메뉴 건너뛰기




Volumn 124, Issue 2, 2011, Pages 545-550

Protein extraction optimisation, characterisation, and functionalities of protein isolate from bitter melon (Momordica charantia) seed

Author keywords

Bitter melon seed; Characterisation; Functionality; Protein

Indexed keywords

BITTER MELON; CHARACTERISATION; DENATURATION TEMPERATURES; EMULSIFYING ACTIVITY; ESSENTIAL AMINO ACIDS; FUNCTIONALITY; HIGH QUALITY; OPTIMISATIONS; OPTIMUM CONDITIONS; PROTEIN EXTRACTION; PROTEIN ISOLATES; RESPONSE SURFACE DESIGNS; SOY PROTEIN ISOLATES; SURFACE HYDROPHOBICITY; U-SHAPED;

EID: 77955771075     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2010.06.068     Document Type: Article
Times cited : (76)

References (27)
  • 1
    • 15744378144 scopus 로고    scopus 로고
    • Characterization and functional properties of Australia rice protein isolates
    • Agboola S., Ng D., Mills D. Characterization and functional properties of Australia rice protein isolates. Journal of Cereal Science 2005, 41:283-290.
    • (2005) Journal of Cereal Science , vol.41 , pp. 283-290
    • Agboola, S.1    Ng, D.2    Mills, D.3
  • 2
    • 0004136913 scopus 로고
    • AACC International, St. Paul, Minnesota, American Association of Cereal Chemists (AACC)
    • American Association of Cereal Chemists (AACC) Approved methods of AACC international 1986, AACC International, St. Paul, Minnesota. 8th ed.
    • (1986) Approved methods of AACC international
  • 3
    • 0004202155 scopus 로고    scopus 로고
    • AOAC International, Gaithersburg, MD, Association of Official Analytical Chemists, (AOAC)
    • Association of Official Analytical Chemists, (AOAC) Official methods of analysis of AOAC international 2005, AOAC International, Gaithersburg, MD. 18th ed.
    • (2005) Official methods of analysis of AOAC international
  • 4
    • 0000922732 scopus 로고
    • Solubility, emulsifying, and foaming properties of rice bran protein concentrates
    • Bera M.B., Mukherjee R.K. Solubility, emulsifying, and foaming properties of rice bran protein concentrates. Journal of Food Science 1989, 54(1):142-145.
    • (1989) Journal of Food Science , vol.54 , Issue.1 , pp. 142-145
    • Bera, M.B.1    Mukherjee, R.K.2
  • 5
    • 0002503849 scopus 로고    scopus 로고
    • Food protein: An overview
    • Marcel Dekker, Inc., New York, S. Damodaran, A. Paraf (Eds.)
    • Damodaran S. Food protein: An overview. Food proteins and their applications 1997, 1-24. Marcel Dekker, Inc., New York. S. Damodaran, A. Paraf (Eds.).
    • (1997) Food proteins and their applications , pp. 1-24
    • Damodaran, S.1
  • 6
    • 33846916404 scopus 로고    scopus 로고
    • Functional properties of fenugreek (Trigonella foenum graecum) protein concentrate
    • El Nasri N.A., El Tinay A.H. Functional properties of fenugreek (Trigonella foenum graecum) protein concentrate. Food Chemistry 2007, 103:582-589.
    • (2007) Food Chemistry , vol.103 , pp. 582-589
    • El Nasri, N.A.1    El Tinay, A.H.2
  • 8
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakawa S., Nakai S. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science 1985, 50:486-491.
    • (1985) Journal of Food Science , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 9
    • 14844358706 scopus 로고    scopus 로고
    • Preparation and characterization of protein isolate from cowpea (Vigna unguiculata L. Walp.)
    • Horax R., Hettiarachchy N.S., Chen P., Jalaluddin M. Preparation and characterization of protein isolate from cowpea (Vigna unguiculata L. Walp.). Journal of Food Science 2004, 69:FCT114-FCT118.
    • (2004) Journal of Food Science , vol.69
    • Horax, R.1    Hettiarachchy, N.S.2    Chen, P.3    Jalaluddin, M.4
  • 11
    • 0034997960 scopus 로고    scopus 로고
    • Extraction, denaturation, and hydrophobic properties of rice flour proteins
    • Ju Z.Y., Hettiarachchy N.S., Rath N. Extraction, denaturation, and hydrophobic properties of rice flour proteins. Journal of Food Science 2001, 66:229-232.
    • (2001) Journal of Food Science , vol.66 , pp. 229-232
    • Ju, Z.Y.1    Hettiarachchy, N.S.2    Rath, N.3
  • 12
    • 84998332173 scopus 로고
    • Determination of foaming properties of proteins by conductivity measurement
    • Kato A., Takahashi A., Matsudomi N., Kobayashi K. Determination of foaming properties of proteins by conductivity measurement. Journal of Food Science 1983, 48:62-65.
    • (1983) Journal of Food Science , vol.48 , pp. 62-65
    • Kato, A.1    Takahashi, A.2    Matsudomi, N.3    Kobayashi, K.4
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 1970, 227:680-686.
    • (1970) Nature , vol.227 , pp. 680-686
    • Laemmli, U.K.1
  • 15
    • 61849155315 scopus 로고    scopus 로고
    • Glycosylation and deamidation of rice endosperm protein for improved solubility and emulsifying properties
    • Paraman I., Hettiarachchy N., Schaefer C. Glycosylation and deamidation of rice endosperm protein for improved solubility and emulsifying properties. Cereal Chemistry 2007, 84:593-599.
    • (2007) Cereal Chemistry , vol.84 , pp. 593-599
    • Paraman, I.1    Hettiarachchy, N.2    Schaefer, C.3
  • 16
    • 34547900269 scopus 로고    scopus 로고
    • Hydrophobicity, solubility, and emulsifying properties of enzyme-modified rice endosperm protein
    • Paraman I., Hettiarachchy N.S., Schaefer C., Beck M.I. Hydrophobicity, solubility, and emulsifying properties of enzyme-modified rice endosperm protein. Cereal Chemistry 2007, 84(4):343-349.
    • (2007) Cereal Chemistry , vol.84 , Issue.4 , pp. 343-349
    • Paraman, I.1    Hettiarachchy, N.S.2    Schaefer, C.3    Beck, M.I.4
  • 17
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce K.N., Kinsella J.E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 1978, 26:716-722.
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , pp. 716-722
    • Pearce, K.N.1    Kinsella, J.E.2
  • 18
    • 0002050733 scopus 로고
    • Soy proteins
    • Applied Science Publishers, Essex, England, B.J.F. Hudson (Ed.)
    • Pearson A.M. Soy proteins. Developments in food proteins 1983, 67-108. Applied Science Publishers, Essex, England. B.J.F. Hudson (Ed.).
    • (1983) Developments in food proteins , pp. 67-108
    • Pearson, A.M.1
  • 19
    • 0031423685 scopus 로고    scopus 로고
    • Solubility and emulsifying properties of soy protein isolate modified by pancreatin
    • Qi M., Hettiarachchy N.S., Kalapathy U. Solubility and emulsifying properties of soy protein isolate modified by pancreatin. Journal of Food Science 1997, 62(6):1110-1115.
    • (1997) Journal of Food Science , vol.62 , Issue.6 , pp. 1110-1115
    • Qi, M.1    Hettiarachchy, N.S.2    Kalapathy, U.3
  • 20
    • 0142186148 scopus 로고    scopus 로고
    • Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration
    • Ragab D.M., Babiker E.E., El Tinay A.H. Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration. Food Chemistry 2004, 84:207-212.
    • (2004) Food Chemistry , vol.84 , pp. 207-212
    • Ragab, D.M.1    Babiker, E.E.2    El Tinay, A.H.3
  • 21
    • 0029099960 scopus 로고
    • Engineering thermostability: Lessons from thermophilic proteins
    • Russell R.J.M., Taylor G.L. Engineering thermostability: Lessons from thermophilic proteins. Current Opinion in Biotechnology 1995, 6:370-374.
    • (1995) Current Opinion in Biotechnology , vol.6 , pp. 370-374
    • Russell, R.J.M.1    Taylor, G.L.2
  • 22
    • 4944222065 scopus 로고    scopus 로고
    • Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion
    • Scheurer S., Lauer I., Foetisch K., Moncin M.S.M., Retzek M., Hartz C., et al. Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion. Journal of Allergy and Clinical Immunology 2004, 114(5):900-907.
    • (2004) Journal of Allergy and Clinical Immunology , vol.114 , Issue.5 , pp. 900-907
    • Scheurer, S.1    Lauer, I.2    Foetisch, K.3    Moncin, M.S.M.4    Retzek, M.5    Hartz, C.6
  • 23
    • 55949132286 scopus 로고    scopus 로고
    • Thermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study
    • Tang C.H., Chen L., Ma C.Y. Thermal aggregation, amino acid composition and in vitro digestibility of vicilin-rich protein isolates from three Phaseolus legumes: A comparative study. Food Chemistry 2009, 113:957-963.
    • (2009) Food Chemistry , vol.113 , pp. 957-963
    • Tang, C.H.1    Chen, L.2    Ma, C.Y.3
  • 24
    • 67349182649 scopus 로고    scopus 로고
    • Physicochemical, functional and structural properties of vicilin-rich protein isolates from three Phaseolus legumes: Effect of heat treatment
    • Tang C.H., Sun X., Yin S.W. Physicochemical, functional and structural properties of vicilin-rich protein isolates from three Phaseolus legumes: Effect of heat treatment. Food Hydrocolloids 2009, 23:1771-1778.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1771-1778
    • Tang, C.H.1    Sun, X.2    Yin, S.W.3
  • 25
    • 42549127262 scopus 로고    scopus 로고
    • Functional properties of grass carp (Ctenopharyngodon idella), nile perch (Lates niloticus) and nile tilapia (Oreochromis niloticus) skin hydrolysates
    • Wasswa J., Tang J., Gu X. Functional properties of grass carp (Ctenopharyngodon idella), nile perch (Lates niloticus) and nile tilapia (Oreochromis niloticus) skin hydrolysates. International Journal of Food Properties 2008, 11:339-350.
    • (2008) International Journal of Food Properties , vol.11 , pp. 339-350
    • Wasswa, J.1    Tang, J.2    Gu, X.3
  • 26
    • 0038215686 scopus 로고    scopus 로고
    • Solubility of protein
    • Springer-Verlag, Berlin, J.F. Zayas (Ed.)
    • Zayas J.F. Solubility of protein. Functionality of proteins in food 1997, 6-22. Springer-Verlag, Berlin. J.F. Zayas (Ed.).
    • (1997) Functionality of proteins in food , pp. 6-22
    • Zayas, J.F.1
  • 27
    • 0023959257 scopus 로고
    • Temperature adaptation of lactate dehydrogenase: Structural, functional and genetic aspects
    • Zuber H. Temperature adaptation of lactate dehydrogenase: Structural, functional and genetic aspects. Biophysical Chemistry 1988, 29:171-179.
    • (1988) Biophysical Chemistry , vol.29 , pp. 171-179
    • Zuber, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.