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Volumn 116, Issue , 2019, Pages 283-290

Solubility and aggregation behavior of protein fractions from the heterotrophically cultivated microalga Chlorella protothecoides

Author keywords

Beverage; Chlorella; Food; Microalgae; Protein; Protothecoides; Solubility; Sustainable

Indexed keywords

ALGAE; ALKALINITY; BEVERAGES; FOOD PRODUCTS; PH; PHASE SEPARATION; SOLUBILITY;

EID: 85052061310     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2018.08.037     Document Type: Article
Times cited : (50)

References (47)
  • 1
    • 37549044716 scopus 로고    scopus 로고
    • Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: Application to apo calmodulin
    • André I., Linse, S., Mulder, F.A.A., Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: Application to apo calmodulin. Journal of the American Chemical Society 129:51 (2007), 15805–15813, 10.1021/ja0721824.
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.51 , pp. 15805-15813
    • André, I.1    Linse, S.2    Mulder, F.A.A.3
  • 2
    • 0022322069 scopus 로고
    • Theory of protein solubility
    • W.H. Wyckoff C.H.W. Hirs S.N. Timasheff Academic Press Cambridge, USA
    • Arakawa, T., Timasheff, S.N., Theory of protein solubility. Wyckoff, W.H., Hirs, C.H.W., Timasheff, S.N., (eds.) Methods in Enzymology, 114, 1985, Academic Press, Cambridge, USA, 49–77.
    • (1985) Methods in Enzymology , vol.114 , pp. 49-77
    • Arakawa, T.1    Timasheff, S.N.2
  • 3
    • 33846502109 scopus 로고    scopus 로고
    • Micro-algae as a source of protein
    • Becker, E.W., Micro-algae as a source of protein. Biotechnology Advances 25:2 (2007), 207–210, 10.1016/j.biotechadv.2006.11.002.
    • (2007) Biotechnology Advances , vol.25 , Issue.2 , pp. 207-210
    • Becker, E.W.1
  • 4
    • 0026046693 scopus 로고
    • The amino-acid and sugar composition of 16 species of microalgae used in mariculture
    • Brown, M.R., The amino-acid and sugar composition of 16 species of microalgae used in mariculture. Journal of Experimental Marine Biology and Ecology 145:1 (1991), 79–99, 10.1016/0022-0981(91)90007-J.
    • (1991) Journal of Experimental Marine Biology and Ecology , vol.145 , Issue.1 , pp. 79-99
    • Brown, M.R.1
  • 5
    • 0002789867 scopus 로고
    • Biochemical composition of microalgae from the green algal classes Chlorophyceae and Prasinophyceae. 1. Amino acids, sugars and pigments
    • Brown, M.R., Jeffrey, S.W., Biochemical composition of microalgae from the green algal classes Chlorophyceae and Prasinophyceae. 1. Amino acids, sugars and pigments. Journal of Experimental Marine Biology and Ecology 161:1 (1992), 91–113, 10.1016/0022-0981(92)90192-D.
    • (1992) Journal of Experimental Marine Biology and Ecology , vol.161 , Issue.1 , pp. 91-113
    • Brown, M.R.1    Jeffrey, S.W.2
  • 6
    • 80052710281 scopus 로고    scopus 로고
    • The impact of cell wall carbohydrate composition on the chitosan flocculation of Chlorella
    • Cheng, Y.-S., Zheng, Y., Labavitch, J.M., Vandergheynst, J.S., The impact of cell wall carbohydrate composition on the chitosan flocculation of Chlorella. Process Biochemistry 46:10 (2011), 1927–1933, 10.1016/j.procbio.2011.06.021.
    • (2011) Process Biochemistry , vol.46 , Issue.10 , pp. 1927-1933
    • Cheng, Y.-S.1    Zheng, Y.2    Labavitch, J.M.3    Vandergheynst, J.S.4
  • 7
    • 33947617349 scopus 로고    scopus 로고
    • Biodiesel from microalgae
    • Chisti, Y., Biodiesel from microalgae. Biotechnology Advances 25:3 (2007), 294–306, 10.1016/j.biotechadv.2007.02.001.
    • (2007) Biotechnology Advances , vol.25 , Issue.3 , pp. 294-306
    • Chisti, Y.1
  • 8
    • 0035007012 scopus 로고    scopus 로고
    • Emulsifying properties of soy protein isolate fractions obtained by isoelectric precipitation
    • Chove, B.E., Grandison, A.S., Lewis, M.J., Emulsifying properties of soy protein isolate fractions obtained by isoelectric precipitation. Journal of the Science of Food and Agriculture 81:8 (2001), 759–763, 10.1002/jsfa.877.
    • (2001) Journal of the Science of Food and Agriculture , vol.81 , Issue.8 , pp. 759-763
    • Chove, B.E.1    Grandison, A.S.2    Lewis, M.J.3
  • 9
    • 84997719778 scopus 로고    scopus 로고
    • The interaction between zein and lecithin in ethanol-water solution and characterization of zein–lecithin composite colloidal nanoparticles
    • Dai, L., Sun, C., Wang, D., Gao, Y., The interaction between zein and lecithin in ethanol-water solution and characterization of zein–lecithin composite colloidal nanoparticles. PLoS One, 11(11), 2016, 10.1371/journal.pone.0167172.
    • (2016) PLoS One , vol.11 , Issue.11
    • Dai, L.1    Sun, C.2    Wang, D.3    Gao, Y.4
  • 11
    • 85052128450 scopus 로고    scopus 로고
    • Livestock solutions for climate change
    • FAO Rome
    • FAO, Livestock solutions for climate change. 2017, FAO, Rome.
    • (2017)
    • FAO1
  • 14
    • 84875077648 scopus 로고    scopus 로고
    • Optimizing protein isolation from defatted and non-defatted Nannochloropsis microalgae biomass
    • Gerde, J.A., Wang, T., Yao, L., Jung, S., Johnson, L.A., Lamsal, B., Optimizing protein isolation from defatted and non-defatted Nannochloropsis microalgae biomass. Algal Research 2:2 (2013), 145–153, 10.1016/j.algal.2013.02.001.
    • (2013) Algal Research , vol.2 , Issue.2 , pp. 145-153
    • Gerde, J.A.1    Wang, T.2    Yao, L.3    Jung, S.4    Johnson, L.A.5    Lamsal, B.6
  • 15
    • 85037377632 scopus 로고    scopus 로고
    • Effect of precipitation, lyophilization, and organic solvent extraction on preparation of protein-rich powders from the microalgae Chlorella protothecoides
    • Grossmann, L., Ebert, S., Hinrichs, J., Weiss, J., Effect of precipitation, lyophilization, and organic solvent extraction on preparation of protein-rich powders from the microalgae Chlorella protothecoides. Algal Research 29 (2018), 266–276, 10.1016/j.algal.2017.11.019.
    • (2018) Algal Research , vol.29 , pp. 266-276
    • Grossmann, L.1    Ebert, S.2    Hinrichs, J.3    Weiss, J.4
  • 16
    • 84986296959 scopus 로고    scopus 로고
    • Accessibility of transglutaminase to induce protein crosslinking in gelled food matrices - Influence of network structure
    • Grossmann, L., Wefers, D., Bunzel, M., Weiss, J., Zeeb, B., Accessibility of transglutaminase to induce protein crosslinking in gelled food matrices - Influence of network structure. LWT - Food Science and Technology 75 (2017), 271–278, 10.1016/j.lwt.2016.09.005.
    • (2017) LWT - Food Science and Technology , vol.75 , pp. 271-278
    • Grossmann, L.1    Wefers, D.2    Bunzel, M.3    Weiss, J.4    Zeeb, B.5
  • 17
    • 84863849291 scopus 로고    scopus 로고
    • Graininess in fresh cheese as affected by post-processing: Influence of tempering and mechanical treatment
    • Hahn, C., Wachter, T., Nöbel, S., Weiss, J., Eibel, H., Hinrichs, J., Graininess in fresh cheese as affected by post-processing: Influence of tempering and mechanical treatment. International Dairy Journal 26:1 (2012), 73–77, 10.1016/j.idairyj.2011.12.013.
    • (2012) International Dairy Journal , vol.26 , Issue.1 , pp. 73-77
    • Hahn, C.1    Wachter, T.2    Nöbel, S.3    Weiss, J.4    Eibel, H.5    Hinrichs, J.6
  • 19
    • 0018801110 scopus 로고
    • Precipitation of egg white proteins below their isoelectric points by sodium dodecyl sulphate and temperature
    • Hegg, P.-O., Precipitation of egg white proteins below their isoelectric points by sodium dodecyl sulphate and temperature. Biochimica et Biophysica Acta (BBA) - Protein Structure 579:1 (1979), 73–87, 10.1016/0005-2795(79)90088-6.
    • (1979) Biochimica et Biophysica Acta (BBA) - Protein Structure , vol.579 , Issue.1 , pp. 73-87
    • Hegg, P.-O.1
  • 21
    • 84859910800 scopus 로고    scopus 로고
    • Toward a molecular understanding of protein solubility: Increased negative surface charge correlates with increased solubility
    • Kramer, R.M., Shende, V.R., Motl, N., Pace, C.N., Scholtz, J.M., Toward a molecular understanding of protein solubility: Increased negative surface charge correlates with increased solubility. Biophysical Journal 102:8 (2012), 1907–1915, 10.1016/j.bpj.2012.01.060.
    • (2012) Biophysical Journal , vol.102 , Issue.8 , pp. 1907-1915
    • Kramer, R.M.1    Shende, V.R.2    Motl, N.3    Pace, C.N.4    Scholtz, J.M.5
  • 22
    • 0000740914 scopus 로고
    • Kurze Charakteristik einiger niedrerer Organismen im Saftfluss der Laubbäume
    • Krüger, W., Kurze Charakteristik einiger niedrerer Organismen im Saftfluss der Laubbäume. Hedwigia 33 (1894), 241–266.
    • (1894) Hedwigia , vol.33 , pp. 241-266
    • Krüger, W.1
  • 23
    • 74249106759 scopus 로고    scopus 로고
    • Ingredients and pH are key to clear beverages that contain whey protein
    • Laclair, C.E., Etzel, M.R., Ingredients and pH are key to clear beverages that contain whey protein. Journal of Food Science 75:1 (2010), 21–27, 10.1111/j.1750-3841.2009.01400.x.
    • (2010) Journal of Food Science , vol.75 , Issue.1 , pp. 21-27
    • Laclair, C.E.1    Etzel, M.R.2
  • 24
    • 84878310546 scopus 로고    scopus 로고
    • Food proteins: A review on their emulsifying properties using a structure–function approach
    • Lam, R.S.H., Nickerson, M.T., Food proteins: A review on their emulsifying properties using a structure–function approach. Food Chemistry 141:2 (2013), 975–984, 10.1016/j.foodchem.2013.04.038.
    • (2013) Food Chemistry , vol.141 , Issue.2 , pp. 975-984
    • Lam, R.S.H.1    Nickerson, M.T.2
  • 25
    • 85044360219 scopus 로고    scopus 로고
    • Pea protein isolate–high methoxyl pectin soluble complexes for improving pea protein functionality: Effect of pH, biopolymer ratio and concentrations
    • Lan, Y., Chen, B., Rao, J., Pea protein isolate–high methoxyl pectin soluble complexes for improving pea protein functionality: Effect of pH, biopolymer ratio and concentrations. Food Hydrocolloids 80 (2018), 245–253, 10.1016/j.foodhyd.2018.02.021.
    • (2018) Food Hydrocolloids , vol.80 , pp. 245-253
    • Lan, Y.1    Chen, B.2    Rao, J.3
  • 26
    • 84957604083 scopus 로고    scopus 로고
    • Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin
    • Li, R., Wu, Z., Wangb, Y., Ding, L., Wang, Y., Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin. Biotechnology Reports 9 (2016), 46–52, 10.1016/j.btre.2016.01.002.
    • (2016) Biotechnology Reports , vol.9 , pp. 46-52
    • Li, R.1    Wu, Z.2    Wangb, Y.3    Ding, L.4    Wang, Y.5
  • 28
    • 33751553722 scopus 로고
    • Nitrogen-to-protein conversion factor for ten cereals and six legumes or oilseeds. A reappraisal of its definition and determination. Variation according to species and to seed protein content
    • Mosse, J., Nitrogen-to-protein conversion factor for ten cereals and six legumes or oilseeds. A reappraisal of its definition and determination. Variation according to species and to seed protein content. Journal of Agricultural and Food Chemistry 38:1 (1990), 18–24.
    • (1990) Journal of Agricultural and Food Chemistry , vol.38 , Issue.1 , pp. 18-24
    • Mosse, J.1
  • 29
    • 85020120389 scopus 로고    scopus 로고
    • Enhancement of the functional properties of whey protein by conjugation with maltodextrin under dry-heating conditions
    • Mulcahy, E.M., Park, C.W., Drake, M., Mulvihill, D.M., O'Mahony, J.A., Enhancement of the functional properties of whey protein by conjugation with maltodextrin under dry-heating conditions. International Journal of Dairy Technology 71:1 (2018), 216–225, 10.1111/1471-0307.12411.
    • (2018) International Journal of Dairy Technology , vol.71 , Issue.1 , pp. 216-225
    • Mulcahy, E.M.1    Park, C.W.2    Drake, M.3    Mulvihill, D.M.4    O'Mahony, J.A.5
  • 30
    • 0000918115 scopus 로고    scopus 로고
    • Analysis of particle sizes, concentration, and refractive index in measurement of light transmittance in the forward-scattering-angle range
    • Nefedov, A.P., Petrov, O.F., Vaulina, O.S., Analysis of particle sizes, concentration, and refractive index in measurement of light transmittance in the forward-scattering-angle range. Applied Optics 36:6 (1997), 1357–1366.
    • (1997) Applied Optics , vol.36 , Issue.6 , pp. 1357-1366
    • Nefedov, A.P.1    Petrov, O.F.2    Vaulina, O.S.3
  • 31
    • 84858954599 scopus 로고    scopus 로고
    • Effect of temperature and pH on the solubility of caseins: Environmental influences on the dissociation of αS- and β-casein
    • Post, A.E., Arnold, B., Weiss, J., Hinrichs, J., Effect of temperature and pH on the solubility of caseins: Environmental influences on the dissociation of αS- and β-casein. Journal of Dairy Science 95:4 (2012), 1603–1616, 10.3168/jds.2011-4641.
    • (2012) Journal of Dairy Science , vol.95 , Issue.4 , pp. 1603-1616
    • Post, A.E.1    Arnold, B.2    Weiss, J.3    Hinrichs, J.4
  • 32
    • 1642276288 scopus 로고    scopus 로고
    • Linear regression approach to study amino acid digestibility in broiler chickens
    • Rodehutscord, M., Kapocius, M., Timmler, R., Dieckmann, A., Linear regression approach to study amino acid digestibility in broiler chickens. British Poultry Science 45:1 (2004), 85–92, 10.1080/00071660410001668905.
    • (2004) British Poultry Science , vol.45 , Issue.1 , pp. 85-92
    • Rodehutscord, M.1    Kapocius, M.2    Timmler, R.3    Dieckmann, A.4
  • 33
    • 84882952135 scopus 로고    scopus 로고
    • Effect of charged polysaccharides on the techno-functional properties of fractions obtained from algae soluble protein isolate
    • Schwenzfeier, A., Wierenga, P.A., Eppink, M.H.M., Gruppen, H., Effect of charged polysaccharides on the techno-functional properties of fractions obtained from algae soluble protein isolate. Food Hydrocolloids 35 (2014), 9–18, 10.1016/j.foodhyd.2013.07.019.
    • (2014) Food Hydrocolloids , vol.35 , pp. 9-18
    • Schwenzfeier, A.1    Wierenga, P.A.2    Eppink, M.H.M.3    Gruppen, H.4
  • 34
    • 80052390254 scopus 로고    scopus 로고
    • Isolation and characterization of soluble protein from the green microalgae Tetraselmis sp
    • Schwenzfeier, A., Wierenga, P.A., Gruppen, H., Isolation and characterization of soluble protein from the green microalgae Tetraselmis sp. Bioresource Technology 102:19 (2011), 9121–9127, 10.1016/j.biortech.2011.07.046.
    • (2011) Bioresource Technology , vol.102 , Issue.19 , pp. 9121-9127
    • Schwenzfeier, A.1    Wierenga, P.A.2    Gruppen, H.3
  • 36
    • 67449119292 scopus 로고    scopus 로고
    • Effects of Glycosylation on the Stability of Protein Pharmaceuticals
    • Sola, R.J., Griebenow, K., Effects of Glycosylation on the Stability of Protein Pharmaceuticals. Journal of Pharmaceutical Sciences 98:4 (2009), 1223–1245.
    • (2009) Journal of Pharmaceutical Sciences , vol.98 , Issue.4 , pp. 1223-1245
    • Sola, R.J.1    Griebenow, K.2
  • 37
    • 0036077429 scopus 로고    scopus 로고
    • Whey protein aggregation under shear conditions – effects of pH-value and removal of calcium
    • Spiegel, T., Huss, M., Whey protein aggregation under shear conditions – effects of pH-value and removal of calcium. International Journal of Food Science & Technology 37:5 (2002), 559–568, 10.1046/j.1365-2621.2002.00612.x.
    • (2002) International Journal of Food Science & Technology , vol.37 , Issue.5 , pp. 559-568
    • Spiegel, T.1    Huss, M.2
  • 38
    • 84985214215 scopus 로고
    • Production and evaluation of pea protein isolate
    • Sumner, A.K., Nielsen, M.A., Youngs, C.G., Production and evaluation of pea protein isolate. Journal of Food Science 46:2 (1981), 364–366, 10.1111/j.1365-2621.1981.tb04862.x.
    • (1981) Journal of Food Science , vol.46 , Issue.2 , pp. 364-366
    • Sumner, A.K.1    Nielsen, M.A.2    Youngs, C.G.3
  • 39
    • 84879449977 scopus 로고    scopus 로고
    • Safety evaluation of whole algalin protein (WAP) from Chlorella protothecoides
    • Szabo, N.J., Matulka, R.A., Chan, T., Safety evaluation of whole algalin protein (WAP) from Chlorella protothecoides. Food and Chemical Toxicology 59 (2013), 34–45, 10.1016/j.fct.2013.05.035.
    • (2013) Food and Chemical Toxicology , vol.59 , pp. 34-45
    • Szabo, N.J.1    Matulka, R.A.2    Chan, T.3
  • 40
    • 84981870950 scopus 로고
    • Effect of temperature and pH on the soluble proteins of Ham
    • Trautman, J.C., Effect of temperature and pH on the soluble proteins of Ham. Journal of Food Science 31:3 (1966), 409–418, 10.1111/j.1365-2621.1966.tb00514.x.
    • (1966) Journal of Food Science , vol.31 , Issue.3 , pp. 409-418
    • Trautman, J.C.1
  • 41
    • 84885703108 scopus 로고    scopus 로고
    • Safety of novel protein sources (insects, microalgae, seaweed, duckweed, and rapeseed) and legislative aspects for their application in food and feed production
    • Van der Spiegel, M., Noordam, M.y., Van der Fels-Klerx, H.j., Safety of novel protein sources (insects, microalgae, seaweed, duckweed, and rapeseed) and legislative aspects for their application in food and feed production. Comprehensive Reviews in Food Science and Food Safety 12:6 (2013), 662–678, 10.1111/1541-4337.12032.
    • (2013) Comprehensive Reviews in Food Science and Food Safety , vol.12 , Issue.6 , pp. 662-678
    • Van der Spiegel, M.1    Noordam, M.Y.2    Van der Fels-Klerx, H.J.3
  • 43
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D., Flügge, U.I., A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Analytical Biochemistry 138:1 (1984), 141–143, 10.1016/0003-2697(84)90782-6.
    • (1984) Analytical Biochemistry , vol.138 , Issue.1 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 44
    • 33750374202 scopus 로고    scopus 로고
    • High quality biodiesel production from a microalga Chlorella protothecoides by heterotrophic growth in fermenters
    • Xu, H., Miao, X., Wu, Q., High quality biodiesel production from a microalga Chlorella protothecoides by heterotrophic growth in fermenters. Journal of Biotechnology 126:4 (2006), 499–507, 10.1016/j.jbiotec.2006.05.002.
    • (2006) Journal of Biotechnology , vol.126 , Issue.4 , pp. 499-507
    • Xu, H.1    Miao, X.2    Wu, Q.3
  • 45
    • 0004248423 scopus 로고    scopus 로고
    • Functionality of Proteins in Food
    • Springer Science & Business Media Berlin
    • Zayas, J.F., Functionality of Proteins in Food. 1996, Springer Science & Business Media, Berlin.
    • (1996)
    • Zayas, J.F.1
  • 46
    • 84963784679 scopus 로고    scopus 로고
    • Accessibility of transglutaminase to induce protein crosslinking in gelled food matrices - impact of membrane structure
    • Zeeb, B., Grossmann, L., Weiss, J., Accessibility of transglutaminase to induce protein crosslinking in gelled food matrices - impact of membrane structure. Food Biophysics 11:2 (2016), 176–183, 10.1007/s11483-016-9428-5.
    • (2016) Food Biophysics , vol.11 , Issue.2 , pp. 176-183
    • Zeeb, B.1    Grossmann, L.2    Weiss, J.3
  • 47
    • 33751158541 scopus 로고
    • Heat-induced conformational changes in whey protein isolate and its relation to foaming properties
    • Zhu, H., Damodaran, S., Heat-induced conformational changes in whey protein isolate and its relation to foaming properties. Journal of Agricultural and Food Chemistry 42:4 (1994), 846–855, 10.1021/jf00040a002.
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , Issue.4 , pp. 846-855
    • Zhu, H.1    Damodaran, S.2


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