Casein hydrolysate. III. Some functional properties of hydrophobic peptides synthesized from hydrolysate

Two different kinds of ‘plastein type’ peptide preparations, one dispersible (yield 97%, w/w of total casein) and the other indispersible (yield 3% w/w of total casein) in water, were synthesized by treating casein hydrolysate with papain. These preparations gave similar elusion patterns by reverse...

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Published inFood hydrocolloids Vol. 5; no. 6; pp. 573 - 579
Main Authors Mozaffar, Zahid, Haque, Zahur U.
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 01.02.1992
Elsevier
Subjects
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
Biotechnology
Food industries
Fundamental and applied biological sciences. Psychology
Hydrolysis
Casein
Peptides
Enzyme
Gel electrophoresis
HPLC chromatography
Papain
Hydrophobicity
Immobilized enzyme
Physicochemical properties
Thermal stability
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Abstract Two different kinds of ‘plastein type’ peptide preparations, one dispersible (yield 97%, w/w of total casein) and the other indispersible (yield 3% w/w of total casein) in water, were synthesized by treating casein hydrolysate with papain. These preparations gave similar elusion patterns by reverse phase high performance liquid chromatography (HPLC) and gave large aggregates with electrophoretic mobility, comparable to that of non-modified casein by non-SDS—PAGE. These aggregates were dissociated by sodium dodecyl sulfate (SDS), indicating non-covalent interaction. Oil holding capacity of both peptide preparations was significantly improved compared to casein or its hydrolysate. The dispersible peptide preparation was highly soluble at neutral pH and was more thermostable than casein. Emulsion activity and stability of both preparations were decreased.
AbstractList Two different kinds of ‘plastein type’ peptide preparations, one dispersible (yield 97%, w/w of total casein) and the other indispersible (yield 3% w/w of total casein) in water, were synthesized by treating casein hydrolysate with papain. These preparations gave similar elusion patterns by reverse phase high performance liquid chromatography (HPLC) and gave large aggregates with electrophoretic mobility, comparable to that of non-modified casein by non-SDS—PAGE. These aggregates were dissociated by sodium dodecyl sulfate (SDS), indicating non-covalent interaction. Oil holding capacity of both peptide preparations was significantly improved compared to casein or its hydrolysate. The dispersible peptide preparation was highly soluble at neutral pH and was more thermostable than casein. Emulsion activity and stability of both preparations were decreased.
Author Mozaffar, Zahid
Haque, Zahur U.
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1992 INIST-CNRS
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Issue 6
Keywords Hydrolysis
Casein
Peptides
Enzyme
Gel electrophoresis
HPLC chromatography
Papain
Hydrophobicity
Immobilized enzyme
Physicochemical properties
Thermal stability
Language English
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References Yamashita, Arai, Kokubo, Aso, Fujimaki (bib5) 1974; 38
Mozaffar, Haque (bib10) 1992; 5
Andrews, Alichanidis (bib13) 1990; 35
Bohoua, Haque (bib15) 1990; 73
Yamashita, Arai, Imaizumi, Amano, Fujimaki (bib6) 1979; 27
Fujimaki (bib4) 1978; 32
Fujimaki, Utaka, Yamashita, Arai (bib1) 1973; 37
Haque, Kinsella (bib14) 1988; 43
Rosas-Romero, Baratta (bib16) 1987; 37
Sukan, Andrews (bib8) 1982; 49
Aso, Yamashita, Arai, Suzuki, Fujimaki (bib2) 1977; 25
Haque, Mozaffar (bib11) 1992; 5
Eriksen, Fagerson (bib3) 1976; 41
Aso, Kimura, Watanabe, Arai (bib7) 1985; 49
Sukan, Andrews (bib9) 1982; 49
Haque, Kinsella (bib12) 1988; 53
References_xml – volume: 37
  start-page: 2303
  year: 1973
  end-page: 2312
  ident: bib1
  publication-title: Agric. Biol. Chem.
  contributor:
    fullname: Arai
– volume: 37
  start-page: 85
  year: 1987
  end-page: 96
  ident: bib16
  publication-title: Qual. Plant Plant Foods Hum. Nutr.
  contributor:
    fullname: Baratta
– volume: 49
  start-page: 1649
  year: 1985
  end-page: 1654
  ident: bib7
  publication-title: Agric. Biol. Chem.
  contributor:
    fullname: Arai
– volume: 25
  start-page: 1138
  year: 1977
  end-page: 1141
  ident: bib2
  publication-title: J. Agric. Food Chem.
  contributor:
    fullname: Fujimaki
– volume: 32
  start-page: 233
  year: 1978
  end-page: 241
  ident: bib4
  publication-title: Ann. Nutr. Aliment.
  contributor:
    fullname: Fujimaki
– volume: 38
  start-page: 1269
  year: 1974
  end-page: 1271
  ident: bib5
  publication-title: Agric. Biol. Chem.
  contributor:
    fullname: Fujimaki
– volume: 53
  start-page: 416
  year: 1988
  end-page: 420
  ident: bib12
  publication-title: J. Food Sci.
  contributor:
    fullname: Kinsella
– volume: 73
  start-page: 104
  year: 1990
  ident: bib15
  publication-title: J. Dairy Sci.
  contributor:
    fullname: Haque
– volume: 43
  start-page: 236
  year: 1988
  end-page: 240
  ident: bib14
  publication-title: Milchwissenschaft
  contributor:
    fullname: Kinsella
– volume: 5
  start-page: 549
  year: 1992
  end-page: 557
  ident: bib10
  publication-title: Food Hydrocoll.
  contributor:
    fullname: Haque
– volume: 27
  start-page: 52
  year: 1979
  end-page: 56
  ident: bib6
  publication-title: J. Agric. Food Chem.
  contributor:
    fullname: Fujimaki
– volume: 35
  start-page: 243
  year: 1990
  end-page: 262
  ident: bib13
  publication-title: Food Chem.
  contributor:
    fullname: Alichanidis
– volume: 41
  start-page: 490
  year: 1976
  end-page: 493
  ident: bib3
  publication-title: J. Food Sci.
  contributor:
    fullname: Fagerson
– volume: 49
  start-page: 265
  year: 1982
  end-page: 278
  ident: bib8
  publication-title: J. Dairy Res.
  contributor:
    fullname: Andrews
– volume: 49
  start-page: 279
  year: 1982
  end-page: 294
  ident: bib9
  publication-title: J. Dairy Res.
  contributor:
    fullname: Andrews
– volume: 5
  start-page: 559
  year: 1992
  end-page: 571
  ident: bib11
  publication-title: Food Hydrocoll.
  contributor:
    fullname: Mozaffar
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SubjectTerms Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
Biological and medical sciences
Biotechnology
Food industries
Fundamental and applied biological sciences. Psychology
Title Casein hydrolysate. III. Some functional properties of hydrophobic peptides synthesized from hydrolysate
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