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Volumn 97, Issue , 2019, Pages

Adsorption kinetics and foaming properties of soluble microalgae fractions at the air/water interface

Author keywords

Arthrospira platensis isolate; Foam stability; Nanosecond pulsed electric field; Overrun; Whey protein isolate; Zeta potential

Indexed keywords

BIOMASS; ELECTRIC FIELDS; EXTRACTION; MICROORGANISMS; PRODUCTION EFFICIENCY; PROTEINS;

EID: 85068155601     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2019.105182     Document Type: Article
Times cited : (36)

References (48)
  • 1
    • 0017379540 scopus 로고
    • Assessment of growth yield of a blue-green alga, Spirulina platensis, in axenic and continuous culture
    • Aiba, S., Ogawa, T., Assessment of growth yield of a blue-green alga, Spirulina platensis, in axenic and continuous culture. Journal of General Microbiology 102 (1977), 179–182 http://doi.org/10.1099/00221287-102-1-179.
    • (1977) Journal of General Microbiology , vol.102 , pp. 179-182
    • Aiba, S.1    Ogawa, T.2
  • 3
    • 84940676569 scopus 로고    scopus 로고
    • Effect of pH on the functional properties of Arthrospira (Spirulina) platensis protein isolate
    • Benelhadj, S., Gharsallaoui, A., Degraeve, P., Attia, H., Ghorbel, D., Effect of pH on the functional properties of Arthrospira (Spirulina) platensis protein isolate. Food Chemistry 194 (2016), 1056–1063 http://doi.org/10.1016/j.foodchem.2015.08.133.
    • (2016) Food Chemistry , vol.194 , pp. 1056-1063
    • Benelhadj, S.1    Gharsallaoui, A.2    Degraeve, P.3    Attia, H.4    Ghorbel, D.5
  • 4
    • 85045909043 scopus 로고    scopus 로고
    • Effect of oil hydrophobicity on the adsorption and rheology of β-lactoglobulin at oil–water interfaces
    • Bergfreund, J., Bertsch, P., Kuster, S., Fischer, P., Effect of oil hydrophobicity on the adsorption and rheology of β-lactoglobulin at oil–water interfaces. Langmuir 34 (2018), 4929–4936 http://doi.org/10.1021/acs.langmuir.8b00458.
    • (2018) Langmuir , vol.34 , pp. 4929-4936
    • Bergfreund, J.1    Bertsch, P.2    Kuster, S.3    Fischer, P.4
  • 5
    • 0032798799 scopus 로고    scopus 로고
    • Protein adsorption at the oil/water interface: Characterization of adsorption kinetics by dynamic interfacial tension measurements
    • Beverung, C.J., Radke, C.J., Blanch, H.W., Protein adsorption at the oil/water interface: Characterization of adsorption kinetics by dynamic interfacial tension measurements. Biophysical Chemistry 81 (1999), 59–80 http://doi.org/10.1016/S0301-4622(99)00082-4.
    • (1999) Biophysical Chemistry , vol.81 , pp. 59-80
    • Beverung, C.J.1    Radke, C.J.2    Blanch, H.W.3
  • 6
    • 85058386033 scopus 로고    scopus 로고
    • Biphasic short time heat degradation of the blue microalgae protein phycocyanin from Arthrospira platensis
    • Böcker, L., Ortmann, S., Surber, J., Leeb, E., Reineke, K., Mathys, A., Biphasic short time heat degradation of the blue microalgae protein phycocyanin from Arthrospira platensis. Innovative Food Science & Emerging Technologies 52 (2019), 116–121 http://doi.org/10.1016/J.IFSET.2018.11.007.
    • (2019) Innovative Food Science & Emerging Technologies , vol.52 , pp. 116-121
    • Böcker, L.1    Ortmann, S.2    Surber, J.3    Leeb, E.4    Reineke, K.5    Mathys, A.6
  • 7
    • 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 (1998), 143–151 http://doi.org/10.1016/S0924-2244(98)00031-4.
    • (1998) Trends in Food Science & Technology , vol.9 , pp. 143-151
    • Bryant, C.M.1    McClements, D.J.2
  • 8
    • 85048269276 scopus 로고    scopus 로고
    • Comprehensive pulsed electric field (PEF) system analysis for microalgae processing
    • Buchmann, L., Bloch, R., Mathys, A., Comprehensive pulsed electric field (PEF) system analysis for microalgae processing. Bioresource Technology 265 (2018), 268–274 http://doi.org/10.1016/j.biortech.2018.06.010.
    • (2018) Bioresource Technology , vol.265 , pp. 268-274
    • Buchmann, L.1    Bloch, R.2    Mathys, A.3
  • 9
    • 85046364593 scopus 로고    scopus 로고
    • Energy input assessment for nanosecond pulsed electric field processing and its application in a case study with Chlorella vulgaris
    • Buchmann, L., Böcker, L., Frey, W., Haberkorn, I., Nyffeler, M., Mathys, A., Energy input assessment for nanosecond pulsed electric field processing and its application in a case study with Chlorella vulgaris. Innovative Food Science & Emerging Technologies 47 (2018), 445–453 http://doi.org/10.1016/j.ifset.2018.04.013.
    • (2018) Innovative Food Science & Emerging Technologies , vol.47 , pp. 445-453
    • Buchmann, L.1    Böcker, L.2    Frey, W.3    Haberkorn, I.4    Nyffeler, M.5    Mathys, A.6
  • 10
    • 85054192317 scopus 로고    scopus 로고
    • Effect of nanosecond pulsed electric field treatment on cell proliferation of microalgae
    • Buchmann, L., Frey, W., Gusbeth, C., Ravaynia, P.S., Mathys, A., Effect of nanosecond pulsed electric field treatment on cell proliferation of microalgae. Bioresource Technology 271 (2019), 402–408 http://doi.org/10.1016/j.biortech.2018.09.124.
    • (2019) Bioresource Technology , vol.271 , pp. 402-408
    • Buchmann, L.1    Frey, W.2    Gusbeth, C.3    Ravaynia, P.S.4    Mathys, A.5
  • 12
    • 85056132978 scopus 로고    scopus 로고
    • Trends in microalgae incorporation into innovative food products with potential health benefits
    • Caporgno, M.P., Mathys, A., Trends in microalgae incorporation into innovative food products with potential health benefits. Frontiers in Nutrition, 5, 2018, 58 http://doi.org/10.3389/fnut.2018.00058.
    • (2018) Frontiers in Nutrition , vol.5 , pp. 58
    • Caporgno, M.P.1    Mathys, A.2
  • 13
    • 0034634779 scopus 로고    scopus 로고
    • The behaviour of protein preparations from blue-green algae (Spirulina platensis strain Pacifica) at the air/water interface
    • Chronakis, I.S., Galatanu, A.N., Nylander, T., Lindman, B., The behaviour of protein preparations from blue-green algae (Spirulina platensis strain Pacifica) at the air/water interface. Colloids and Surfaces A: Physicochemical and Engineering Aspects 173 (2000), 181–192 http://doi.org/10.1016/S0927-7757(00)00548-3.
    • (2000) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.173 , pp. 181-192
    • Chronakis, I.S.1    Galatanu, A.N.2    Nylander, T.3    Lindman, B.4
  • 14
    • 85065492587 scopus 로고    scopus 로고
    • Shear rheological properties of acid hydrolyzed insoluble proteins from Chlorella protothecoides at the oil-water interface
    • Dai, L., Bergfreund, J., Reichert, C.L., Fischer, P., Weiss, J., Shear rheological properties of acid hydrolyzed insoluble proteins from Chlorella protothecoides at the oil-water interface. Journal of Colloid and Interface Science 551 (2019), 297–304 http://doi.org/10.1016/J.JCIS.2019.05.029.
    • (2019) Journal of Colloid and Interface Science , vol.551 , pp. 297-304
    • Dai, L.1    Bergfreund, J.2    Reichert, C.L.3    Fischer, P.4    Weiss, J.5
  • 15
    • 0031057506 scopus 로고    scopus 로고
    • Adsorption of protein and the stability of emulsions
    • Dalgleish, D.G., Adsorption of protein and the stability of emulsions. Trends in Food Science & Technology 8 (1997), 1–6 http://doi.org/10.1016/S0924-2244(97)01001-7.
    • (1997) Trends in Food Science & Technology , vol.8 , pp. 1-6
    • Dalgleish, D.G.1
  • 16
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran, S., Protein stabilization of emulsions and foams. Journal of Food Science 70 (2006), 54–66 http://doi.org/10.1111/j.1365-2621.2005.tb07150.x.
    • (2006) Journal of Food Science , vol.70 , pp. 54-66
    • Damodaran, S.1
  • 18
    • 85024995072 scopus 로고
    • Functional properties of protein products of mass cultivated blue‐green alga Spirulina platensis
    • Devi, M.A., Venkataraman, L.V., Functional properties of protein products of mass cultivated blue‐green alga Spirulina platensis. Journal of Food Science 49 (1984), 24–27 http://doi.org/10.1111/j.1365-2621.1984.tb13660.x.
    • (1984) Journal of Food Science , vol.49 , pp. 24-27
    • Devi, M.A.1    Venkataraman, L.V.2
  • 19
    • 0032809028 scopus 로고    scopus 로고
    • Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology
    • Dickinson, E., Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology. Colloids and Surfaces B: Biointerfaces 15 (1999), 161–176 http://doi.org/10.1016/S0927-7765(99)00042-9.
    • (1999) Colloids and Surfaces B: Biointerfaces , vol.15 , pp. 161-176
    • Dickinson, E.1
  • 20
    • 37049084567 scopus 로고
    • Coalescence stability of emulsion-sized droplets at a planar oil–water interface and the relationship to protein film surface rheology
    • 1: Physical Chemistry in Condensed Phases
    • Dickinson, E., Murray, B.S., Stainsby, G., Coalescence stability of emulsion-sized droplets at a planar oil–water interface and the relationship to protein film surface rheology. Journal of the Chemical Society, Faraday Transactions 84 (1988), 871–883 1: Physical Chemistry in Condensed Phases http://doi.org/10.1039/f19888400871.
    • (1988) Journal of the Chemical Society, Faraday Transactions , vol.84 , pp. 871-883
    • Dickinson, E.1    Murray, B.S.2    Stainsby, G.3
  • 22
    • 84879250963 scopus 로고    scopus 로고
    • Rheology of interfacial protein-polysaccharide composites
    • Fischer, P., Rheology of interfacial protein-polysaccharide composites. The European Physical Journal - Special Topics 222 (2013), 73–81 http://doi.org/10.1140/epjst/e2013-01827-x.
    • (2013) The European Physical Journal - Special Topics , vol.222 , pp. 73-81
    • Fischer, P.1
  • 23
    • 34548849116 scopus 로고    scopus 로고
    • Emulsion drops in external flow fields — the role of liquid interfaces
    • Fischer, P., Erni, P., Emulsion drops in external flow fields — the role of liquid interfaces. Current Opinion in Colloid & Interface Science 12 (2007), 196–205 http://doi.org/10.1016/J.COCIS.2007.07.014.
    • (2007) Current Opinion in Colloid & Interface Science , vol.12 , pp. 196-205
    • Fischer, P.1    Erni, P.2
  • 24
    • 25844500998 scopus 로고    scopus 로고
    • Factors determining the physical properties of protein foams
    • Foegeding, E.A., Luck, P.J., Davis, J.P., Factors determining the physical properties of protein foams. Food Hydrocolloids 20 (2006), 284–292 http://doi.org/10.1016/J.FOODHYD.2005.03.014.
    • (2006) Food Hydrocolloids , vol.20 , pp. 284-292
    • Foegeding, E.A.1    Luck, P.J.2    Davis, J.P.3
  • 28
    • 67349238149 scopus 로고    scopus 로고
    • Physico-chemical factors controlling the foamability and foam stability of milk proteins: Sodium caseinate and whey protein concentrates
    • Marinova, K.G., Basheva, E.S., Nenova, B., Temelska, M., Mirarefi, A.Y., Campbell, B., et al. Physico-chemical factors controlling the foamability and foam stability of milk proteins: Sodium caseinate and whey protein concentrates. Food Hydrocolloids 23 (2009), 1864–1876 http://doi.org/10.1016/J.FOODHYD.2009.03.003.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1864-1876
    • Marinova, K.G.1    Basheva, E.S.2    Nenova, B.3    Temelska, M.4    Mirarefi, A.Y.5    Campbell, B.6
  • 29
    • 85029899772 scopus 로고    scopus 로고
    • The impact of microalgae in food science and technology
    • Matos, Â.P., The impact of microalgae in food science and technology. Journal of the American Oil Chemists’ Society 94 (2017), 1333–1350 http://doi.org/10.1007/s11746-017-3050-7.
    • (2017) Journal of the American Oil Chemists’ Society , vol.94 , pp. 1333-1350
    • Matos, Â.P.1
  • 30
    • 84875939276 scopus 로고    scopus 로고
    • The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions
    • 046601
    • Mezzenga, R., Fischer, P., The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions. Reports on Progress in Physics, 76, 2013 046601 http://doi.org/10.1088/0034-4885/76/4/046601.
    • (2013) Reports on Progress in Physics , vol.76
    • Mezzenga, R.1    Fischer, P.2
  • 31
    • 84897994105 scopus 로고    scopus 로고
    • Mechanical properties of protein adsorption layers at the air/water and oil/water interface: A comparison in light of the thermodynamical stability of proteins
    • Mitropoulos, V., Mütze, A., Fischer, P., Mechanical properties of protein adsorption layers at the air/water and oil/water interface: A comparison in light of the thermodynamical stability of proteins. Advances in Colloid and Interface Science 206 (2014), 195–206 http://doi.org/10.1016/J.CIS.2013.11.004.
    • (2014) Advances in Colloid and Interface Science , vol.206 , pp. 195-206
    • Mitropoulos, V.1    Mütze, A.2    Fischer, P.3
  • 32
    • 33751080377 scopus 로고    scopus 로고
    • Impact of static pressure and volumetric energy input on the microstructure of food foam whipped in a rotor–stator device
    • Müller-Fischer, N., Suppiger, D., Windhab, E.J., Impact of static pressure and volumetric energy input on the microstructure of food foam whipped in a rotor–stator device. Journal of Food Engineering 80 (2007), 306–316 http://doi.org/10.1016/J.JFOODENG.2006.05.026.
    • (2007) Journal of Food Engineering , vol.80 , pp. 306-316
    • Müller-Fischer, N.1    Suppiger, D.2    Windhab, E.J.3
  • 33
    • 79851507537 scopus 로고    scopus 로고
    • Comparative effect of thermal treatment on the physicochemical properties of whey and egg white protein foams
    • Nicorescu, I., Vial, C., Talansier, E., Lechevalier, V., Loisel, C., Della Valle, D., et al. Comparative effect of thermal treatment on the physicochemical properties of whey and egg white protein foams. Food Hydrocolloids 25 (2011), 797–808 http://doi.org/10.1016/J.FOODHYD.2010.09.020.
    • (2011) Food Hydrocolloids , vol.25 , pp. 797-808
    • Nicorescu, I.1    Vial, C.2    Talansier, E.3    Lechevalier, V.4    Loisel, C.5    Della Valle, D.6
  • 34
    • 84984422567 scopus 로고
    • Physico‐chemical and functional properties of proteins from spray dried algae (Spirulina platensis)
    • Nirmala, C., Prakash, V., Venkataraman, L.V., Physico‐chemical and functional properties of proteins from spray dried algae (Spirulina platensis). Food/Nahrung 36 (1992), 569–577 http://doi.org/10.1002/food.19920360608.
    • (1992) Food/Nahrung , vol.36 , pp. 569-577
    • Nirmala, C.1    Prakash, V.2    Venkataraman, L.V.3
  • 35
    • 84966553333 scopus 로고    scopus 로고
    • Structural markers of the evolution of whey protein isolate powder during aging and effects on foaming properties
    • Norwood, E.-A., Le Floch-Fouéré, C., Briard-Bion, V., Schuck, P., Croguennec, T., Jeantet, R., Structural markers of the evolution of whey protein isolate powder during aging and effects on foaming properties. Journal of Dairy Science 99 (2016), 5265–5272 http://doi.org/10.3168/jds.2015-10788.
    • (2016) Journal of Dairy Science , vol.99 , pp. 5265-5272
    • Norwood, E.-A.1    Le Floch-Fouéré, C.2    Briard-Bion, V.3    Schuck, P.4    Croguennec, T.5    Jeantet, R.6
  • 36
    • 85037534950 scopus 로고    scopus 로고
    • Foams stabilized by β-lactoglobulin amyloid fibrils: Effect of pH
    • Peng, D., Yang, J., Li, J., Tang, C., Li, B., Foams stabilized by β-lactoglobulin amyloid fibrils: Effect of pH. Journal of Agricultural and Food Chemistry 65 (2017), 10658–10665 http://doi.org/10.1021/acs.jafc.7b03669.
    • (2017) Journal of Agricultural and Food Chemistry , vol.65 , pp. 10658-10665
    • Peng, D.1    Yang, J.2    Li, J.3    Tang, C.4    Li, B.5
  • 37
    • 0003150011 scopus 로고    scopus 로고
    • Foaming, foam films, antifoaming and defoaming
    • Pugh, R.J., Foaming, foam films, antifoaming and defoaming. Advances in Colloid and Interface Science 64 (1996), 67–142 http://doi.org/10.1016/0001-8686(95)00280-4.
    • (1996) Advances in Colloid and Interface Science , vol.64 , pp. 67-142
    • Pugh, R.J.1
  • 38
    • 85008450507 scopus 로고    scopus 로고
    • Effect of genotype on the physicochemical and functional attributes of faba bean (Vicia faba L.) protein isolates
    • Singhal, A., Stone, A.K., Vandenberg, A., Tyler, R., Nickerson, M.T., Effect of genotype on the physicochemical and functional attributes of faba bean (Vicia faba L.) protein isolates. Food Science and Biotechnology 25 (2016), 1513–1522 http://doi.org/10.1007/s10068-016-0235-z.
    • (2016) Food Science and Biotechnology , vol.25 , pp. 1513-1522
    • Singhal, A.1    Stone, A.K.2    Vandenberg, A.3    Tyler, R.4    Nickerson, M.T.5
  • 39
    • 85028917973 scopus 로고    scopus 로고
    • Autotrophic and heterotrophic microalgae and cyanobacteria cultivation for food and feed: Life cycle assessment
    • Smetana, S., Sandmann, M., Rohn, S., Pleissner, D., Heinz, V., Autotrophic and heterotrophic microalgae and cyanobacteria cultivation for food and feed: Life cycle assessment. Bioresource Technology 245 (2017), 162–170 http://doi.org/10.1016/j.biortech.2017.08.113.
    • (2017) Bioresource Technology , vol.245 , pp. 162-170
    • Smetana, S.1    Sandmann, M.2    Rohn, S.3    Pleissner, D.4    Heinz, V.5
  • 40
    • 84861069987 scopus 로고    scopus 로고
    • Protein separation and characterization procedures
    • S. Nielsen Springer Cham
    • Smith, D.M., Protein separation and characterization procedures. Nielsen, S., (eds.) Food analysis. Food science text series., 2017, Springer, Cham, 431–453.
    • (2017) Food analysis. Food science text series. , pp. 431-453
    • Smith, D.M.1
  • 41
    • 2842597271 scopus 로고
    • The theory of Ostwald ripening
    • Voorhees, P.W., The theory of Ostwald ripening. Journal of Statistical Physics 38 (1985), 231–252 http://doi.org/10.1007/BF01017860.
    • (1985) Journal of Statistical Physics , vol.38 , pp. 231-252
    • Voorhees, P.W.1
  • 42
    • 85018440322 scopus 로고    scopus 로고
    • Concentration and characterization of microalgae proteins from Chlorella pyrenoidosa
    • Waghmare, A.G., Salve, M.K., LeBlanc, J.G., Arya, S.S., Concentration and characterization of microalgae proteins from Chlorella pyrenoidosa. Bioresources and Bioprocessing, 3, 2016, 16 http://doi.org/10.1186/s40643-016-0094-8.
    • (2016) Bioresources and Bioprocessing , vol.3 , pp. 16
    • Waghmare, A.G.1    Salve, M.K.2    LeBlanc, J.G.3    Arya, S.S.4
  • 43
    • 0142216171 scopus 로고    scopus 로고
    • Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air−water interface
    • Wierenga, P.A., Meinders, M.B.J., Egmond, M.R., Voragen, F.A.G.J., de Jongh, H.H.J., Protein exposed hydrophobicity reduces the kinetic barrier for adsorption of ovalbumin to the air−water interface. Langmuir 19 (2003), 8964–8970 http://doi.org/10.1021/LA034868P.
    • (2003) Langmuir , vol.19 , pp. 8964-8970
    • Wierenga, P.A.1    Meinders, M.B.J.2    Egmond, M.R.3    Voragen, F.A.G.J.4    de Jongh, H.H.J.5
  • 45
    • 1842533485 scopus 로고    scopus 로고
    • Nutritional evaluation of protein concentrates isolated from two red seaweeds: Hypnea charoides and Hypnea japonica in growing rats
    • Wong, K.H., Cheung, P.C.K., Ang, P.O. Jr., Nutritional evaluation of protein concentrates isolated from two red seaweeds: Hypnea charoides and Hypnea japonica in growing rats. Hydrobiologia 512 (2004), 271–278 http://doi.org/10.1023/B:HYDR.0000020337.13945.20.
    • (2004) Hydrobiologia , vol.512 , pp. 271-278
    • Wong, K.H.1    Cheung, P.C.K.2    Ang, P.O.3
  • 46
    • 0038215686 scopus 로고    scopus 로고
    • Foaming properties of proteins
    • J.F. Zayas Springer Berlin, Heidelberg
    • Zayas, J.F., Foaming properties of proteins. Zayas, J.F., (eds.) Functionality of proteins in food, 1997, Springer, Berlin, Heidelberg, 262–309 http://doi.org/10.1007/978-3-642-59116-7_6.
    • (1997) Functionality of proteins in food , pp. 262-309
    • Zayas, J.F.1
  • 47
    • 1442335307 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on competitive protein adsorption to air/water interfaces in aqueous foams made with mixed milk proteins
    • Zhang, Z., Dalgleish, D., Goff, H., Effect of pH and ionic strength on competitive protein adsorption to air/water interfaces in aqueous foams made with mixed milk proteins. Colloids and Surfaces B: Biointerfaces 34 (2004), 113–121 http://doi.org/10.1016/j.colsurfb.2003.11.009.
    • (2004) Colloids and Surfaces B: Biointerfaces , vol.34 , pp. 113-121
    • Zhang, Z.1    Dalgleish, D.2    Goff, H.3
  • 48
    • 0005127283 scopus 로고    scopus 로고
    • Ionic strength dependence of protein adsorption to dye-ligand adsorbents
    • Zhang, S., Sun, Y., Ionic strength dependence of protein adsorption to dye-ligand adsorbents. AIChE Journal 48 (2002), 178–186 http://doi.org/10.1002/aic.690480118.
    • (2002) AIChE Journal , vol.48 , pp. 178-186
    • Zhang, S.1    Sun, Y.2


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