메뉴 건너뛰기




Volumn 63, Issue 1, 2015, Pages 562-568

Partial replacement of β-casein by napin, a rapeseed protein, as ingredient for processed foods: Thermoreversible aggregation

Author keywords

Aggregation; Calcium; Casein; Napin; Plant protein

Indexed keywords

AGGLOMERATION; AMINES; CALCIUM; CASEIN; CHELATION; DAIRIES; DIGITAL STORAGE; ETHYLENE; OILSEEDS; PHYSICOCHEMICAL PROPERTIES; PROCESSED FOODS; SODIUM CHLORIDE;

EID: 84928699677     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2015.03.084     Document Type: Article
Times cited : (26)

References (34)
  • 4
    • 33947111877 scopus 로고    scopus 로고
    • The poor digestibility of rapeseed protein is balanced by its very high metabolic utilization in humans
    • Bos C., Airinei G., Mariotti F., Benamouzig R., Berot S., Evrard J., et al. The poor digestibility of rapeseed protein is balanced by its very high metabolic utilization in humans. Journal of Nutrition 2007, 137(3):597-600.
    • (2007) Journal of Nutrition , vol.137 , Issue.3 , pp. 597-600
    • Bos, C.1    Airinei, G.2    Mariotti, F.3    Benamouzig, R.4    Berot, S.5    Evrard, J.6
  • 6
    • 0013429814 scopus 로고
    • Role of electrostatic forces in the interaction of soy proteins with lysozyme
    • Damodaran S., Kinsella J.E. Role of electrostatic forces in the interaction of soy proteins with lysozyme. Cereal Chemistry 1986, 63(5):381-383.
    • (1986) Cereal Chemistry , vol.63 , Issue.5 , pp. 381-383
    • Damodaran, S.1    Kinsella, J.E.2
  • 10
    • 0035146503 scopus 로고    scopus 로고
    • Milk protein interfacial layers and the relationships to emulsion stability and rheology
    • Dickinson E. Milk protein interfacial layers and the relationships to emulsion stability and rheology. Colloids and Surfaces B: Biointerfaces 2001, 20:197-210.
    • (2001) Colloids and Surfaces B: Biointerfaces , vol.20 , pp. 197-210
    • Dickinson, E.1
  • 11
    • 84928701255 scopus 로고    scopus 로고
    • Chapter 3: feeding the world
    • FAO, Rome, Avalaible at
    • FAO Chapter 3: feeding the world. FAO Statistical YearBook 2013 2013, FAO, Rome, Avalaible at. http://www.fao.org/docrep/018/i3107e/i3107e.PDF.
    • (2013) FAO Statistical YearBook 2013
  • 12
    • 0030291941 scopus 로고    scopus 로고
    • Assignment of the disulfide bonds in napin, a seed storage protein from Brassica napus, using matrix-assisted laser desorption ionization mass spectrometry
    • Gehrig P.M., Biemann K. Assignment of the disulfide bonds in napin, a seed storage protein from Brassica napus, using matrix-assisted laser desorption ionization mass spectrometry. Peptide Research 1996, 9(6):308-314.
    • (1996) Peptide Research , vol.9 , Issue.6 , pp. 308-314
    • Gehrig, P.M.1    Biemann, K.2
  • 14
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: casting light on the black boxes, the structure in dairy products
    • Horne D.S. Casein interactions: casting light on the black boxes, the structure in dairy products. International Dairy Journal 1998, 8(3):171-177.
    • (1998) International Dairy Journal , vol.8 , Issue.3 , pp. 171-177
    • Horne, D.S.1
  • 15
    • 0016908045 scopus 로고
    • Heat-induced complex-formation between myosin and soybean 7S globulins
    • King N.L. Heat-induced complex-formation between myosin and soybean 7S globulins. Journal of Agricultural and Food Chemistry 1977, 25:166-171.
    • (1977) Journal of Agricultural and Food Chemistry , vol.25 , pp. 166-171
    • King, N.L.1
  • 16
    • 0003918425 scopus 로고
    • Protein interactions. An overview
    • VCH, Weinheim, H. Visser (Ed.)
    • Koning M.M.G., Visser H. Protein interactions. An overview. Protein interactions 1992, 1-24. VCH, Weinheim. H. Visser (Ed.).
    • (1992) Protein interactions , pp. 1-24
    • Koning, M.M.G.1    Visser, H.2
  • 17
    • 0034988471 scopus 로고    scopus 로고
    • Behaviou of a protein isolate from rapeseed (Brassica napus) and its main protein components - globulin and albumin - at air/solution and solid interfaces, and in emulsions
    • Krause J.-P., Schwenke K.D. Behaviou of a protein isolate from rapeseed (Brassica napus) and its main protein components - globulin and albumin - at air/solution and solid interfaces, and in emulsions. Colloids and Surfaces B: Biointerfaces 2001, 21(1-3):201-204.
    • (2001) Colloids and Surfaces B: Biointerfaces , vol.21 , Issue.1-3 , pp. 201-204
    • Krause, J.-P.1    Schwenke, K.D.2
  • 18
    • 1542576762 scopus 로고    scopus 로고
    • The structure and properties of Napin-seed storage protein from rape (Brassica napus L.)
    • Krzyzaniak A., Burova T., Haertle T., Barciszewski J. The structure and properties of Napin-seed storage protein from rape (Brassica napus L.). Nahrung-Food 1998, 42(3-4):201-204.
    • (1998) Nahrung-Food , vol.42 , Issue.3-4 , pp. 201-204
    • Krzyzaniak, A.1    Burova, T.2    Haertle, T.3    Barciszewski, J.4
  • 19
    • 0031548175 scopus 로고    scopus 로고
    • Interactions in micellar solutions of β-casein
    • (see also pages 207-209)
    • Leclerc E., Calmettes P. Interactions in micellar solutions of β-casein. Physica B 1997, 234-236. (see also pages 207-209).
    • (1997) Physica B , pp. 234-236
    • Leclerc, E.1    Calmettes, P.2
  • 20
    • 0036653008 scopus 로고    scopus 로고
    • Toward sustainable production of protein-rich foods: appraisal of eight crops for Western Europe. PART I. Analysis of the primary links of the production chain
    • Linnemann A.R., Dijkstra D.S. Toward sustainable production of protein-rich foods: appraisal of eight crops for Western Europe. PART I. Analysis of the primary links of the production chain. Critical Reviews in Food Science and Nutrition 2002, 42(4):377-401.
    • (2002) Critical Reviews in Food Science and Nutrition , vol.42 , Issue.4 , pp. 377-401
    • Linnemann, A.R.1    Dijkstra, D.S.2
  • 22
    • 0035270215 scopus 로고    scopus 로고
    • Emulsifying and foaming properties of native and chemically modified peptides from the 2S and 12S proteins of rapeseed (Brassica napus L.)
    • Malabat C., Sanchez-Vioque R., Rabiller C., Gueguen J. Emulsifying and foaming properties of native and chemically modified peptides from the 2S and 12S proteins of rapeseed (Brassica napus L.). Journal of the American Oil Chemists Society 2001, 78(3):235-241.
    • (2001) Journal of the American Oil Chemists Society , vol.78 , Issue.3 , pp. 235-241
    • Malabat, C.1    Sanchez-Vioque, R.2    Rabiller, C.3    Gueguen, J.4
  • 24
    • 0032445176 scopus 로고    scopus 로고
    • Heat-induce gelation properties of salt-soluble muscle proteins as affected by non-meat proteins
    • McCord A., Smyth A.B., O'Neill E.E. Heat-induce gelation properties of salt-soluble muscle proteins as affected by non-meat proteins. Journal of Food Science 1998, 63(4):580-583.
    • (1998) Journal of Food Science , vol.63 , Issue.4 , pp. 580-583
    • McCord, A.1    Smyth, A.B.2    O'Neill, E.E.3
  • 25
    • 79952364480 scopus 로고    scopus 로고
    • Determination of calcium-binding constants of caseins, phosphoserine, citrate and pyrophosphate: a modelling approach using free calcium measurement
    • Mekmene O., Gaucheron F. Determination of calcium-binding constants of caseins, phosphoserine, citrate and pyrophosphate: a modelling approach using free calcium measurement. Food Chemistry 2011, 127:676-682.
    • (2011) Food Chemistry , vol.127 , pp. 676-682
    • Mekmene, O.1    Gaucheron, F.2
  • 26
    • 0002507895 scopus 로고
    • Purification and characterization of proteins from the 2S fraction from seeds for the Brassicaceae family
    • Monsalve R.I., Rodriguez R. Purification and characterization of proteins from the 2S fraction from seeds for the Brassicaceae family. Journal of Experimental Botany 1990, 41(222):89-94.
    • (1990) Journal of Experimental Botany , vol.41 , Issue.222 , pp. 89-94
    • Monsalve, R.I.1    Rodriguez, R.2
  • 27
    • 33846849437 scopus 로고    scopus 로고
    • Temperature affects the supramolecular structures resulting from α-lactalbumin-lysozyme interaction
    • Nigen M., Croguennec T., Renard D., Bouhallab S. Temperature affects the supramolecular structures resulting from α-lactalbumin-lysozyme interaction. Biochemistry 2007, 46:1248-1255.
    • (2007) Biochemistry , vol.46 , pp. 1248-1255
    • Nigen, M.1    Croguennec, T.2    Renard, D.3    Bouhallab, S.4
  • 28
    • 84982066206 scopus 로고
    • Chemical modification of proteins. Part 12. Effect of succinylation on some physic-chemical and functional properties of the albumin fraction from rapeseed
    • Nitecka E., Raab B., Schwenke K.D. Chemical modification of proteins. Part 12. Effect of succinylation on some physic-chemical and functional properties of the albumin fraction from rapeseed. Die Nahrung 1986, 30(10):975-985.
    • (1986) Die Nahrung , vol.30 , Issue.10 , pp. 975-985
    • Nitecka, E.1    Raab, B.2    Schwenke, K.D.3
  • 30
    • 79955791164 scopus 로고    scopus 로고
    • Kinetics and structure during self-assembly of oppositely charged proteins in aqueous solution
    • Salvatore D., Croguennec T., Bouhallab S., Forge V., Nicolai T. Kinetics and structure during self-assembly of oppositely charged proteins in aqueous solution. Biomacromolecules 2011, 12:1920-1926.
    • (2011) Biomacromolecules , vol.12 , pp. 1920-1926
    • Salvatore, D.1    Croguennec, T.2    Bouhallab, S.3    Forge, V.4    Nicolai, T.5
  • 33
    • 0002772383 scopus 로고
    • Chemistry of the caseins
    • Elsevier Applied Science, London, P.F. Fox (Ed.)
    • Swaisgood H.E. Chemistry of the caseins. Advanced dairy chemistry: Proteins 1992, 63-110. Elsevier Applied Science, London. P.F. Fox (Ed.).
    • (1992) Advanced dairy chemistry: Proteins , pp. 63-110
    • Swaisgood, H.E.1
  • 34
    • 0010602249 scopus 로고
    • Egg proteins
    • Academic Press, New York, H. Neurath, K. Bailey (Eds.)
    • Warner R.C. Egg proteins. The proteins 1954, 435-485. Academic Press, New York. H. Neurath, K. Bailey (Eds.).
    • (1954) The proteins , pp. 435-485
    • Warner, R.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.