메뉴 건너뛰기




Volumn 119, Issue 3, 2013, Pages 573-579

Amaranth protein films from thermally treated proteins

Author keywords

Amaranth proteins; Mechanical properties; Protein cross linking; Protein films; Thermal treatment

Indexed keywords

AMARANTH PROTEIN ISOLATES; CROSS-LINKING DEGREE; DENATURATION TEMPERATURES; POLYPEPTIDE CHAIN; PROTEIN CROSSLINKING; PROTEIN FILMS; PROTEIN FRACTIONS; WATER SOLUBILITIES;

EID: 84880271397     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2013.06.006     Document Type: Article
Times cited : (23)

References (48)
  • 1
    • 77957596321 scopus 로고    scopus 로고
    • Influence of pH on structure and function of amaranth (Amaranthus hypochondriacus) protein isolates
    • L.E. Abugoch, N.E. Martínez, and M.C. Añón Influence of pH on structure and function of amaranth (Amaranthus hypochondriacus) protein isolates Cereal Chemistry 87 5 2010 448 453
    • (2010) Cereal Chemistry , vol.87 , Issue.5 , pp. 448-453
    • Abugoch, L.E.1    Martínez, N.E.2    Añón, M.C.3
  • 2
    • 0003995078 scopus 로고
    • AOAC, 15th ed. Association of Official Analytical Chemists Washington, DC
    • AOAC Official Methods of Analysis 15th ed. 1990 Association of Official Analytical Chemists Washington, DC
    • (1990) Official Methods of Analysis
  • 4
    • 0344774197 scopus 로고
    • Standard test methods for water vapor transmission of materials. Designation: E 96-80
    • ASTM ASTM, Philadelphia, PA
    • ASTM, 1989. Standard test methods for water vapor transmission of materials. Designation: E 96-80. Annual Book of ASTM Standards. ASTM, Philadelphia, PA, pp. 745-754.
    • (1989) Annual Book of ASTM Standards , pp. 745-754
  • 5
    • 0002810970 scopus 로고
    • Standard test methods for tensile properties of thin plastic sheeting
    • ASTM ASTM, Philadelphia, PA
    • ASTM, 1991. Standard test methods for tensile properties of thin plastic sheeting. Designation: D882-91. Annual Book of ASTM Standards. ASTM, Philadelphia, PA, pp. 182-190.
    • (1991) Designation: D882-91 , pp. 182-190
  • 6
    • 77549086369 scopus 로고
    • Standard test methods for moisture content of paper and paperboard by oven drying. Designation: D644-94
    • ASTM ASTM, Philadelphia, PA
    • ASTM, 1994. Standard test methods for moisture content of paper and paperboard by oven drying. Designation: D644-94. Annual Book of ASTM Standards. ASTM, Philadelphia, PA, pp. 1-2.
    • (1994) Annual Book of ASTM Standards , pp. 1-2
  • 7
    • 33847700119 scopus 로고    scopus 로고
    • Effect of thermal treatment on the proteins of amaranth isolates
    • DOI 10.1002/jsfa.2751
    • M.V. Avanza, and M.C. Añón Effect of thermal treatment on the proteins of amaranth isolates Journal of the Science of Food and Agriculture 87 2007 616 623 (Pubitemid 46374839)
    • (2007) Journal of the Science of Food and Agriculture , vol.87 , Issue.4 , pp. 616-623
    • Avanza, M.V.1    Anon, M.C.2
  • 8
    • 84907421467 scopus 로고    scopus 로고
    • Rheological characterization of amaranth protein gels
    • DOI 10.1016/j.foodhyd.2004.12.002
    • M.V. Avanza, M.C. Puppo, and M.C. Añón Rheological characterization of amaranth protein gels Food Hydrocolloids 19 2005 889 898 (Pubitemid 40545964)
    • (2005) Food Hydrocolloids , vol.19 , Issue.5 , pp. 889-898
    • Avanza, M.V.1    Puppo, M.C.2    Anon, M.C.3
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Analytical Biochemistry 72 1976 248 254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
  • 11
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from hat-denatured whey
    • DOI 10.1016/S0924-2244(98)00031-4, PII S0924224498000314
    • C.M. Bryant, and D.J. McClements Molecular bases of protein functionality with special consideration of cold-set gels derived from heat-denatured whey Trends Food Science and Technology 9 4 1998 143 151 (Pubitemid 28348656)
    • (1998) Trends in Food Science and Technology , vol.9 , Issue.4 , pp. 143-151
    • Bryant, C.M.1    Julian McClements, D.2
  • 12
    • 34047248365 scopus 로고    scopus 로고
    • Preparation and physical properties of soy protein isolate and gelatin composite films
    • DOI 10.1016/j.foodhyd.2006.09.001, PII S0268005X06002037
    • N. Cao, Y. Fu, and J. He Preparation and physical properties of soy protein isolate and gelatin composite films Food Hydrocolloids 21 2007 1153 1162 (Pubitemid 46546505)
    • (2007) Food Hydrocolloids , vol.21 , Issue.7 , pp. 1153-1162
    • Cao, N.1    Fu, Y.2    He, J.3
  • 13
    • 0036287555 scopus 로고    scopus 로고
    • Film-forming mechanism and heat denaturation effects on the physical and chemical properties of pea-protein-isolate edible films
    • W.S. Choi, and J.H. Han Film-forming mechanism and heat denaturation effects on the physical and chemical properties of pea-protein-isolate edible films Journal of Food Science 67 4 2002 1399 1406 (Pubitemid 34696098)
    • (2002) Journal of Food Science , vol.67 , Issue.4 , pp. 1399-1406
    • Choi, W.S.1    Han, J.H.2
  • 14
    • 0031937086 scopus 로고    scopus 로고
    • Proteins as agricultural polymers for packaging production
    • B. Cuq, N. Gontard, and S. Guilbert Proteins as agricultural polymers for packaging production Cereal Chemistry 75 1998 1 9 (Pubitemid 28131977)
    • (1998) Cereal Chemistry , vol.75 , Issue.1 , pp. 1-9
    • Cuq, B.1    Gontard, N.2    Guilbert, S.3
  • 15
    • 0029174274 scopus 로고
    • Disulfide bonds in protein folding and stability
    • B.A. Shirley, Humana Press, Inc. Totowa, New Jersey
    • N. Darby, and T.E. Creighton Disulfide bonds in protein folding and stability B.A. Shirley, Protein Stability and Folding: Theory and Practice 1995 Humana Press, Inc. Totowa, New Jersey 219 252
    • (1995) Protein Stability and Folding: Theory and Practice , pp. 219-252
    • Darby, N.1    Creighton, T.E.2
  • 18
    • 84880269719 scopus 로고    scopus 로고
    • Effect of potato oxidized starch on the physico-chemical properties of soy protein isolate-based edible films
    • in press
    • Galus, S., Lenart, A., Voilley, A., Debeaufort, F., in press. Effect of potato oxidized starch on the physico-chemical properties of soy protein isolate-based edible films. Food Technology and Biotechnology.
    • Food Technology and Biotechnology
    • Galus, S.1    Lenart, A.2    Voilley, A.3    Debeaufort, F.4
  • 20
    • 0000257069 scopus 로고
    • Edible films and coatings from soymilk and soy protein
    • A. Gennadios, and C.L. Weller Edible films and coatings from soymilk and soy protein Cereal Foods World 36 1991 1004 1009
    • (1991) Cereal Foods World , vol.36 , pp. 1004-1009
    • Gennadios, A.1    Weller, C.L.2
  • 21
    • 0002147601 scopus 로고
    • Edible coatings and film based on proteins
    • J.M. Krochta, E.A. Baldwin, M. Nisperos-Carriedo, Technomic Publishing Co., Inc. Lancaster
    • A. Gennadios, T.H. McHugh, C.L. Weller, and J.M. Krochta Edible coatings and film based on proteins J.M. Krochta, E.A. Baldwin, M. Nisperos-Carriedo, Edible Coatings and Films to Improve Food Quality 1994 Technomic Publishing Co., Inc. Lancaster 201 278
    • (1994) Edible Coatings and Films to Improve Food Quality , pp. 201-278
    • Gennadios, A.1    McHugh, T.H.2    Weller, C.L.3    Krochta, J.M.4
  • 23
    • 84987349540 scopus 로고
    • Edible wheat gluten films: Influence of the main process variables on films properties using response surface methodology
    • N. Gontard, S. Guilbert, and J. Cuq Edible wheat gluten films: influence of the main process variables on films properties using response surface methodology Journal of Food Science 57 1992 190 195
    • (1992) Journal of Food Science , vol.57 , pp. 190-195
    • Gontard, N.1    Guilbert, S.2    Cuq, J.3
  • 24
    • 0000827783 scopus 로고
    • Technology and applications of edible protective films
    • M. Mathlouthi, Elsevier Science New York
    • S. Guilbert Technology and applications of edible protective films M. Mathlouthi, Food Packaging and Preservation: Theory and Practice 1986 Elsevier Science New York 371 394
    • (1986) Food Packaging and Preservation: Theory and Practice , pp. 371-394
    • Guilbert, S.1
  • 25
    • 69949096492 scopus 로고    scopus 로고
    • Effect of heat treatment of film-forming solution on the properties of film from cuttlefish (Sepia pharaonis) skin gelatine
    • M.S. Hoque, S. Benjakul, and T. Prodpran Effect of heat treatment of film-forming solution on the properties of film from cuttlefish (Sepia pharaonis) skin gelatine Journal of Food Engineering 96 2010 66 73
    • (2010) Journal of Food Engineering , vol.96 , pp. 66-73
    • Hoque, M.S.1    Benjakul, S.2    Prodpran, T.3
  • 26
    • 0002314075 scopus 로고
    • Edible films and coatings: A review
    • J.J. Kester, and O.R. Fennema Edible films and coatings: a review Food Technology 40 1986 47 58
    • (1986) Food Technology , vol.40 , pp. 47-58
    • Kester, J.J.1    Fennema, O.R.2
  • 27
    • 0035997458 scopus 로고    scopus 로고
    • Heat curing of soy protein films at selected temperatures and pressures
    • DOI 10.1006/fstl.2001.0825
    • K.M. Kim, C.L. Weller, M.A. Hanna, and A. Gennadios Heat curing of soy protein films at selected temperatures and pressures LWT - Food Science and Technology 35 2002 140 145 (Pubitemid 34800906)
    • (2002) LWT - Food Science and Technology , vol.35 , Issue.2 , pp. 140-145
    • Kim, K.M.1    Weller, C.L.2    Hanna, M.A.3    Gennadios, A.4
  • 28
    • 70549102292 scopus 로고    scopus 로고
    • Water vapor permeability, thermal and wetting properties of whey protein isolate based edible films
    • S. Kokoszka, F. Debeaufortm, A. Lenart, and A. Voilley Water vapor permeability, thermal and wetting properties of whey protein isolate based edible films International Dairy Journal 20 2010 53 60
    • (2010) International Dairy Journal , vol.20 , pp. 53-60
    • Kokoszka, S.1    Debeaufortm, F.2    Lenart, A.3    Voilley, A.4
  • 30
    • 85052685949 scopus 로고    scopus 로고
    • Edible protein films and coatings
    • S. Damodaran, A. Paraf, Marcel Dekker New York
    • J.M. Krochta Edible protein films and coatings S. Damodaran, A. Paraf, Food Proteins and Their Applications 1997 Marcel Dekker New York 529 549
    • (1997) Food Proteins and Their Applications , pp. 529-549
    • Krochta, J.M.1
  • 31
    • 21344470927 scopus 로고    scopus 로고
    • Case history of grain amaranth as an alternative crop
    • J.W. Lehmann Case history of grain amaranth as an alternative crop Cereal Foods World 41 1996 399 411
    • (1996) Cereal Foods World , vol.41 , pp. 399-411
    • Lehmann, J.W.1
  • 32
    • 0033000586 scopus 로고    scopus 로고
    • Evidence confirming the existence of a 7S globulin-like storage protein in Amaranthus hypochondriacus seed
    • DOI 10.1016/S0308-8146(98)00221-0, PII S0308814698002210
    • M.F. Marcone Evidence confirming the existence of a 7S globulin-like storage protein in Amaranthus hypochondriacus seed Food Chemistry 65 1999 533 542 (Pubitemid 29142476)
    • (1999) Food Chemistry , vol.65 , Issue.4 , pp. 533-542
    • Marcone, M.F.1
  • 33
    • 2542574202 scopus 로고    scopus 로고
    • Composition and structural characterization of amaranth protein isolates
    • E.N. Martínez, and M.C. Añón Composition and structural characterization of amaranth protein isolates Journal of Agricultural and Food Chemistry 44 1996 2523 2530
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 2523-2530
    • Martínez, E.N.1    Añón, M.C.2
  • 35
    • 84907421511 scopus 로고    scopus 로고
    • Effect of the solution pH on solubility and some structural properties of soybean protein isolate films
    • A.N. Mauri, and M.C. Añón Effect of the solution pH on solubility and some structural properties of soybean protein isolate films Journal of the Science of Food and Agriculture 86 7 2006 1064 1072
    • (2006) Journal of the Science of Food and Agriculture , vol.86 , Issue.7 , pp. 1064-1072
    • Mauri, A.N.1    Añón, M.C.2
  • 36
    • 5844240927 scopus 로고
    • Hydrophilic edible films: Modified procedure for water vapor permeability and explanation of thickness effects
    • T.H. McHugh, R. Avena-Bustillos, and J.M. Krochta Hydrophilic edible films: modified procedure for water vapor permeability and explanation of thickness effects Journal of the Science of Food and Agriculture 58 1993 899 903
    • (1993) Journal of the Science of Food and Agriculture , vol.58 , pp. 899-903
    • McHugh, T.H.1    Avena-Bustillos, R.2    Krochta, J.M.3
  • 37
    • 4644251002 scopus 로고    scopus 로고
    • Effect of pH and ionic strength modifications on thermal denaturation of the 11S globulin of sunflower (Helianthus annuus)
    • M.I. Molina, S. Petruccelli, and M.C. Añón Effect of pH and ionic strength modifications on thermal denaturation of the 11S globulin of sunflower (Helianthus annuus) Journal of Agricultural Food Chemistry 52 2004 6023 6029
    • (2004) Journal of Agricultural Food Chemistry , vol.52 , pp. 6023-6029
    • Molina, M.I.1    Petruccelli, S.2    Añón, M.C.3
  • 38
    • 0034877450 scopus 로고    scopus 로고
    • Denaturation time and temperature effects on solubility, tensile properties, and oxygen permeability of whey protein edible films
    • M.B. Pérez-Gago, and J.M. Krochta Denaturation time and temperature effects on solubility, tensile properties, and oxygen permeability of whey protein edible films Journal of Food Science 66 5 2001 705 710 (Pubitemid 32752322)
    • (2001) Journal of Food Science , vol.66 , Issue.5 , pp. 705-710
    • Perez-gago, M.B.1    Krochta, J.M.2
  • 39
    • 0033379642 scopus 로고    scopus 로고
    • Water vapor permeability, solubility, and tensile properties of heat-denatured versus native whey protein films
    • M.B. Pérez-Gago, P. Nadaud, and J.M. Krochta Water vapor permeability, solubility, and tensile properties of heat-denatured versus native whey protein films Journal of Food Science 64 1999 1034 1037 (Pubitemid 30059502)
    • (1999) Journal of Food Science , vol.64 , Issue.6 , pp. 1034-1037
    • Perez-Gago, M.B.1    Nadaud, P.2    Krochta, J.M.3
  • 41
    • 77549085534 scopus 로고    scopus 로고
    • Biodegradable sunflower protein films naturally activated with antioxidant compounds
    • P.R. Salgado, S.E. Molina Ortiz, S. Petruccelli, and A.N. Mauri Biodegradable sunflower protein films naturally activated with antioxidant compounds Food Hydrocolloids 24 5 2010 525 533
    • (2010) Food Hydrocolloids , vol.24 , Issue.5 , pp. 525-533
    • Salgado, P.R.1    Molina Ortiz, S.E.2    Petruccelli, S.3    Mauri, A.N.4
  • 42
    • 0036403887 scopus 로고    scopus 로고
    • Amaranth protein isolates modified by hydrolytic and thermal treatments. Relationship between structure and solubility
    • DOI 10.1016/S0963-9969(02)00089-3, PII S0963996902000893
    • A.A. Scilingo, S.E. Molina, E.N. Martínez, and M.C. Añón Amaranth protein isolates modified by hydrolytic and thermal treatments. Relationship between structure and solubility Food Research International 35 9 2002 855 862 (Pubitemid 35224862)
    • (2002) Food Research International , vol.35 , Issue.9 , pp. 855-862
    • Scilingo, A.A.1    Molina Ortiz, S.E.2    Martinez, E.N.3    Aon, M.C.4
  • 44
    • 1542681443 scopus 로고    scopus 로고
    • Film-forming properties and edible films of plant proteins
    • F.F. Shih Film forming properties and edible films of plant proteins Nahrung 42 1998 254 256 (Pubitemid 128503185)
    • (1998) Nahrung - Food , vol.42 , Issue.3-4 , pp. 254-256
    • Shih, F.F.1
  • 45
    • 84986436992 scopus 로고
    • Enzymatic treatments and thermal effects on edible soy protein films
    • Y.M. Stuchell, and J.M. Krochta Enzymatic treatments and thermal effects on edible soy protein films Journal of Food Science 59 1994 1332 1337
    • (1994) Journal of Food Science , vol.59 , pp. 1332-1337
    • Stuchell, Y.M.1    Krochta, J.M.2
  • 46
    • 33947311515 scopus 로고    scopus 로고
    • Modulation of mechanical and surface hydrophobic properties of food protein films by transglutaminase treatment
    • DOI 10.1016/j.foodres.2006.09.010, PII S0963996906001554
    • C.H. Tang, and Y. Jiang Modulation of mechanical and surface hydrophobic properties of food protein films by transglutaminase treatment Food Research International 40 2007 504 509 (Pubitemid 46441849)
    • (2007) Food Research International , vol.40 , Issue.4 , pp. 504-509
    • Tang, C.-H.1    Jiang, Y.2
  • 47
    • 8344256558 scopus 로고    scopus 로고
    • Development and characterization of biofilms based on amaranth flour (Amaranthus caudatus)
    • D. Tapia-Blácido, P.J.A. Sobral, and F.C. Menegalli Development and characterization of biofilms based on amaranth flour (Amaranthus caudatus) Journal of Food Engineering 67 2005 215 223
    • (2005) Journal of Food Engineering , vol.67 , pp. 215-223
    • Tapia-Blácido, D.1    Sobral, P.J.A.2    Menegalli, F.C.3
  • 48
    • 34250815610 scopus 로고    scopus 로고
    • Contribution of the starch, protein, and lipid fractions to the physical, thermal, and structural properties of amaranth (Amaranthus caudatus) flour films
    • D. Tapia-Blácido, A.N. Mauri, F.C. Menegalli, P.J.A. Sobral, and M.C. Añón Contribution of the starch, protein, and lipid fractions to the physical, thermal, and structural properties of amaranth (Amaranthus caudatus) flour films Journal of Food Science 72 5 2007 293 300
    • (2007) Journal of Food Science , vol.72 , Issue.5 , pp. 293-300
    • Tapia-Blácido, D.1    Mauri, A.N.2    Menegalli, F.C.3    Sobral, P.J.A.4    Añón, M.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.