
    • Kauppinen JK, Moffatt DJ, Mantsch HH and Comeron DG, Fourier self-deconvolution: a method for resolving intrinsically overlapped bands. Appl Spectrosc 35: 271-276 (1981).
    • (1981) Appl Spectrosc , vol.35 , pp. 271-276
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3    Comeron, D.G.4
  • 13
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler DM and Susi H, Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25: 469-487 (1986).
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 15
    • 28944450583 scopus 로고    scopus 로고
    • Microchemical structure of soybean seeds revealed in situ by ultraspatially resolved synchrotron Fourier transformed infrared microspectroscopy
    • Pietrzak LN and Miller SS, Microchemical structure of soybean seeds revealed in situ by ultraspatially resolved synchrotron Fourier transformed infrared microspectroscopy. J Agric Food Chem 53: 9304-9311 (2005).
    • (2005) J Agric Food Chem , vol.53 , pp. 9304-9311
    • Pietrzak, L.N.1    Miller, S.S.2
  • 16
    • 38849174735 scopus 로고    scopus 로고
    • FTIR spectra studies on the secondary structures of 7S and 11S globulins from soybean proteins using AOT reverse micellar extraction
    • Zhao X, Chen F, Xue W and Lee L, FTIR spectra studies on the secondary structures of 7S and 11S globulins from soybean proteins using AOT reverse micellar extraction. Food Hydrocolloids 22: 568-575 (2008).
    • (2008) Food Hydrocolloids , vol.22 , pp. 568-575
    • Zhao, X.1    Chen, F.2    Xue, W.3    Lee, L.4
  • 17
    • 0036213931 scopus 로고    scopus 로고
    • Thermal gelation of globulin from Phaseolus angularis (red bean)
    • Meng GT and Ma C, Thermal gelation of globulin from Phaseolus angularis (red bean). Food Res Int 35: 377-385 (2002).
    • (2002) Food Res Int , vol.35 , pp. 377-385
    • Meng, G.T.1    Ma, C.2
  • 18
    • 84986533844 scopus 로고
    • Functional properties of winged bean (Psophocarpus tetragonobus L. DC) proteins
    • Sathe SK, Deshpande SS and Salunkhe DK, Functional properties of winged bean (Psophocarpus tetragonobus L. DC) proteins. J Food Sci 47: 503-509 (1982).
    • (1982) J Food Sci , vol.47 , pp. 503-509
    • Sathe, S.K.1    Deshpande, S.S.2    Salunkhe, D.K.3
  • 20
    • 75149150222 scopus 로고    scopus 로고
    • Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques
    • Boye JI, Aksay S, Roufik S, Ribereau S, Mondor M, Farnworth E, et al, Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques. Food Res Int 43: 537-546 (2010).
    • (2010) Food Res Int , vol.43 , pp. 537-546
    • Boye, J.I.1    Aksay, S.2    Roufik, S.3    Ribereau, S.4    Mondor, M.5    Farnworth, E.6
  • 21
    • 84986513624 scopus 로고
    • Functional properties of lupin seed (Lupinus mutabilis) proteins and protein concentrates
    • Sathe SK, Deshpande SS and Salunkhe DK, Functional properties of lupin seed (Lupinus mutabilis) proteins and protein concentrates. J Food Sci 47: 491-497 (1982).
    • (1982) J Food Sci , vol.47 , pp. 491-497
    • Sathe, S.K.1    Deshpande, S.S.2    Salunkhe, D.K.3
  • 23
    • 51249180057 scopus 로고
    • Functional properties of soy proteins
    • Kinsella JE, Functional properties of soy proteins. J Am Oil Chem Soc 56: 940-958 (1979).
    • (1979) J Am Oil Chem Soc , vol.56 , pp. 940-958
    • Kinsella, J.E.1
  • 24
    • 49349130487 scopus 로고
    • Legumin and vicilin, storage proteins of legume seeds
    • Derbyshire S, Wright DJ and Boulter D, Legumin and vicilin, storage proteins of legume seeds. Phytochemistry 15: 3-24 (1976).
    • (1976) Phytochemistry , vol.15 , pp. 3-24
    • Derbyshire, S.1    Wright, D.J.2    Boulter, D.3
  • 25
    • 0036328803 scopus 로고    scopus 로고
    • Texture property of 6 legume curds in relation to their protein constituents
    • Cai R, McCurdy A and Baik BK, Texture property of 6 legume curds in relation to their protein constituents. J Food Sci 67: 1725-1730 (2002).
    • (2002) J Food Sci , vol.67 , pp. 1725-1730
    • Cai, R.1    McCurdy, A.2    Baik, B.K.3
  • 26
    • 0031423685 scopus 로고    scopus 로고
    • Solubility and emulsifying properties of soybean protein isolates modified by pancreatin
    • Qi M, Hettiarchchy NS and Kalapathy U, Solubility and emulsifying properties of soybean protein isolates modified by pancreatin. J Food Sci 62: 1110-1115 (1997).
    • (1997) J Food Sci , vol.62 , pp. 1110-1115
    • Qi, M.1    Hettiarchchy, N.S.2    Kalapathy, U.3
  • 27
    • 0041833728 scopus 로고    scopus 로고
    • Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate
    • Rangel A, Domont G, Pedrosa C and Ferreira S, Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate. J Agric Food Chem 51: 5792-5797 (2003).
    • (2003) J Agric Food Chem , vol.51 , pp. 5792-5797
    • Rangel, A.1    Domont, G.2    Pedrosa, C.3    Ferreira, S.4
  • 28
    • 47849112122 scopus 로고    scopus 로고
    • Emulsifying properties of chickpea protein isolates: influence of pH and NaCl
    • Zhang T, Jiang B, Mu W and Wang Z, Emulsifying properties of chickpea protein isolates: influence of pH and NaCl. Food Hydrocolloids 23: 146-152 (2009).
    • (2009) Food Hydrocolloids , vol.23 , pp. 146-152
    • Zhang, T.1    Jiang, B.2    Mu, W.3    Wang, Z.4
  • 29
    • 14844355902 scopus 로고    scopus 로고
    • Functional properties of protein isolate from cowpea (Vingna unguiculata L. Walp.)
    • Horax R, Hettiarchchy NS, Chen P and Jalaluddin M, Functional properties of protein isolate from cowpea (Vingna unguiculata L. Walp.). J Food Sci 69: 119-121 (2004).
    • (2004) J Food Sci , vol.69 , pp. 119-121
    • Horax, R.1    Hettiarchchy, N.S.2    Chen, P.3    Jalaluddin, M.4
  • 30
    • 70849134948 scopus 로고    scopus 로고
    • Chickpea protein isolates obtained by wet extraction as emulsifying agents
    • Papalamprou EM, Doxastakis GI and Kiosseoglou V, Chickpea protein isolates obtained by wet extraction as emulsifying agents. J Sci Food Agric 90: 304-313 (2010).
    • (2010) J Sci Food Agric , vol.90 , pp. 304-313
    • Papalamprou, E.M.1    Doxastakis, G.I.2    Kiosseoglou, V.3
  • 31
    • 84986736567 scopus 로고
    • Rheological characterization of gels
    • Ross-Murphy SB, Rheological characterization of gels. J Texture Stud 26: 391-400 (1995).
    • (1995) J Texture Stud , vol.26 , pp. 391-400
    • Ross-Murphy, S.B.1
  • 32
    • 0037048720 scopus 로고    scopus 로고
    • Influence of pH and ionic strength on heat-induced formation and rheological properties of soy protein gels in relation to denaturation and their protein compositions
    • Renkema JMS, Gruppen H and Vliet TV, Influence of pH and ionic strength on heat-induced formation and rheological properties of soy protein gels in relation to denaturation and their protein compositions. J Agric Food Chem 50: 6064-6071 (2002).
    • (2002) J Agric Food Chem , vol.50 , pp. 6064-6071
    • Renkema, J.M.S.1    Gruppen, H.2    Vliet, T.V.3
  • 33
    • 0000266715 scopus 로고
    • Network structure formation in thermally induced gelation of glycinin
    • Nakamura T, Utsumi S and Mori T, Network structure formation in thermally induced gelation of glycinin. J Agric Food Chem 32: 349-352 (1984).
    • (1984) J Agric Food Chem , vol.32 , pp. 349-352
    • Nakamura, T.1    Utsumi, S.2    Mori, T.3
  • 34
    • 0000358270 scopus 로고
    • Role of the thermal denaturation-aggregation relationship in determining the rheological properties of heat induced networks for ovalbumin and vicilin
    • Arntfield SD, Murray ED, Ismond MAH and Bernatsky AM, Role of the thermal denaturation-aggregation relationship in determining the rheological properties of heat induced networks for ovalbumin and vicilin. J Food Sci 54: 1624-1631 (1989).
    • (1989) J Food Sci , vol.54 , pp. 1624-1631
    • Arntfield, S.D.1    Murray, E.D.2    Ismond, M.A.H.3    Bernatsky, A.M.4
  • 35
    • 0000579294 scopus 로고
    • The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation
    • Arntfield SD and Murray ED, The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation. Can Inst Food Sci Technol J 14: 289-294 (1981).
    • (1981) Can Inst Food Sci Technol J , vol.14 , pp. 289-294
    • Arntfield, S.D.1    Murray, E.D.2
  • 36
    • 0000425603 scopus 로고    scopus 로고
    • Functional properties of protein concentrates from three Chinese indigenous legume seeds
    • Chau C, Cheung PCK and Wong Y, Functional properties of protein concentrates from three Chinese indigenous legume seeds. J Agric Food Chem 45: 2500-2503 (1997).
    • (1997) J Agric Food Chem , vol.45 , pp. 2500-2503
    • Chau, C.1    Cheung, P.C.K.2    Wong, Y.3
  • 37
    • 51649169160 scopus 로고
    • Protein-water interactions and functional properties
    • Chou DH and Morr CV, Protein-water interactions and functional properties. J Am Oil Chem Soc 56: 53-62 (1979).
    • (1979) J Am Oil Chem Soc , vol.56 , pp. 53-62
    • Chou, D.H.1    Morr, C.V.2
  • 38
    • 0001186821 scopus 로고
    • Functional properties of proteins in foods: possible relationships between structure and function in foams
    • Kinsella JE, Functional properties of proteins in foods: possible relationships between structure and function in foams. Food Chem 7: 273-288 (1981).
    • (1981) Food Chem , vol.7 , pp. 273-288
    • Kinsella, J.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.