메뉴 건너뛰기




Volumn 86, Issue , 2019, Pages 134-140

Functionalisation of pea protein by tryptic hydrolysis – Characterisation of interfacial and functional properties

Author keywords

Emulsion; Hydrolysis; Interfacial properties; Pea protein

Indexed keywords

ALKALINITY; EMULSIFICATION; EMULSIONS; OILS AND FATS; OSTWALD RIPENING; SOLUBILITY;

EID: 85053437950     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2018.03.013     Document Type: Article
Times cited : (76)

References (32)
  • 1
    • 84871724197 scopus 로고    scopus 로고
    • The effects of limited enzymatic hydrolysis on the physicochemical and emulsifying properties of a lentil protein isolate
    • Avramenko, N.A., Low, N.H., Nickerson, M.T., The effects of limited enzymatic hydrolysis on the physicochemical and emulsifying properties of a lentil protein isolate. Food Research International 51:1 (2013), 162–169 https://doi.org/10.1016/j.foodres.2012.11.020.
    • (2013) Food Research International , vol.51 , Issue.1 , pp. 162-169
    • Avramenko, N.A.1    Low, N.H.2    Nickerson, M.T.3
  • 5
    • 84949088038 scopus 로고    scopus 로고
    • Effect of pH on the inter-relationships between the physicochemical, interfacial and emulsifying properties for pea, soy, lentil and canola protein isolates
    • Chang, C., Tu, S., Ghosh, S., Nickerson, M.T., Effect of pH on the inter-relationships between the physicochemical, interfacial and emulsifying properties for pea, soy, lentil and canola protein isolates. Food Research International 77 (2015), 360–367 https://doi.org/10.1016/j.foodres.2015.08.012.
    • (2015) Food Research International , vol.77 , pp. 360-367
    • Chang, C.1    Tu, S.2    Ghosh, S.3    Nickerson, M.T.4
  • 6
    • 84948283862 scopus 로고
    • Legumin of pisum sativum and vicia faba
    • Croy, R.R.D., Derbyshire, E., Krishna, T.G., Boulter, D., Legumin of pisum sativum and vicia faba. New Phytologist 83 (1979), 29–35 https://doi.org/10.1111/j.1469-8137.1979.tb00723.x.
    • (1979) New Phytologist , vol.83 , pp. 29-35
    • Croy, R.R.D.1    Derbyshire, E.2    Krishna, T.G.3    Boulter, D.4
  • 7
    • 0004068127 scopus 로고
    • Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.) - I. Legumin
    • Croy, R.R.D., Gatehouse, J.A., Evans, I.M., Boulter, D., Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.) - I. Legumin. Planta 148:1 (1980), 49–56 https://doi.org/10.1007/BF00385441.
    • (1980) Planta , vol.148 , Issue.1 , pp. 49-56
    • Croy, R.R.D.1    Gatehouse, J.A.2    Evans, I.M.3    Boulter, D.4
  • 8
    • 0019082050 scopus 로고
    • The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)
    • Croy, R.R.D., Gatehouse, J.A., Tyler, M., Boulter, D., The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.). Biochemical Journal 191 (1980), 509–516.
    • (1980) Biochemical Journal , vol.191 , pp. 509-516
    • Croy, R.R.D.1    Gatehouse, J.A.2    Tyler, M.3    Boulter, D.4
  • 9
    • 0001243460 scopus 로고
    • Seed globulins of the gramineae and leguminosae
    • Retrieved from
    • Danielsson, C.E., Seed globulins of the gramineae and leguminosae. Biochemical Journal 44:4 (1949), 387–400 Retrieved from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1274878&tool=pmcentrez&rendertype=abstract.
    • (1949) Biochemical Journal , vol.44 , Issue.4 , pp. 387-400
    • Danielsson, C.E.1
  • 10
    • 85169583355 scopus 로고    scopus 로고
    • Fennema's food chemistry
    • 5th ed.
    • Fennema, O.R., Fennema's food chemistry. 5th ed., 2017.
    • (2017)
    • Fennema, O.R.1
  • 11
    • 0019618394 scopus 로고
    • Characterisation and subunit structures of the vicilin storage proteins of pea (pisum sativum l.)
    • Gatehouse, J.A., Croy, R.R.D., Morton, H., Tyler, M., Boulter, D., Characterisation and subunit structures of the vicilin storage proteins of pea (pisum sativum l.). European Journal of Biochemistry 118:3 (1981), 627–633 https://doi.org/10.1111/j.1432-1033.1981.tb05565.x.
    • (1981) European Journal of Biochemistry , vol.118 , Issue.3 , pp. 627-633
    • Gatehouse, J.A.1    Croy, R.R.D.2    Morton, H.3    Tyler, M.4    Boulter, D.5
  • 12
    • 0021104094 scopus 로고
    • Sequence specificity of the post -translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.)
    • Gatehouse, J.A., Lycett, G.W., Delauney, A.J., Croy, R.R.D., Sequence specificity of the post -translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.). Biochemical Journal 212 (1983), 427–432.
    • (1983) Biochemical Journal , vol.212 , pp. 427-432
    • Gatehouse, J.A.1    Lycett, G.W.2    Delauney, A.J.3    Croy, R.R.D.4
  • 13
    • 84986799915 scopus 로고
    • Quantitative and qualitative variability of pea (pisum sativum l.) protein composition
    • Gueguen, J., Barbot, J., Quantitative and qualitative variability of pea (pisum sativum l.) protein composition. Journal of the Science of Food and Agriculture 42 (1988), 209–224 https://doi.org/10.1002/jsfa.2740420304.
    • (1988) Journal of the Science of Food and Agriculture , vol.42 , pp. 209-224
    • Gueguen, J.1    Barbot, J.2
  • 14
    • 1542526976 scopus 로고    scopus 로고
    • Structural and functional changes of faba bean legumin during super- limited tryptic hydrolysis
    • Henning, T., Mothes, R., Dudek, S., Schwenke, K.D., Structural and functional changes of faba bean legumin during super- limited tryptic hydrolysis. Nahrung-Food 41:2 (1997), 81–86 https://doi.org/10.1002/food.19970410205.
    • (1997) Nahrung-Food , vol.41 , Issue.2 , pp. 81-86
    • Henning, T.1    Mothes, R.2    Dudek, S.3    Schwenke, K.D.4
  • 15
    • 35348862011 scopus 로고    scopus 로고
    • Physicochemical and bitterness properties of enzymatic pea protein hydrolysates
    • Humiski, L.M., Aluko, R.E., Physicochemical and bitterness properties of enzymatic pea protein hydrolysates. Journal of Food Science, 72(8), 2007 https://doi.org/10.1111/j.1750-3841.2007.00475.x.
    • (2007) Journal of Food Science , vol.72 , Issue.8
    • Humiski, L.M.1    Aluko, R.E.2
  • 16
    • 84984529526 scopus 로고
    • Changes in interfacial properties of legumin from faba beans (Vicia faba I.) by tryptic hydrolysis
    • Krause, J.-P., Schwenke, K.D., Changes in interfacial properties of legumin from faba beans (Vicia faba I.) by tryptic hydrolysis. Food/Nahrung 39:5–6 (1995), 396–405 https://doi.org/10.1002/food.19950390505.
    • (1995) Food/Nahrung , vol.39 , Issue.5-6 , pp. 396-405
    • Krause, J.-P.1    Schwenke, K.D.2
  • 17
    • 85007560086 scopus 로고    scopus 로고
    • In vitro digestibility, protein composition and techno-functional properties of Saskatchewan grown yellow field peas (Pisum sativum L.) as affected by processing
    • Ma, Z., Boye, J.I., Hu, X., In vitro digestibility, protein composition and techno-functional properties of Saskatchewan grown yellow field peas (Pisum sativum L.) as affected by processing. Food Research International 92 (2017), 64–78 https://doi.org/10.1016/j.foodres.2016.12.012.
    • (2017) Food Research International , vol.92 , pp. 64-78
    • Ma, Z.1    Boye, J.I.2    Hu, X.3
  • 19
    • 35349018463 scopus 로고    scopus 로고
    • Critical review of techniques and methodologies for characterization of emulsion stability
    • McClements, D.J., Critical review of techniques and methodologies for characterization of emulsion stability. Critical Reviews in Food Science and Nutrition 47:7 (2007), 611–649 https://doi.org/10.1080/10408390701289292.
    • (2007) Critical Reviews in Food Science and Nutrition , vol.47 , Issue.7 , pp. 611-649
    • McClements, D.J.1
  • 20
    • 0004130627 scopus 로고    scopus 로고
    • Food emulsions: Principles, practices, and techniques
    • 3rd ed.
    • McClements, D.J., Food emulsions: Principles, practices, and techniques. 3rd ed., 2016.
    • (2016)
    • McClements, D.J.1
  • 21
    • 0001909237 scopus 로고
    • Effect of tryptic digestion on emulsifying properties of soy protein
    • Ochiai, K., Kamata, Y., Shibasaki, K., Effect of tryptic digestion on emulsifying properties of soy protein. Agricultural & Biological Chemistry 46:1 (1982), 91–96 https://doi.org/10.1080/00021369.1982.10865031.
    • (1982) Agricultural & Biological Chemistry , vol.46 , Issue.1 , pp. 91-96
    • Ochiai, K.1    Kamata, Y.2    Shibasaki, K.3
  • 22
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing the functionality of food proteins by enzymatic modification
    • Panyam, D., Enhancing the functionality of food proteins by enzymatic modification. Trends in Food Science & Technology 7:4 (1996), 120–125 https://doi.org/10.1016/0924-2244(96)10012-1.
    • (1996) Trends in Food Science & Technology , vol.7 , Issue.4 , pp. 120-125
    • Panyam, D.1
  • 23
    • 0024853054 scopus 로고
    • A study of the trypsinolysis of pea 11S globulin
    • Plumb, G.W., Carr, H.J., Newby, V.K., Lambert, N., A study of the trypsinolysis of pea 11S globulin. Bba 999 (1989), 281–288 https://doi.org/10.1016/0167-4838(89)90010-1.
    • (1989) Bba , vol.999 , pp. 281-288
    • Plumb, G.W.1    Carr, H.J.2    Newby, V.K.3    Lambert, N.4
  • 25
    • 0041524989 scopus 로고    scopus 로고
    • Reflections about the functional potential of legume proteins: A review
    • Schwenke, K.D., Reflections about the functional potential of legume proteins: A review. Nahrung-Food 45:6 (2001), 377–381 https://doi.org/10.1002/1521-3803(20011001)45:6<377::AID-FOOD377>3.0.CO;2-G.
    • (2001) Nahrung-Food , vol.45 , Issue.6 , pp. 377-381
    • Schwenke, K.D.1
  • 26
    • 1542786800 scopus 로고    scopus 로고
    • The solubility of trypsin pea protein hydrolysates (Short communication)
    • Soral-Smietana, M., Swigon, A., Amarowicz, R., Sijtsama, L., The solubility of trypsin pea protein hydrolysates (Short communication). Nahrung-Food 42:03–04 (1998), 217–218 https://doi.org/10.1002/(SICI)1521-3803(199808)42:03/04<217::AID-FOOD217>3.0.CO;2-2.
    • (1998) Nahrung-Food , vol.42 , Issue.3-4 , pp. 217-218
    • Soral-Smietana, M.1    Swigon, A.2    Amarowicz, R.3    Sijtsama, L.4
  • 28
    • 84960089093 scopus 로고    scopus 로고
    • Functional properties of pea protein hydrolysates in emulsions and spray-dried microcapsules
    • Tamm, F., Herbst, S., Brodkorb, A., Drusch, S., Functional properties of pea protein hydrolysates in emulsions and spray-dried microcapsules. Food Hydrocolloids 58 (2016), 204–214 https://doi.org/10.1016/j.foodhyd.2016.02.032.
    • (2016) Food Hydrocolloids , vol.58 , pp. 204-214
    • Tamm, F.1    Herbst, S.2    Brodkorb, A.3    Drusch, S.4
  • 29
    • 33751341296 scopus 로고    scopus 로고
    • Adsorption at the air-water interface and emulsification properties of grain legume protein derivatives from pea and broad bean
    • Tsoukala, A., Papalamprou, E., Makri, E., Doxastakis, G., Braudo, E.E., Adsorption at the air-water interface and emulsification properties of grain legume protein derivatives from pea and broad bean. Colloids and Surfaces B: Biointerfaces 53:2 (2006), 203–208 https://doi.org/10.1016/j.colsurfb.2006.08.019.
    • (2006) Colloids and Surfaces B: Biointerfaces , vol.53 , Issue.2 , pp. 203-208
    • Tsoukala, A.1    Papalamprou, E.2    Makri, E.3    Doxastakis, G.4    Braudo, E.E.5
  • 30
    • 12344333869 scopus 로고    scopus 로고
    • Functional properties of soy protein hydrolysates obtained by selective proteolysis
    • Tsumura, K., Saito, T., Tsuge, K., Ashida, H., Kugimiya, W., Inouye, K., Functional properties of soy protein hydrolysates obtained by selective proteolysis. LWT - Food Science and Technology 38:3 (2005), 255–261 https://doi.org/10.1016/j.lwt.2004.06.007.
    • (2005) LWT - Food Science and Technology , vol.38 , Issue.3 , pp. 255-261
    • Tsumura, K.1    Saito, T.2    Tsuge, K.3    Ashida, H.4    Kugimiya, W.5    Inouye, K.6
  • 31
    • 84966311919 scopus 로고    scopus 로고
    • Nonlinear surface dilatational rheology and foaming behavior of protein and protein fibrillar aggregates in the presence of natural surfactant
    • Wan, Z., Yang, X., Sagis, L.M.C., Nonlinear surface dilatational rheology and foaming behavior of protein and protein fibrillar aggregates in the presence of natural surfactant. Langmuir 32:15 (2016), 3679–3690 https://doi.org/10.1021/acs.langmuir.6b00446.
    • (2016) Langmuir , vol.32 , Issue.15 , pp. 3679-3690
    • Wan, Z.1    Yang, X.2    Sagis, L.M.C.3
  • 32
    • 34147181809 scopus 로고    scopus 로고
    • Effect of interfacial rheology on model emulsion coalescence. I. Interfacial rheology
    • Yarranton, H.W., Sztukowski, D.M., Urrutia, P., Effect of interfacial rheology on model emulsion coalescence. I. Interfacial rheology. Journal of Colloid and Interface Science 310:1 (2007), 246–252 https://doi.org/10.1016/j.jcis.2007.01.071.
    • (2007) Journal of Colloid and Interface Science , vol.310 , Issue.1 , pp. 246-252
    • Yarranton, H.W.1    Sztukowski, D.M.2    Urrutia, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.