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Volumn 90, Issue 3, 2010, Pages 409-417

Effect of acetic acid deamidation-induced modification on functional and nutritional properties and conformation of wheat gluten

Author keywords

Acetic acid; Deamidation; Functional properties; Nutritional characteristics; Protein conformation; Wheat gluten

Indexed keywords

ACETIC ACID; AMINO ACID; GLUTEN; HYDROCHLORIC ACID; NITROGEN; PEPTIDE; SULFUR; VEGETABLE PROTEIN;

EID: 73349103194     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3830     Document Type: Article
Times cited : (79)

References (33)
  • 1
    • 0000575127 scopus 로고
    • Conformation and surface properties of deamidated gluten
    • Matsudomi N, Kato A and Kobayashi K, Conformation and surface properties of deamidated gluten. Agric Biol Chem 46:1583-1586 (1982).
    • (1982) Agric Biol Chem , vol.46 , pp. 1583-1586
    • Matsudomi, N.1    Kato, A.2    Kobayashi, K.3
  • 3
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • Wright HT and Urry DW, Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit Rev Biochem Mol Biol 26:41-52 (1991).
    • (1991) Crit Rev Biochem Mol Biol , vol.26 , pp. 41-52
    • Wright, H.T.1    Urry, D.W.2
  • 4
    • 0013086446 scopus 로고
    • Modification of food proteins by non-enzymatic methods, in Biochemistry of Food Proteins
    • ed. by Hudson BJF, London
    • Shih FF, Modification of food proteins by non-enzymatic methods, in Biochemistry of Food Proteins, ed. by Hudson BJF. Elsevier Applied Science, London, pp. 235-248 (1992).
    • (1992) Elsevier Applied Science , pp. 235-248
    • Shih, F.F.1
  • 5
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
    • Tyler-Cross R and Schirch V, Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J Biol Chem 33:22549-22556 (1991).
    • (1991) J Biol Chem , vol.33 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2
  • 6
    • 0000105243 scopus 로고
    • Comparative study on kinetics of nonenzymatic deamidation of soy protein and egg white lysozyme
    • Zhang J, Lee TC and Ho CT, Comparative study on kinetics of nonenzymaticdeamidationofsoyproteinandegg whitelysozyme. J Agric Food Chem 41:2286-2290 (1993).
    • (1993) J Agric Food Chem , vol.41 , pp. 2286-2290
    • Zhang, J.1    Lee, T.C.2    Ho, C.T.3
  • 7
    • 1842428450 scopus 로고
    • Wheat gliadin in foams for food products
    • McDonald CE and Pence JW, Wheat gliadin in foams for food products. Food Technol 15:141-146 (1961).
    • (1961) Food Technol , vol.15 , pp. 141-146
    • McDonald, C.E.1    Pence, J.W.2
  • 8
    • 0016958589 scopus 로고
    • Preparation and properties of acid-solubilized gluten conformation
    • Wu CH, Nakai S and Powrie WD, Preparation and properties of acid-solubilized gluten conformation. J Agric Food Chem 24:504-510 (1976).
    • (1976) J Agric Food Chem , vol.24 , pp. 504-510
    • Wu, C.H.1    Nakai, S.2    Powrie, W.D.3
  • 9
    • 0001407358 scopus 로고
    • Conformational changes and functional properties of acid-modified soy protein
    • Matsudomi N, Sasaki T, Kato A and Kobayashi K, Conformational changes and functional properties of acid-modified soy protein. J Agric Biol Chem 49:1251-1256 (1985).
    • (1985) J Agric Biol Chem , vol.49 , pp. 1251-1256
    • Matsudomi, N.1    Sasaki, T.2    Kato, A.3    Kobayashi, K.4
  • 10
    • 73149101935 scopus 로고
    • Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin
    • Batt CA, Identification and characterization of deamidation sites in the conserved regions of human immunoglobulin. J Food Sci 52:1583-1587 (1987).
    • (1987) J Food Sci , vol.52 , pp. 1583-1587
    • Batt, C.A.1
  • 11
    • 0032850080 scopus 로고    scopus 로고
    • Acid modification of proteins from soymilk residue (okara)
    • Chan WM and Ma CY, Acid modification of proteins from soymilk residue (okara). Food Res Int 32:119-127 (1999).
    • (1999) Food Res Int , vol.32 , pp. 119-127
    • Chan, W.M.1    Ma, C.Y.2
  • 13
    • 0015341416 scopus 로고
    • Preparation and isolation of acid-catalyzed hydrolysates from wheat gluten
    • Aranyi C and Hawrylewiczl EJ, Preparation and isolation of acid-catalyzed hydrolysates from wheat gluten. J Agric Food Chem 20:670-675 (1972).
    • (1972) J Agric Food Chem , vol.20 , pp. 670-675
    • Aranyi, C.1    Hawrylewiczl, E.J.2
  • 16
    • 0001121937 scopus 로고
    • Effects of deamidation with chymotrypsin at pH 10 on the functional properties of proteins
    • Kato A, Tanaka A, Lee Y, Matsudomi N and Kobayashi K, Effects of deamidation with chymotrypsin at pH 10 on the functional properties of proteins. J Agric Food Chem 35:285-288 (1987).
    • (1987) J Agric Food Chem , vol.35 , pp. 285-288
    • Kato, A.1    Tanaka, A.2    Lee, Y.3    Matsudomi, N.4    Kobayashi, K.5
  • 17
    • 0018536145 scopus 로고
    • Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenosulfonic acid
    • Ader-Nissen J, Determination of degree of hydrolysis of food protein hydrolysates by trinitrobenzenosulfonic acid. J Agric Food Chem 27:1256-1262 (1979).
    • (1979) J Agric Food Chem , vol.27 , pp. 1256-1262
    • Ader-Nissen, J.1
  • 18
    • 0015579498 scopus 로고
    • A simplified method for a quantitative assay of small amounts of protein in biological material
    • Schacterle GR and Pollack RL, A simplified method for a quantitative assay of small amounts of protein in biological material. Anal Biochem 51:654-655 (1973).
    • (1973) Anal Biochem , vol.51 , pp. 654-655
    • Schacterle, G.R.1    Pollack, R.L.2
  • 19
    • 0004202155 scopus 로고
    • AOAC, 15th edn). Association of Official Analytical Chemists, Arlington, VA
    • AOAC, Official Methods of Analysis (15th edn). Association of Official Analytical Chemists, Arlington, VA (1990).
    • (1990) Official Methods of Analysis
  • 20
    • 0001296380 scopus 로고    scopus 로고
    • Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes
    • Haskard CA and Li-Chan ECY, Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes. J Agric Food Chem 46:2671-2677 (1998).
    • (1998) J Agric Food Chem , vol.46 , pp. 2671-2677
    • Haskard, C.A.1    Li-Chan, E.C.Y.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce KN and Kinsella JE, Emulsifying properties of proteins: evaluation of a turbidimetric technique. J Agric Food Chem 26:716-723 (1978).
    • (1978) J Agric Food Chem , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 23
    • 0026104647 scopus 로고
    • Enzymatic modification of soy protein concentrates by fungal and bacterial proteases
    • Bernardi DLS, Pilosof AMR and Bartholomal GB, Enzymatic modification of soy protein concentrates by fungal and bacterial proteases. J Am Oil Chem Soc 68:102-105 (1991).
    • (1991) J Am Oil Chem Soc , vol.68 , pp. 102-105
    • Bernardi, D.L.S.1    Pilosof, A.M.R.2    Bartholomal, G.B.3
  • 24
    • 0023305467 scopus 로고
    • A new, rapid and high sensitivity analysis of amino acid in food type samples
    • Bildlingmeyer BA, Cohen SA, Tarvin TL and Frost B, A new, rapid and high sensitivity analysis of amino acid in food type samples. J Assoc Off Anal Chem 70:241-247 (1987).
    • (1987) J Assoc Off Anal Chem , vol.70 , pp. 241-247
    • Bildlingmeyer, B.A.1    Cohen, S.A.2    Tarvin, T.L.3    Frost, B.4
  • 25
    • 0009849104 scopus 로고
    • SDS-catalyzed deamidation of oilseed proteins
    • Shih FF and Kalmar AD, SDS-catalyzed deamidation of oilseed proteins. J Agric Food Chem 35:671-675 (1987).
    • (1987) J Agric Food Chem , vol.35 , pp. 671-675
    • Shih, F.F.1    Kalmar, A.D.2
  • 26
    • 0025769655 scopus 로고
    • Near-infrared Fourier transform Raman and conventional Raman studies of calf-crystallins in the lyophilized state and in solution
    • Chen W, Nie SM and Kuck JFR, Near-infrared Fourier transform Raman and conventional Raman studies of calf-crystallins in the lyophilized state and in solution. J Biophys 60:447-455 (1991).
    • (1991) J Biophys , vol.60 , pp. 447-455
    • Chen, W.1    Nie, S.M.2    Kuck, J.F.R.3
  • 27
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method
    • Raussens V, Ruysschaert JM and Goormaghtigh E, Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method. Anal Biochem 319:114-121 (2003).
    • (2003) Anal Biochem , vol.319 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 28
    • 13844267690 scopus 로고    scopus 로고
    • Effects of some additives on wheat gluten solubility: A structural approach
    • Mejri M, Roge B, BenSouissi A, Michels F and Mathlouthi M, Effects of some additives on wheat gluten solubility: a structural approach. Food Chem 92:7-15 (2005).
    • (2005) Food Chem , vol.92 , pp. 7-15
    • Mejri, M.1    Roge, B.2    Bensouissi, A.3    Michels, F.4    Mathlouthi, M.5
  • 29
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • Wang JS, Zhao MM and Yang XQ, Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration. J Cereal Sci 44:93-100 (2006).
    • (2006) J Cereal Sci , vol.44 , pp. 93-100
    • Wang, J.S.1    Zhao, M.M.2    Yang, X.Q.3
  • 30
    • 0017709445 scopus 로고
    • β-Turn in proteins
    • Chou PY and Fasman GD, β-Turn in proteins. J Mol Biol 115:135-175 (1977).
    • (1977) J Mol Biol , vol.115 , pp. 135-175
    • Chou, P.Y.1    Fasman, G.D.2
  • 31
    • 0000117038 scopus 로고
    • Relationships between hydrophobicity and foaming characteristics of food proteins
    • Townsend A and Nakai S, Relationships between hydrophobicity and foaming characteristics of food proteins. J Food Sci 48:588-594 (1983).
    • (1983) J Food Sci , vol.48 , pp. 588-594
    • Townsend, A.1    Nakai, S.2
  • 32
    • 0003000024 scopus 로고
    • Modification of food proteins by enzymatic methods, in Biochemistry of Food Proteins
    • ed. by Hudson BJF, New York, NY
    • Hamada JS, Modification of food proteins by enzymatic methods, in Biochemistry of Food Proteins, ed. by Hudson BJF. Elsevier Applied Science, New York, NY, pp. 249-270 (1992).
    • (1992) Elsevier Applied Science , pp. 249-270
    • Hamada, J.S.1
  • 33
    • 0016188201 scopus 로고
    • Deamidation of glutaminyl residues: Dependence on pH, temperature, and ionic strength
    • Scotchler JW and Robinson AB, Deamidation of glutaminyl residues: dependence on pH, temperature, and ionic strength. Anal Biochem 59:319-322 (1974).
    • (1974) Anal Biochem , vol.59 , pp. 319-322
    • Scotchler, J.W.1    Robinson, A.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.