메뉴 건너뛰기




Volumn 245, Issue 7, 2019, Pages 1519-1531

Formation, stability, and sensory characteristics of a lentil-based milk substitute as affected by homogenisation and pasteurisation

Author keywords

Emulsion; Homogenisation; Lentil protein; Milk substitutes; Pasteurisation; Protein functionality

Indexed keywords

EMULSIFICATION; EMULSIONS; HEAT TREATMENT; HIGH PRESSURE EFFECTS; HOMOGENIZATION METHOD; OSTWALD RIPENING; PARTICLE SIZE; PARTICLE SIZE ANALYSIS; PASTEURIZATION; SENSORY ANALYSIS; SOLS;

EID: 85065638286     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-019-03286-0     Document Type: Article
Times cited : (70)

References (41)
  • 2
    • 85065642441 scopus 로고    scopus 로고
    • Accessed 17 Aug 2018
    • Mintel Group Ltd. (2018) US non-dairy milk sales grow 61% over the last 5 years|Mintel.com. http://www.mintel.com/press-centre/food-and-drink/us-non-dairy-milk-sales-grow-61-over-the-last-five-years. Accessed 17 Aug 2018
    • (2018) US Non-Dairy Milk Sales Grow 61% over the Last 5 Years|Mintel.Com
  • 3
    • 85065646656 scopus 로고    scopus 로고
    • Accessed 17 Aug 2018
    • Mintel Group Ltd. (2018) Taste is top reason Americans eat plant-based proteins|Mintel.com. http://www.mintel.com/press-centre/food-and-drink/taste-is-the-top-reason-us-consumers-eat-plant-based-proteins. Accessed 17 Aug 2018
    • (2018) Taste is Top Reason Americans Eat Plant-Based Proteins|Mintel.Com
  • 4
    • 84993929587 scopus 로고    scopus 로고
    • The impacts of dietary change on greenhouse gas emissions, land use, water use, and health: a systematic review
    • Aleksandrowicz L, Green R, Joy EJM et al (2016) The impacts of dietary change on greenhouse gas emissions, land use, water use, and health: a systematic review. PLoS One. 10.1371/journal.pone.0165797
    • (2016) PLoS One
    • Aleksandrowicz, L.1    Green, R.2    Joy, E.J.M.3
  • 5
    • 85032935325 scopus 로고    scopus 로고
    • How well do plant based alternatives fare nutritionally compared to cow’s milk?
    • Vanga SK, Raghavan V (2018) How well do plant based alternatives fare nutritionally compared to cow’s milk? J Food Sci Technol 55:10–20. 10.1007/s13197-017-2915-y
    • (2018) J Food Sci Technol , vol.55 , pp. 10-20
    • Vanga, S.K.1    Raghavan, V.2
  • 6
    • 84994234398 scopus 로고    scopus 로고
    • Evaluation of physicochemical and glycaemic properties of commercial plant-based milk substitutes
    • Jeske S, Zannini E, Arendt EK (2017) Evaluation of physicochemical and glycaemic properties of commercial plant-based milk substitutes. Plant Foods Hum Nutr 72:26–33. 10.1007/s11130-016-0583-0
    • (2017) Plant Foods Hum Nutr , vol.72 , pp. 26-33
    • Jeske, S.1    Zannini, E.2    Arendt, E.K.3
  • 7
    • 85050127382 scopus 로고    scopus 로고
    • Nutritional implications of an increasing consumption of non-dairy plant-based beverages instead of cow’s milk in Switzerland
    • Sousa A, Kopf-Bolanz KA, Kopf-Bolanz K (2017) Nutritional implications of an increasing consumption of non-dairy plant-based beverages instead of cow’s milk in Switzerland. Adv Dairy Res. 10.4172/2329-888X.1000197
    • (2017) Adv Dairy Res
    • Sousa, A.1    Kopf-Bolanz, K.A.2    Kopf-Bolanz, K.3
  • 8
    • 0344701685 scopus 로고    scopus 로고
    • Processing of Soybeans into Ingredients
    • Riaz MN, (ed), 1, Taylor & Francis Group, Boca Raton
    • Riaz MN (2006) Processing of Soybeans into Ingredients. In: Riaz MN (ed) Soy application in food, 1st edn. Taylor & Francis Group, Boca Raton
    • (2006) Soy application in food
    • Riaz, M.N.1
  • 10
    • 85037825420 scopus 로고    scopus 로고
    • Global production, processing and utilization of lentil: a review
    • Joshi M, Timilsena Y, Adhikari B (2017) Global production, processing and utilization of lentil: a review. J Integr Agric 16:2898–2913. 10.1016/S2095-3119(17)61793-3
    • (2017) J Integr Agric , vol.16 , pp. 2898-2913
    • Joshi, M.1    Timilsena, Y.2    Adhikari, B.3
  • 11
    • 85034754911 scopus 로고    scopus 로고
    • Lentil protein: a review of functional properties and food application. An overview of lentil protein functionality
    • Jarpa-Parra M (2018) Lentil protein: a review of functional properties and food application. An overview of lentil protein functionality. Int J Food Sci Technol 53:892–903. 10.1111/ijfs.13685
    • (2018) Int J Food Sci Technol , vol.53 , pp. 892-903
    • Jarpa-Parra, M.1
  • 12
    • 84958292174 scopus 로고    scopus 로고
    • Preparation of salad dressing emulsions using lentil, chickpea and pea protein isolates: a response surface methodology study
    • Ma Z, Boye JI, Simpson BK (2016) Preparation of salad dressing emulsions using lentil, chickpea and pea protein isolates: a response surface methodology study. J Food Qual 39:274–291. 10.1111/jfq.12190
    • (2016) J Food Qual , vol.39 , pp. 274-291
    • Ma, Z.1    Boye, J.I.2    Simpson, B.K.3
  • 13
    • 84861094510 scopus 로고    scopus 로고
    • Interfacial and emulsifying properties of lentil protein isolate
    • Joshi M, Adhikari B, Aldred P et al (2012) Interfacial and emulsifying properties of lentil protein isolate. Food Chem 134:1343–1353. 10.1016/j.foodchem.2012.03.029
    • (2012) Food Chem , vol.134 , pp. 1343-1353
    • Joshi, M.1    Adhikari, B.2    Aldred, P.3
  • 14
    • 85027952307 scopus 로고    scopus 로고
    • The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin
    • Johnston SP, Nickerson MT, Low NH (2015) The physicochemical properties of legume protein isolates and their ability to stabilize oil-in-water emulsions with and without genipin. J Food Sci Technol 52:4135–4145. 10.1007/s13197-014-1523-3
    • (2015) J Food Sci Technol , vol.52 , pp. 4135-4145
    • Johnston, S.P.1    Nickerson, M.T.2    Low, N.H.3
  • 15
    • 0011570781 scopus 로고
    • Protein-stabilized emulsions
    • Dickinson E (1994) Protein-stabilized emulsions. Water in Foods 1:59–74
    • (1994) Water in Foods , vol.1 , pp. 59-74
    • Dickinson, E.1
  • 16
    • 0002207547 scopus 로고
    • Relationships between structure and functional properties of food proteins
    • Fox PF, Condon JJ, (eds), Applied Science Publishers, London
    • Kinsella JE (1982) Relationships between structure and functional properties of food proteins. In: Fox PF, Condon JJ (eds) food proteins. Applied Science Publishers, London
    • (1982) food proteins
    • Kinsella, J.E.1
  • 17
    • 84970926858 scopus 로고    scopus 로고
    • Can protein functionalities be enhanced by high-pressure homogenization?—a study on functional properties of lupin proteins
    • Bader S, Bez J, Eisner P (2011) Can protein functionalities be enhanced by high-pressure homogenization?—a study on functional properties of lupin proteins. Proced Food Sci 1:1359–1366. 10.1016/J.PROFOO.2011.09.201
    • (2011) Proced Food Sci , vol.1 , pp. 1359-1366
    • Bader, S.1    Bez, J.2    Eisner, P.3
  • 18
    • 30344478568 scopus 로고    scopus 로고
    • Functional properties of whey proteins as affected by dynamic high-pressure treatment
    • Bouaouina H, Desrumaux A, Loisel C, Legrand J (2006) Functional properties of whey proteins as affected by dynamic high-pressure treatment. Int Dairy J 16:275–284. 10.1016/j.idairyj.2005.05.004
    • (2006) Int Dairy J , vol.16 , pp. 275-284
    • Bouaouina, H.1    Desrumaux, A.2    Loisel, C.3    Legrand, J.4
  • 20
    • 85019931007 scopus 로고    scopus 로고
    • Effect of lentil proteins isolate concentration on the formation, stability and rheological behavior of oil-in-water nanoemulsions
    • Primozic M, Duchek A, Nickerson M, Ghosh S (2017) Effect of lentil proteins isolate concentration on the formation, stability and rheological behavior of oil-in-water nanoemulsions. Food Chem 237:65–74. 10.1016/J.FOODCHEM.2017.05.079
    • (2017) Food Chem , vol.237 , pp. 65-74
    • Primozic, M.1    Duchek, A.2    Nickerson, M.3    Ghosh, S.4
  • 21
    • 85035022692 scopus 로고    scopus 로고
    • Formation, stability and in vitro digestibility of nanoemulsions stabilized by high-pressure homogenized lentil proteins isolate
    • Primozic M, Duchek A, Nickerson M, Ghosh S (2018) Formation, stability and in vitro digestibility of nanoemulsions stabilized by high-pressure homogenized lentil proteins isolate. Food Hydrocoll 77:126–141. 10.1016/j.foodhyd.2017.09.028
    • (2018) Food Hydrocoll , vol.77 , pp. 126-141
    • Primozic, M.1    Duchek, A.2    Nickerson, M.3    Ghosh, S.4
  • 22
    • 84255186340 scopus 로고    scopus 로고
    • Lentil and chickpea protein-stabilized emulsions: optimization of emulsion formulation
    • Can KA, Nickerson MT, Low NH (2011) Lentil and chickpea protein-stabilized emulsions: optimization of emulsion formulation. J Agric Food Chem 59:13203–13211. 10.1021/jf203028n
    • (2011) J Agric Food Chem , vol.59 , pp. 13203-13211
    • Can, K.A.1    Nickerson, M.T.2    Low, N.H.3
  • 24
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakawa SS, Nakai S (1985) Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J Food Eng 50:486–491. 10.1111/j.1365-2621.1985.tb13433.x
    • (1985) J Food Eng , vol.50 , pp. 486-491
    • Hayakawa, S.S.1    Nakai, S.2
  • 25
    • 22544461048 scopus 로고    scopus 로고
    • Changes in sulfhydryl content of egg white proteins due to heat and pressure treatment
    • Van der Plancken I, Van Loey A, Hendrickx MEG (2005) Changes in sulfhydryl content of egg white proteins due to heat and pressure treatment. J Agric Food Chem 53:5726–5733. 10.1021/jf050289+
    • (2005) J Agric Food Chem , vol.53 , pp. 5726-5733
    • Van der Plancken, I.1    Van Loey, A.2    Hendrickx, M.E.G.3
  • 27
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield N (2007) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1:2876–2890. 10.1038/nprot.2006.202
    • (2007) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.1
  • 28
    • 38049144912 scopus 로고    scopus 로고
    • Thermal stability of soy protein isolate and hydrolysate ingredients
    • Ryan M, McEvoy E, Duignan S et al (2008) Thermal stability of soy protein isolate and hydrolysate ingredients. Food Chem 108:503–510. 10.1016/j.foodchem.2007.11.001
    • (2008) Food Chem , vol.108 , pp. 503-510
    • Ryan, M.1    McEvoy, E.2    Duignan, S.3
  • 29
    • 0034768027 scopus 로고    scopus 로고
    • Development and application of confocal scanning laser microscopy methods for studying the distribution of fat and protein in selected dairy products
    • Auty MAE, Twomey M, Guinee TP, Mulvihill DM (2018) Development and application of confocal scanning laser microscopy methods for studying the distribution of fat and protein in selected dairy products. J Dairy Res 68:417–427. 10.1017/S0022029901004873
    • (2018) J Dairy Res , vol.68 , pp. 417-427
    • Auty, M.A.E.1    Twomey, M.2    Guinee, T.P.3    Mulvihill, D.M.4
  • 30
    • 84924080242 scopus 로고    scopus 로고
    • Effect of high pressure homogenisation and heat treatment on physical properties and stability of almond and hazelnut milks
    • Bernat N, Cháfer M, Rodríguez-García J et al (2015) Effect of high pressure homogenisation and heat treatment on physical properties and stability of almond and hazelnut milks. LWT Food Sci Technol 62:488–496. 10.1016/j.lwt.2014.10.045
    • (2015) LWT Food Sci Technol , vol.62 , pp. 488-496
    • Bernat, N.1    Cháfer, M.2    Rodríguez-García, J.3
  • 32
    • 0032798799 scopus 로고    scopus 로고
    • Protein adsorption at the oil/water interface: characterization of adsorption kinetics by dynamic interfacial tension measurements
    • Beverung CJ, Radke CJ, Blanch HW (1999) Protein adsorption at the oil/water interface: characterization of adsorption kinetics by dynamic interfacial tension measurements. Biophys Chem 81:59–80. 10.1016/S0301-4622(99)00082-4
    • (1999) Biophys Chem , vol.81 , pp. 59-80
    • Beverung, C.J.1    Radke, C.J.2    Blanch, H.W.3
  • 33
    • 0011543220 scopus 로고
    • Food processing characteristics of soybean proteins
    • Saio K, Kajikawa M, Watanabe T (1971) Food processing characteristics of soybean proteins. Agric Biol Chem 35:890–898. 10.1080/00021369.1971.10860005
    • (1971) Agric Biol Chem , vol.35 , pp. 890-898
    • Saio, K.1    Kajikawa, M.2    Watanabe, T.3
  • 34
    • 84908328220 scopus 로고    scopus 로고
    • Understanding the differences in gelling properties between lupin protein isolate and soy protein isolate
    • Berghout JAM, Boom RM, van der Goot AJ (2015) Understanding the differences in gelling properties between lupin protein isolate and soy protein isolate. Food Hydrocoll 43:465–472. 10.1016/j.foodhyd.2014.07.003
    • (2015) Food Hydrocoll , vol.43 , pp. 465-472
    • Berghout, J.A.M.1    Boom, R.M.2    van der Goot, A.J.3
  • 35
    • 85025566810 scopus 로고
    • Mixed proteinaceous emulsifiers: review of competitive protein adsorption and the relationship to food colloid stabilization
    • Dickinson E (1986) Mixed proteinaceous emulsifiers: review of competitive protein adsorption and the relationship to food colloid stabilization. Top Catal 1:3–23. 10.1016/S0268-005X(86)80003-0
    • (1986) Top Catal , vol.1 , pp. 3-23
    • Dickinson, E.1
  • 36
    • 84978245469 scopus 로고    scopus 로고
    • Comparative study of the effects of processing on the nutritional, physicochemical and functional properties of lentil
    • Aryee ANA, Boye JI (2015) Comparative study of the effects of processing on the nutritional, physicochemical and functional properties of lentil. J Food Process Preserv. 10.1111/jfpp.12824
    • (2015) J Food Process Preserv
    • Aryee, A.N.A.1    Boye, J.I.2
  • 38
    • 33845550183 scopus 로고
    • Structure–function relationships of food proteins with an emphasis on the importance of protein hydrophobicity
    • Nakai S (1983) Structure–function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. J Agric Food Chem 3:676–683. 10.1021/jf00118a001
    • (1983) J Agric Food Chem , vol.3 , pp. 676-683
    • Nakai, S.1
  • 39
    • 84899922127 scopus 로고    scopus 로고
    • Heat stability of reconstituted milk protein concentrate powders
    • Crowley SV, Megemont M, Gazi I et al (2014) Heat stability of reconstituted milk protein concentrate powders. Int Dairy J 37:104–110. 10.1016/J.IDAIRYJ.2014.03.005
    • (2014) Int Dairy J , vol.37 , pp. 104-110
    • Crowley, S.V.1    Megemont, M.2    Gazi, I.3
  • 40
    • 38049037759 scopus 로고    scopus 로고
    • Thermal degradation of anthocyanins and its impact on color and in vitro antioxidant capacity
    • Sadilova E, Carle R, Stintzing FC (2007) Thermal degradation of anthocyanins and its impact on color and in vitro antioxidant capacity. Mol Nutr Food Res 51:1461–1471. 10.1002/mnfr.200700179
    • (2007) Mol Nutr Food Res , vol.51 , pp. 1461-1471
    • Sadilova, E.1    Carle, R.2    Stintzing, F.C.3
  • 41
    • 85065638409 scopus 로고    scopus 로고
    • Regulation (EC) No 1924/2006 of the European Parliament and of the Council of 20 December 2006 on nutrition and health claims made on foods
    • European Parliament and Council of the European Union (2006) Regulation (EC) No 1924/2006 of the European Parliament and of the Council of 20 December 2006 on nutrition and health claims made on foods
    • (2006)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.