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Volumn 63, Issue , 2017, Pages 43-49

The formation of non-heat-treated whey protein cold-set hydrogels via non-toxic chemical cross-linking

Author keywords

Alkali catalyzed; Circular dichroism; Protein conformation; Water holding capacity

Indexed keywords

ALKALINITY; AMINO ACIDS; CATALYSIS; CITRIC ACID; CROSSLINKING; GELATION; PH; PROTEINS; SCANNING ELECTRON MICROSCOPY; TEMPERATURE;

EID: 84983672035     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2016.08.024     Document Type: Article
Times cited : (41)

References (27)
  • 1
  • 2
    • 84911487584 scopus 로고    scopus 로고
    • Transglutaminase-induced or citric acid-mediated cross-linking of whey proteins to tune the characteristics of subsequently desolvated sub-micron and nano-scaled particles
    • Bagheri, L., Yarmand, M., Madadlou, A., Mousavi, M.E., Transglutaminase-induced or citric acid-mediated cross-linking of whey proteins to tune the characteristics of subsequently desolvated sub-micron and nano-scaled particles. Journal of Microencapsulation 31:7 (2014), 636–643.
    • (2014) Journal of Microencapsulation , vol.31 , Issue.7 , pp. 636-643
    • Bagheri, L.1    Yarmand, M.2    Madadlou, A.3    Mousavi, M.E.4
  • 5
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
    • Bryant, C.M., McClements, D.J., Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trends in Food Science & Technology 9:4 (1998), 143–151.
    • (1998) Trends in Food Science & Technology , vol.9 , Issue.4 , pp. 143-151
    • Bryant, C.M.1    McClements, D.J.2
  • 6
    • 27744556217 scopus 로고    scopus 로고
    • Effect of temperature and inoculum concentration on gel microstructure, permeability and syneresis kinetics. Cottage cheese-type gels
    • Castillo, M., Lucey, J.A., Wang, T., Payne, F.A., Effect of temperature and inoculum concentration on gel microstructure, permeability and syneresis kinetics. Cottage cheese-type gels. International Dairy Journal 16 (2006), 153–163.
    • (2006) International Dairy Journal , vol.16 , pp. 153-163
    • Castillo, M.1    Lucey, J.A.2    Wang, T.3    Payne, F.A.4
  • 8
    • 33745609556 scopus 로고    scopus 로고
    • Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTIR spectroscopy
    • Eissa, A.S., Puhl, C., Kadla, J.F., Khan, S.A., Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTIR spectroscopy. Biomacromolecules 7:6 (2006), 1707–1713.
    • (2006) Biomacromolecules , vol.7 , Issue.6 , pp. 1707-1713
    • Eissa, A.S.1    Puhl, C.2    Kadla, J.F.3    Khan, S.A.4
  • 9
    • 84929313931 scopus 로고    scopus 로고
    • Characteristics of the bulk hydrogels made of the citric acid cross-linked whey protein microgels
    • Farjami, T., Madadlou, A., Labbafi, M., Characteristics of the bulk hydrogels made of the citric acid cross-linked whey protein microgels. Food Hydrocolloids 50 (2015), 159–165.
    • (2015) Food Hydrocolloids , vol.50 , pp. 159-165
    • Farjami, T.1    Madadlou, A.2    Labbafi, M.3
  • 10
    • 84891834781 scopus 로고    scopus 로고
    • Synthesis and characterization of citric acid-based pH-sensitive biopolymeric hydrogels
    • Franklin, D.S., Guhanathan, S., Synthesis and characterization of citric acid-based pH-sensitive biopolymeric hydrogels. Polymer Bulletin 71:1 (2014), 93–110.
    • (2014) Polymer Bulletin , vol.71 , Issue.1 , pp. 93-110
    • Franklin, D.S.1    Guhanathan, S.2
  • 11
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N.J., Using circular dichroism spectra to estimate protein secondary structure. Nature Protocols 1:6 (2006), 2876–2890.
    • (2006) Nature Protocols , vol.1 , Issue.6 , pp. 2876-2890
    • Greenfield, N.J.1
  • 12
    • 0040915889 scopus 로고    scopus 로고
    • Effects of lecithin on thermally induced whey protein isolate gels
    • Ikeda, S., Foegeding, E.A., Effects of lecithin on thermally induced whey protein isolate gels. Food Hydrocolloids 13:3 (1999), 239–244.
    • (1999) Food Hydrocolloids , vol.13 , Issue.3 , pp. 239-244
    • Ikeda, S.1    Foegeding, E.A.2
  • 13
    • 0001356218 scopus 로고    scopus 로고
    • Gelation of pH-aggregated whey protein isolate solution induced by heat, protease, calcium salt, and acidulant
    • Ju, Z.Y., Kilara, A., Gelation of pH-aggregated whey protein isolate solution induced by heat, protease, calcium salt, and acidulant. Journal of Agricultural and Food Chemistry 46:5 (1998), 1830–1835.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.5 , pp. 1830-1835
    • Ju, Z.Y.1    Kilara, A.2
  • 15
    • 33745913040 scopus 로고    scopus 로고
    • Microstructure and rheological properties of Iranian White cheese coagulated at various temperatures
    • Madadlou, A., Khosroshahi, A., Mousavi, S.M., Djome, Z.E., Microstructure and rheological properties of Iranian White cheese coagulated at various temperatures. Journal of Dairy Science 89:7 (2006), 2359–2364.
    • (2006) Journal of Dairy Science , vol.89 , Issue.7 , pp. 2359-2364
    • Madadlou, A.1    Khosroshahi, A.2    Mousavi, S.M.3    Djome, Z.E.4
  • 16
    • 18844450965 scopus 로고    scopus 로고
    • Caustic-induced gelation of whey deposits in the alkali cleaning of membranes
    • Mercadé-Prieto, R., Chen, X.D., Caustic-induced gelation of whey deposits in the alkali cleaning of membranes. Journal of Membrane Science 254:1 (2005), 157–167.
    • (2005) Journal of Membrane Science , vol.254 , Issue.1 , pp. 157-167
    • Mercadé-Prieto, R.1    Chen, X.D.2
  • 17
    • 66249139567 scopus 로고    scopus 로고
    • Alkali cold gelation of whey proteins. Part I: Sol− Gel− sol (− gel) transitions
    • Mercadé-Prieto, R., Gunasekaran, S., Alkali cold gelation of whey proteins. Part I: Sol− Gel− sol (− gel) transitions. Langmuir 25:10 (2009), 5785–5792.
    • (2009) Langmuir , vol.25 , Issue.10 , pp. 5785-5792
    • Mercadé-Prieto, R.1    Gunasekaran, S.2
  • 19
    • 0004026407 scopus 로고    scopus 로고
    • Lehninger principles of biochemistry
    • Macmillan
    • Nelson, D.L., Lehninger, A.L., Cox, M.M., Lehninger principles of biochemistry. 2008, Macmillan.
    • (2008)
    • Nelson, D.L.1    Lehninger, A.L.2    Cox, M.M.3
  • 20
    • 79959908730 scopus 로고    scopus 로고
    • Loosening of globular structure under alkaline pH affects accessibility of β-lactoglobulin to tyrosinase-induced oxidation and subsequent cross-linking
    • Partanen, R., Torkkeli, M., Hellman, M., Permi, P., Serimaa, R., Buchert, J., et al. Loosening of globular structure under alkaline pH affects accessibility of β-lactoglobulin to tyrosinase-induced oxidation and subsequent cross-linking. Enzyme and Microbial Technology 49:2 (2011), 131–138.
    • (2011) Enzyme and Microbial Technology , vol.49 , Issue.2 , pp. 131-138
    • Partanen, R.1    Torkkeli, M.2    Hellman, M.3    Permi, P.4    Serimaa, R.5    Buchert, J.6
  • 21
    • 84908627707 scopus 로고    scopus 로고
    • Effect of crosslink density on the water-binding capacity of whey protein microparticles
    • Peters, J.P., Luyten, H., Alting, A.C., Boom, R.M., van der Goot, A.J., Effect of crosslink density on the water-binding capacity of whey protein microparticles. Food Hydrocolloids 44 (2015), 277–284.
    • (2015) Food Hydrocolloids , vol.44 , pp. 277-284
    • Peters, J.P.1    Luyten, H.2    Alting, A.C.3    Boom, R.M.4    van der Goot, A.J.5
  • 22
    • 59849100134 scopus 로고    scopus 로고
    • Wet cross-linking gliadin fibers with citric acid and a quantitative relationship between cross-linking conditions and mechanical properties
    • Reddy, N., Li, Y., Yang, Y., Wet cross-linking gliadin fibers with citric acid and a quantitative relationship between cross-linking conditions and mechanical properties. Journal of Agricultural and Food Chemistry 57 (2009), 90–98.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 90-98
    • Reddy, N.1    Li, Y.2    Yang, Y.3
  • 23
    • 84930205253 scopus 로고    scopus 로고
    • Low-temperature crosslinking of proteins using non-toxic citric acid in neutral aqueous medium: Mechanism and kinetic study
    • Xu, H., Shen, L., Xu, L., Yang, Y., Low-temperature crosslinking of proteins using non-toxic citric acid in neutral aqueous medium: Mechanism and kinetic study. Industrial Crops and Products 74 (2015), 234–240.
    • (2015) Industrial Crops and Products , vol.74 , pp. 234-240
    • Xu, H.1    Shen, L.2    Xu, L.3    Yang, Y.4
  • 24
    • 84922442493 scopus 로고    scopus 로고
    • Controlled delivery of hollow corn protein nanoparticles via non-toxic crosslinking: In vivo and drug loading study
    • Xu, H., Shen, L., Xu, L., Yang, Y., Controlled delivery of hollow corn protein nanoparticles via non-toxic crosslinking: In vivo and drug loading study. Biomedical Microdevices 17:1 (2015), 1–8.
    • (2015) Biomedical Microdevices , vol.17 , Issue.1 , pp. 1-8
    • Xu, H.1    Shen, L.2    Xu, L.3    Yang, Y.4
  • 25
    • 84861962627 scopus 로고    scopus 로고
    • Properties and potential medical applications of regenerated casein fibers crosslinked with citric acid
    • Yang, Y., Reddy, N., Properties and potential medical applications of regenerated casein fibers crosslinked with citric acid. International Journal of Biological Macromolecules 51:1 (2012), 37–44.
    • (2012) International Journal of Biological Macromolecules , vol.51 , Issue.1 , pp. 37-44
    • Yang, Y.1    Reddy, N.2
  • 26
    • 84945420671 scopus 로고    scopus 로고
    • Impacts of glucosamine/oligochitosan glycation and cross-linking by transglutaminase on the structure and in vitro antigenicity of whey proteins
    • Zhang, Y.H., Liu, J.Q., Xu, D., Zhao, X.H., Impacts of glucosamine/oligochitosan glycation and cross-linking by transglutaminase on the structure and in vitro antigenicity of whey proteins. International Journal of Dairy Technology 69 (2016), 169–176.
    • (2016) International Journal of Dairy Technology , vol.69 , pp. 169-176
    • Zhang, Y.H.1    Liu, J.Q.2    Xu, D.3    Zhao, X.H.4
  • 27
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou, H.X., Rivas, G., Minton, A.P., Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences. Annual Review of Biophysics, 37, 2008, 375.
    • (2008) Annual Review of Biophysics , vol.37 , pp. 375
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.