메뉴 건너뛰기




Volumn 50, Issue 1, 2012, Pages 53-58

Structural modification of wheat gluten by dry heat-enhanced enzymatic hydrolysis

Author keywords

Dry heat; Enzymatic hydrolysis; FTIR; SE HPLC; Wheat gluten

Indexed keywords

TRITICUM AESTIVUM;

EID: 84861953369     PISSN: 13309862     EISSN: 13342606     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (18)

References (25)
  • 1
    • 57749110515 scopus 로고    scopus 로고
    • Effect of thermal treatment on the enzymatic hydrolysis of chicken proteins
    • C. Cui, X. Zhou, M. Zhao, B. Yang, Effect of thermal treatment on the enzymatic hydrolysis of chicken proteins, Innov. Food Sci. Emerg. Technol. 10 (2009) 37-41.
    • (2009) Innov. Food Sci. Emerg. Technol. , vol.10 , pp. 37-41
    • Cui, C.1    Zhou, X.2    Zhao, M.3    Yang, B.4
  • 2
    • 33646696127 scopus 로고    scopus 로고
    • Enzymatic proteolysis, under high pressure of soybean whey: Analysis of peptides and the allergen Gly m1 in the hydrolysates
    • E. Peñas, G. Préstamo, F. Polo, R. Gomez, Enzymatic proteolysis, under high pressure of soybean whey: Analysis of peptides and the allergen Gly m1 in the hydrolysates, Food Chem. 99 (2006) 569-573.
    • (2006) Food Chem , vol.99 , pp. 569-573
    • Peñas, E.1    Préstamo, G.2    Polo, F.3    Gomez, R.4
  • 3
    • 33748803590 scopus 로고    scopus 로고
    • Characteristics of Bellamya purificata snail foot protein and enzymatic hydrolysates
    • S.H. Xia, Z. Wang, S.Y. Xu, Characteristics of Bellamya purificata snail foot protein and enzymatic hydrolysates, Food Chem. 101 (2007) 1188-1196.
    • (2007) Food Chem , vol.101 , pp. 1188-1196
    • Xia, S.H.1    Wang, Z.2    Xu, S.Y.3
  • 4
    • 53949126169 scopus 로고    scopus 로고
    • Rheological behavior of heat--induced wheat gliadin gel
    • S. Sun, Y. Song, Q. Zheng, Rheological behavior of heat--induced wheat gliadin gel, Food Hydrocolloids, 23 (2009) 1054-1056.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1054-1056
    • Sun, S.1    Song, Y.2    Zheng, Q.3
  • 5
    • 33744974758 scopus 로고    scopus 로고
    • High pressure-induced changes in milk proteins and possible applications in dairy technology
    • F.R. Lopez, High pressure-induced changes in milk proteins and possible applications in dairy technology, Int. Dairy J. 16 (2006) 1119-1131.
    • (2006) Int. Dairy J. , vol.16 , pp. 1119-1131
    • Lopez, F.R.1
  • 6
    • 34547607821 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on rheological, thermal and structural changes in Basmati rice flour slurry
    • J. Ahmed, H.S. Ramaswamy, A. Ayad, I. Alli, P. Alvarez, Effect of high-pressure treatment on rheological, thermal and structural changes in Basmati rice flour slurry, J. Cereal Sci. 46 (2007) 148-156.
    • (2007) J. Cereal Sci. , vol.46 , pp. 148-156
    • Ahmed, J.1    Ramaswamy, H.S.2    Ayad, A.3    Alli, I.4    Alvarez, P.5
  • 7
    • 33646774999 scopus 로고    scopus 로고
    • Adsorption--induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis
    • N. Brandes, P.B. Welzel, C. Werner, L.W. Kroh, Adsorption--induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis, J. Colloid Interface Sci. 299 (2006) 56-69.
    • (2006) J. Colloid Interface Sci. , vol.299 , pp. 56-69
    • Brandes, N.1    Welzel, P.B.2    Werner, C.3    Kroh, L.W.4
  • 8
    • 27544467437 scopus 로고    scopus 로고
    • Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy
    • S.W. Ellepola, S.M. Choi, C.Y. Ma, Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy, Int. J. Biol. Macromol. 37 (2005) 12-20.
    • (2005) Int. J. Biol. Macromol. , vol.37 , pp. 12-20
    • Ellepola, S.W.1    Choi, S.M.2    Ma, C.Y.3
  • 9
    • 0034370011 scopus 로고    scopus 로고
    • Foaming properties of enzymatically hydrolysed wheat gluten
    • S.R. Drago, R.J. González, Foaming properties of enzymatically hydrolysed wheat gluten, Innov. Food Sci. Emerg. Technol. 1 (2001) 269-273.
    • (2001) Innov. Food Sci. Emerg. Technol. , vol.1 , pp. 269-273
    • Drago, S.R.1    González, R.J.2
  • 10
    • 33846230958 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates
    • X. Kong, H. Zhou, H. Qian, Enzymatic hydrolysis of wheat gluten by proteases and properties of the resulting hydrolysates, Food Chem. 102 (2007) 759-763.
    • (2007) Food Chem , vol.102 , pp. 759-763
    • Kong, X.1    Zhou, H.2    Qian, H.3
  • 11
    • 0032446301 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates
    • A. Achouri, Z. Wang, S. Xu, Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates, Food Res. Int. 31 (1998) 617-623.
    • (1998) Food Res. Int. , vol.31 , pp. 617-623
    • Achouri, A.1    Wang, Z.2    Xu, S.3
  • 12
    • 0035972696 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from FTIR spectra using neural networks
    • M. Severcan, F. Severcan, P.I. Haris, Estimation of protein secondary structure from FTIR spectra using neural networks, J. Mol. Struct. 565-566 (2001) 383-387.
    • (2001) J. Mol. Struct. , vol.565-566 , pp. 383-387
    • Severcan, M.1    Severcan, F.2    Haris, P.I.3
  • 13
    • 0029114262 scopus 로고
    • Molecular flexibility in wheat gluten proteins submitted to heating
    • J. Hargreaves, Y. Popineau, M.M. Le, M.A. Hemminga, Molecular flexibility in wheat gluten proteins submitted to heating, FEBS Lett. 372 (1995) 103-107.
    • (1995) FEBS Lett , vol.372 , pp. 103-107
    • Hargreaves, J.1    Popineau, Y.2    Le, M.M.3    Hemminga, M.A.4
  • 14
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • P.I. Haris, F. Severcan, FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media, J. Mol. Catal. B-Enzym. 7 (1999) 207-221.
    • (1999) J. Mol. Catal. B-Enzym. , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 15
    • 69249222742 scopus 로고    scopus 로고
    • Protein secondary structure content in solution, films and tissues: Redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra
    • E. Goormaghtigh, R. Gasper, A. Bénard, A. Goldsztein, V. Raussens, Protein secondary structure content in solution, films and tissues: Redundancy and complementarity of the information content in circular dichroism, transmission and ATR FTIR spectra, Biochim. Biophys. Acta, 1794 (2009) 1332- 1343.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1332-1343
    • Goormaghtigh, E.1    Gasper, R.2    Bénard, A.3    Goldsztein, A.4    Raussens, V.5
  • 16
    • 35948929431 scopus 로고    scopus 로고
    • Conformational changes in salivary proline-rich protein 1 upon adsorption to calcium phosphate crystals
    • S. Elangovan, H.C. Margolis, F.G. Oppenheim, E. Beniash, Conformational changes in salivary proline-rich protein 1 upon adsorption to calcium phosphate crystals, Langmuir, 23 (2007) 11200-11205.
    • (2007) Langmuir , vol.23 , pp. 11200-11205
    • Elangovan, S.1    Margolis, H.C.2    Oppenheim, F.G.3    Beniash, E.4
  • 17
    • 13844267690 scopus 로고    scopus 로고
    • Effects of some additives on wheat gluten solubility: A structural approach
    • M. Mejri, B. Rogé, A. BenSouissi, F. Michels, M. Mathlouthi, Effects of some additives on wheat gluten solubility: A structural approach, Food Chem. 92 (2005) 7-15.
    • (2005) Food Chem , vol.92 , pp. 7-15
    • Mejri, M.1    Rogé, B.2    BenSouissi, A.3    Michels, F.4    Mathlouthi, M.5
  • 18
    • 12144267492 scopus 로고    scopus 로고
    • Underlying hydrophobic sequence periodicity of protein tertiary structure
    • B.D. Silverman, Underlying hydrophobic sequence periodicity of protein tertiary structure, J. Biomol. Struct. Dyn. 22 (2005) 411-424.
    • (2005) J. Biomol. Struct. Dyn. , vol.22 , pp. 411-424
    • Silverman, B.D.1
  • 19
    • 39649119647 scopus 로고    scopus 로고
    • Effect of heat on rheology, surface hydrophobicity and molecular weight distribution of glutens extracted from flours with different bread-making quality
    • C.E. Stathopoulos, A.A. Tsiami, J.D. Schofield, B.J. Dobraszczyk, Effect of heat on rheology, surface hydrophobicity and molecular weight distribution of glutens extracted from flours with different bread-making quality, J. Cereal Sci. 47 (2008) 134-143.
    • (2008) J. Cereal Sci. , vol.47 , pp. 134-143
    • Stathopoulos, C.E.1    Tsiami, A.A.2    Schofield, J.D.3    Dobraszczyk, B.J.4
  • 20
    • 0034643864 scopus 로고    scopus 로고
    • Thermal behavior of native and hydrophobized wheat gluten, gliadin and glutenin-rich fractions by modulated DSC
    • V. Micard, S. Guilbert, Thermal behavior of native and hydrophobized wheat gluten, gliadin and glutenin-rich fractions by modulated DSC, Int. J. Biol. Macromol. 27 (2000) 229-236.
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 229-236
    • Micard, V.1    Guilbert, S.2
  • 21
    • 0036747380 scopus 로고    scopus 로고
    • High-pressure as a tool to study some proteins' properties: Conformational modification, activity and oligomeric dissociation
    • V. Lullien-Pellerin, C. Balny, High-pressure as a tool to study some proteins' properties: Conformational modification, activity and oligomeric dissociation, Innov. Food Sci. Emerg. Technol. 3 (2002) 209-221.
    • (2002) Innov. Food Sci. Emerg. Technol. , vol.3 , pp. 209-221
    • Lullien-Pellerin, V.1    Balny, C.2
  • 22
    • 0038301270 scopus 로고    scopus 로고
    • Cluster composition of liquid water derived from laser-Raman spectra and molecular simulation data
    • M. Starzak, M. Mathlouthi, Cluster composition of liquid water derived from laser-Raman spectra and molecular simulation data, Food Chem. 82 (2003) 3-22.
    • (2003) Food Chem , vol.82 , pp. 3-22
    • Starzak, M.1    Mathlouthi, M.2
  • 23
    • 68949214303 scopus 로고    scopus 로고
    • Characteristics of enzymatic hydrolysis of thermal-treated wheat gluten
    • J.S. Wang, Z.Y. Wei, L. Li, K. Bian, M.M. Zhao, Characteristics of enzymatic hydrolysis of thermal-treated wheat gluten, J. Cereal Sci. 50 (2009) 205-209.
    • (2009) J. Cereal Sci. , vol.50 , pp. 205-209
    • Wang, J.S.1    Wei, Z.Y.2    Li, L.3    Bian, K.4    Zhao, M.M.5
  • 24
    • 34047259662 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: Studies on gluten, gliadin and glutenin
    • R. Kieffer, F. Schurer, P. Köhler, H. Wieser, Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: Studies on gluten, gliadin and glutenin, J. Cereal Sci. 45 (2007) 285-292.
    • (2007) J. Cereal Sci. , vol.45 , pp. 285-292
    • Kieffer, R.1    Schurer, F.2    Köhler, P.3    Wieser, H.4
  • 25
    • 33847159988 scopus 로고    scopus 로고
    • Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates
    • E.L. da Costa, J.A. da Rocha Gontijo, F.M. Netto, Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates, Int. Dairy J. 17 (2007) 632-640.
    • (2007) Int. Dairy J. , vol.17 , pp. 632-640
    • Da Costa, E.L.1    Da Rocha Gontijo, J.A.2    Netto, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.