메뉴 건너뛰기




Volumn 61, Issue 49, 2013, Pages 12139-12145

Effects of malondialdehyde modification on the in vitro digestibility of soy protein isolate

Author keywords

amino acid; electrophoresis; in vitro digestibility; MDA; Schiff base; soy protein isolate

Indexed keywords

CALORIMETRIC ENTHALPIES; IN-VITRO; IN-VITRO DIGESTIONS; LIPID PEROXIDATION; MDA; NON-COVALENT INTERACTION; SCHIFF-BASE; SOY PROTEIN ISOLATES;

EID: 84890500338     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf404099y     Document Type: Article
Times cited : (62)

References (36)
  • 1
    • 0025734606 scopus 로고
    • Soy protein in relation to human protein and amino acid nutrition
    • Young, V. R. Soy protein in relation to human protein and amino acid nutrition J. Am. Diet. Assoc. 1991, 91, 828-835
    • (1991) J. Am. Diet. Assoc. , vol.91 , pp. 828-835
    • Young, V.R.1
  • 2
    • 0034681114 scopus 로고    scopus 로고
    • Modifications of proteins by polyunsaturated fatty acid peroxidation products
    • Refsgaard, H. H. F.; Tsai, L.; Stadtman, E. R. Modifications of proteins by polyunsaturated fatty acid peroxidation products Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 611-616
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 611-616
    • Refsgaard, H.H.F.1    Tsai, L.2    Stadtman, E.R.3
  • 3
    • 0032892342 scopus 로고    scopus 로고
    • Fluorescence due to interactions of oxidizing soybean oil and soy proteins
    • Liang, J.-H. Fluorescence due to interactions of oxidizing soybean oil and soy proteins Food Chem. 1999, 66, 103-108
    • (1999) Food Chem. , vol.66 , pp. 103-108
    • Liang, J.-H.1
  • 4
    • 0033829087 scopus 로고    scopus 로고
    • Kinetics of fluorescence formation in whole milk powders during oxidation
    • Liang, J.-H. Kinetics of fluorescence formation in whole milk powders during oxidation Food Chem. 2000, 71, 459-463
    • (2000) Food Chem. , vol.71 , pp. 459-463
    • Liang, J.-H.1
  • 5
    • 79960699367 scopus 로고    scopus 로고
    • Effects of oxidative modification on thermal aggregation and gel properties of soy protein by malondialdehyde
    • 10.1007/s13197-011-0533-7
    • Wu, W.; Hua, Y.; Lin, Q. Effects of oxidative modification on thermal aggregation and gel properties of soy protein by malondialdehyde J. Food Sci. Technol. 2011, 10.1007/s13197-011-0533-7
    • (2011) J. Food Sci. Technol.
    • Wu, W.1    Hua, Y.2    Lin, Q.3
  • 6
    • 79960699367 scopus 로고    scopus 로고
    • Effects of oxidative modification on thermal aggregation and gel properties of soy protein by peroxyl radicals
    • Wu, W.; Hua, Y.; Lin, Q.; Xiao, H. Effects of oxidative modification on thermal aggregation and gel properties of soy protein by peroxyl radicals Int. J. Food Sci. Technol. 2011, 46, 1891-1897
    • (2011) Int. J. Food Sci. Technol. , vol.46 , pp. 1891-1897
    • Wu, W.1    Hua, Y.2    Lin, Q.3    Xiao, H.4
  • 7
    • 84875627100 scopus 로고    scopus 로고
    • Effect of oxidation on the emulsifying properties of soy protein isolate
    • Chen, N.; Zhao, M.; Sun, W.; Ren, J.; Cui, C. Effect of oxidation on the emulsifying properties of soy protein isolate Food Res. Int. 2013, 52, 26-32
    • (2013) Food Res. Int. , vol.52 , pp. 26-32
    • Chen, N.1    Zhao, M.2    Sun, W.3    Ren, J.4    Cui, C.5
  • 8
    • 84879830459 scopus 로고    scopus 로고
    • Effect of protein oxidation on the in vitro digestibility of soy protein isolate
    • Chen, N.; Zhao, M.; Sun, W. Effect of protein oxidation on the in vitro digestibility of soy protein isolate Food Chem. 2013, 141, 3224-3229
    • (2013) Food Chem. , vol.141 , pp. 3224-3229
    • Chen, N.1    Zhao, M.2    Sun, W.3
  • 9
    • 0001679509 scopus 로고
    • Lipid hydroperoxide reactivity with proteins and amino acids: A review
    • Gardner, H. W. Lipid hydroperoxide reactivity with proteins and amino acids: a review J. Agric. Food Chem. 1979, 27, 220-229
    • (1979) J. Agric. Food Chem. , vol.27 , pp. 220-229
    • Gardner, H.W.1
  • 10
    • 84985241735 scopus 로고
    • Malonaldehyde concentrations in food are affected by cooking conditions
    • Newburg, D. S.; Concon, J. M. Malonaldehyde concentrations in food are affected by cooking conditions J. Food Sci. 1980, 45, 1681-1683
    • (1980) J. Food Sci. , vol.45 , pp. 1681-1683
    • Newburg, D.S.1    Concon, J.M.2
  • 11
    • 0032167889 scopus 로고    scopus 로고
    • Formation of liver microsomal MDA-protein adducts in mice with chronic dietary iron overload
    • Valerio, L. G., Jr.; Petersen, D. R. Formation of liver microsomal MDA-protein adducts in mice with chronic dietary iron overload Toxicol. Lett. 1998, 98, 31-39
    • (1998) Toxicol. Lett. , vol.98 , pp. 31-39
    • Valerio Jr., L.G.1    Petersen, D.R.2
  • 12
    • 84868314089 scopus 로고    scopus 로고
    • Differential oxidative modification of proteins in MRL+/+ and MRL/lpr mice: Increased formation of lipid peroxidation-derived aldehyde-protein adducts may contribute to accelerated onset of autoimmune response
    • Wang, G.; Li, H.; Firoze Khan, M. Differential oxidative modification of proteins in MRL+/+ and MRL/lpr mice: Increased formation of lipid peroxidation-derived aldehyde-protein adducts may contribute to accelerated onset of autoimmune response Free Radical Res. 2012, 46, 1472-1481
    • (2012) Free Radical Res. , vol.46 , pp. 1472-1481
    • Wang, G.1    Li, H.2    Firoze Khan, M.3
  • 13
    • 84987277428 scopus 로고
    • A multienzyme technique for estimating protein digestibility
    • Hsu, H. W.; Vavak, D. L.; Satterlee, L. D.; Miller, G. A. A multienzyme technique for estimating protein digestibility J. Food Sci. 1977, 42, 1269-1273
    • (1977) J. Food Sci. , vol.42 , pp. 1269-1273
    • Hsu, H.W.1    Vavak, D.L.2    Satterlee, L.D.3    Miller, G.A.4
  • 14
    • 34447301257 scopus 로고    scopus 로고
    • Effect of oxidation on in vitro digestibility of skeletal muscle
    • Santé-Lhoutellier, V.; Aubry, L.; Gatellier, P. Effect of oxidation on in vitro digestibility of skeletal muscle J. Agric. Food Chem. 2007, 55, 5343-5348
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 5343-5348
    • Santé-Lhoutellier, V.1    Aubry, L.2    Gatellier, P.3
  • 15
    • 46549088922 scopus 로고    scopus 로고
    • Effect of animal (lamb) diet and meat storage on myofibrillar protein oxidation and in vitro digestibility
    • Santé-Lhoutellier, V.; Engel, E.; Aubry, L.; Gatellier, P. Effect of animal (lamb) diet and meat storage on myofibrillar protein oxidation and in vitro digestibility Meat Sci. 2008, 79, 777-783
    • (2008) Meat Sci. , vol.79 , pp. 777-783
    • Santé-Lhoutellier, V.1    Engel, E.2    Aubry, L.3    Gatellier, P.4
  • 16
    • 28444464486 scopus 로고    scopus 로고
    • Soybean protein aggregation induced by lipoxygenase catalyzed linoleic acid oxidation
    • Huang, Y.; Hua, Y.; Qiu, A. Soybean protein aggregation induced by lipoxygenase catalyzed linoleic acid oxidation Food Res. Int. 2006, 39, 240-249
    • (2006) Food Res. Int. , vol.39 , pp. 240-249
    • Huang, Y.1    Hua, Y.2    Qiu, A.3
  • 17
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • Nielsen, P. M.; Petersen, D.; Dambmann, C. Improved method for determining food protein degree of hydrolysis J. Food Sci. 2001, 66, 642-646
    • (2001) J. Food Sci. , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambmann, C.3
  • 18
    • 84859919502 scopus 로고    scopus 로고
    • Formation of lysine-derived oxidation products and loss of tryptophan during processing of porcine patties with added avocado byproducts
    • Utrera, M.; Rodríguez-Carpena, J.-G.; Morcuende, D.; Estevez, M. Formation of lysine-derived oxidation products and loss of tryptophan during processing of porcine patties with added avocado byproducts J. Agric. Food Chem. 2012, 60, 3917-3926
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 3917-3926
    • Utrera, M.1    Rodríguez-Carpena, J.-G.2    Morcuende, D.3    Estevez, M.4
  • 19
    • 0023916408 scopus 로고
    • Protein determination using bicinchoninic acid in the presence of sulfhydryl reagents
    • Hill, H. D.; Straka, J. G. Protein determination using bicinchoninic acid in the presence of sulfhydryl reagents Anal. Biochem. 1988, 170, 203-208
    • (1988) Anal. Biochem. , vol.170 , pp. 203-208
    • Hill, H.D.1    Straka, J.G.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0033827809 scopus 로고    scopus 로고
    • Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates
    • Liu, G.; Xiong, Y. L.; Butterfield, D. A. Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates J. Food Sci. 2000, 65, 811-818
    • (2000) J. Food Sci. , vol.65 , pp. 811-818
    • Liu, G.1    Xiong, Y.L.2    Butterfield, D.A.3
  • 23
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer, H.; Schaur, R. J.; Zollner, H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radical Biol. Med. 1991, 11, 81-128
    • (1991) Free Radical Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 24
    • 84866724337 scopus 로고    scopus 로고
    • Mass spectrometric evidence of malonaldehyde and 4-hydroxynonenal adductions to radical-scavenging soy peptides
    • Zhao, J.; Chen, J.; Zhu, H.; Xiong, Y. L. Mass spectrometric evidence of malonaldehyde and 4-hydroxynonenal adductions to radical-scavenging soy peptides J. Agric. Food Chem. 2012, 60, 9727-9736
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 9727-9736
    • Zhao, J.1    Chen, J.2    Zhu, H.3    Xiong, Y.L.4
  • 25
    • 0037096983 scopus 로고    scopus 로고
    • Effects of modifications of α-crystallin on its chaperone and other properties
    • Derham, B. K.; Harding, J. J. Effects of modifications of α-crystallin on its chaperone and other properties Biochem. J. 2002, 364, 711-717
    • (2002) Biochem. J. , vol.364 , pp. 711-717
    • Derham, B.K.1    Harding, J.J.2
  • 26
    • 34648831597 scopus 로고    scopus 로고
    • Reaction of the indole group with malondialdehyde: Application for the derivatization of tryptophan residues in peptides
    • Foettinger, A.; Melmer, M.; Leitner, A.; Lindner, W. Reaction of the indole group with malondialdehyde: application for the derivatization of tryptophan residues in peptides Bioconjugate Chem. 2007, 18, 1678-1683
    • (2007) Bioconjugate Chem. , vol.18 , pp. 1678-1683
    • Foettinger, A.1    Melmer, M.2    Leitner, A.3    Lindner, W.4
  • 27
    • 43649088044 scopus 로고    scopus 로고
    • Protein-protein interactions during high-moisture extrusion for fibrous meat analogues and comparison of protein solubility methods using different solvent systems
    • Liu, K.; Hsieh, F.-H. Protein-protein interactions during high-moisture extrusion for fibrous meat analogues and comparison of protein solubility methods using different solvent systems J. Agric. Food Chem. 2008, 56, 2681-2687
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 2681-2687
    • Liu, K.1    Hsieh, F.-H.2
  • 28
    • 33645903211 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the thermal properties of soy protein isolates
    • Tang, C.-H.; Chen, Z.; Li, L.; Yang, X.-Q. Effect of transglutaminase treatment on the thermal properties of soy protein isolates Food Res. Int. 2006, 39, 704-711
    • (2006) Food Res. Int. , vol.39 , pp. 704-711
    • Tang, C.-H.1    Chen, Z.2    Li, L.3    Yang, X.-Q.4
  • 29
    • 77954556099 scopus 로고    scopus 로고
    • PH shifting alters solubility characteristics and thermal stability of soy protein isolate and its globulin fractions in different pH, salt concentration, and temperature conditions
    • Jiang, J.; Xiong, Y. L.; Chen, J. pH shifting alters solubility characteristics and thermal stability of soy protein isolate and its globulin fractions in different pH, salt concentration, and temperature conditions J. Agric. Food Chem. 2010, 58, 8035-8042
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 8035-8042
    • Jiang, J.1    Xiong, Y.L.2    Chen, J.3
  • 30
    • 84876150414 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory activity of soy protein subjected to selective hydrolysis and thermal processing
    • Margatan, W.; Ruud, K.; Wang, Q.; Markowski, T.; Ismail, B. Angiotensin converting enzyme inhibitory activity of soy protein subjected to selective hydrolysis and thermal processing J. Agric. Food Chem. 2013, 61, 3460-3467
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 3460-3467
    • Margatan, W.1    Ruud, K.2    Wang, Q.3    Markowski, T.4    Ismail, B.5
  • 31
    • 0000579294 scopus 로고
    • The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation
    • Arntfield, S. D.; Murray, E. D. The influence of processing parameters on food protein functionality. I. Differential scanning calorimetry as an indicator of protein denaturation Can. Inst. Food Sci. Technol. J. 1981, 14, 289-294
    • (1981) Can. Inst. Food Sci. Technol. J. , vol.14 , pp. 289-294
    • Arntfield, S.D.1    Murray, E.D.2
  • 32
    • 84907421537 scopus 로고
    • Electrophoretic, solubility, and functional properties of commercial soy protein isolates
    • Arrese, E. L.; Sorgentini, D. A.; Wagner, J. R.; Añón, M. C. Electrophoretic, solubility, and functional properties of commercial soy protein isolates J. Agric. Food Chem. 1991, 39, 1029-1032
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1029-1032
    • Arrese, E.L.1    Sorgentini, D.A.2    Wagner, J.R.3    Añón, M.C.4
  • 33
    • 84859152164 scopus 로고    scopus 로고
    • Microfluidization as a potential technique to modify surface properties of soy protein isolate
    • Shen, L.; Tang, C.-H. Microfluidization as a potential technique to modify surface properties of soy protein isolate Food Res. Int. 2012, 48, 108-118
    • (2012) Food Res. Int. , vol.48 , pp. 108-118
    • Shen, L.1    Tang, C.-H.2
  • 34
    • 67249118991 scopus 로고    scopus 로고
    • Structural modification of soy protein by the lipid peroxidation product malondialdehyde
    • Wu, W.; Zhang, C.; Hua, Y. Structural modification of soy protein by the lipid peroxidation product malondialdehyde J. Sci. Food Agric. 2009, 89, 1416-1423
    • (2009) J. Sci. Food Agric. , vol.89 , pp. 1416-1423
    • Wu, W.1    Zhang, C.2    Hua, Y.3
  • 35
    • 3142603220 scopus 로고    scopus 로고
    • Selective proteolysis of the glycinin and β-conglycinin fractions in a soy protein isolate by pepsin and papain with controlled pH and temperature
    • Tsumura, K.; Saito, T.; Kugimiya, W.; Inouye, K. Selective proteolysis of the glycinin and β-conglycinin fractions in a soy protein isolate by pepsin and papain with controlled pH and temperature J. Food Sci. 2004, 69, 363-367
    • (2004) J. Food Sci. , vol.69 , pp. 363-367
    • Tsumura, K.1    Saito, T.2    Kugimiya, W.3    Inouye, K.4
  • 36
    • 0022016803 scopus 로고
    • Protein digestion and amino acid and peptide absorption
    • Silk, D. B. A.; Grimble, G. K.; Rees, R. G. Protein digestion and amino acid and peptide absorption Proc. Nutr. Soc. 1985, 44, 63-72
    • (1985) Proc. Nutr. Soc. , vol.44 , pp. 63
    • Silk, D.B.A.1    Grimble, G.K.2    Rees, R.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.