메뉴 건너뛰기




Volumn 15, Issue 3, 2012, Pages 638-655

Limited deamidation of soybean protein isolates by glutaminase and its impacts on the selected properties

Author keywords

Emulsify property; Glutaminase; Iron (II) chelating activity; Rheological property; Soybean protein isolates

Indexed keywords

CHELATING ACTIVITY; EMULSIFY PROPERTY; GLUTAMINASE; RHEOLOGICAL PROPERTY; SOYBEAN PROTEINS;

EID: 84860434347     PISSN: 10942912     EISSN: 15322386     Source Type: Journal    
DOI: 10.1080/10942912.2010.494760     Document Type: Article
Times cited : (19)

References (45)
  • 1
    • 85057431059 scopus 로고    scopus 로고
    • Enzymatic modification of proteins in food systems. In
    • Sikorski, Z.E.; Eds.; CRC Press: New York
    • Haard, N.F. Enzymatic modification of proteins in food systems. In: Chemical and Functional Properties of Food Proteins; Sikorski, Z.E.; Eds.; CRC Press: New York, 2001; 170-173.
    • (2001) Chemical and Functional Properties of Food Proteins , pp. 170-173
    • Haard, N.F.1
  • 2
    • 0028250433 scopus 로고
    • Deamidation of food proteins to improve functionality
    • Hamada, J.S. Deamidation of food proteins to improve functionality. Critical Reviews in Food Science & Nutrition 1994, 34 (3), 283-292.
    • (1994) Critical Reviews in Food Science & Nutrition , vol.34 , Issue.3 , pp. 283-292
    • Hamada, J.S.1
  • 3
    • 84985224923 scopus 로고
    • Preparation and functional properties of enzymatically deamidated soy proteins
    • Hamada, J.S.; Marshall, W.E. Preparation and functional properties of enzymatically deamidated soy proteins. Journal of Food Science 1989, 54 (3), 598-601.
    • (1989) Journal of Food Science , vol.54 , Issue.3 , pp. 598-601
    • Hamada, J.S.1    Marshall, W.E.2
  • 4
    • 0001129193 scopus 로고
    • Functional properties of deamidated oat protein isolates
    • Ma, C.Y.; Khanzada, G. Functional properties of deamidated oat protein isolates. Journal of Food Science 1987, 52 (6), 1583-1587.
    • (1987) Journal of Food Science , vol.52 , Issue.6 , pp. 1583-1587
    • Ma, C.Y.1    Khanzada, G.2
  • 5
    • 84985294295 scopus 로고
    • Effect of anions on the deamidation of soy protein
    • Shih, F.F. Effect of anions on the deamidation of soy protein. Journal of Food Science 1991, 56 (2), 452-454.
    • (1991) Journal of Food Science , vol.56 , Issue.2 , pp. 452-454
    • Shih, F.F.1
  • 6
    • 33748437518 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by proteinglutaminase on structure and functional properties of wheat gluten
    • Yong, Y.H.; Yamaguchi, S.; Matsumura, Y. Effects of enzymatic deamidation by proteinglutaminase on structure and functional properties of wheat gluten. Journal of Agricultural and Food Chemistry 2006, 54 (16), 6034-6040.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.16 , pp. 6034-6040
    • Yong, Y.H.1    Yamaguchi, S.2    Matsumura, Y.3
  • 7
    • 70149092311 scopus 로고    scopus 로고
    • Interfacial properties of deamidated wheat protein in relation to its ability to stabilize oil-in-water emulsions
    • Day, L.; Xu, M.; Lundin, L.; Wooster, T.J. Interfacial properties of deamidated wheat protein in relation to its ability to stabilize oil-in-water emulsions. Food Hydrocolloids 2009, 23 (8), 2158-2167.
    • (2009) Food Hydrocolloids , vol.23 , Issue.8 , pp. 2158-2167
    • Day, L.1    Xu, M.2    Lundin, L.3    Wooster, T.J.4
  • 9
    • 0003000024 scopus 로고
    • Modification of food proteins by enzymatic methods. In
    • Hudson, B.J.F.; Ed.; Elsevier Applied Science: London
    • Hamada, J.S. Modification of food proteins by enzymatic methods. In: Biochemistry of Food Proteins; Hudson, B.J.F.; Ed.; Elsevier Applied Science: London, 1992; 249-270.
    • (1992) Biochemistry of Food Proteins , pp. 249-270
    • Hamada, J.S.1
  • 10
    • 47849090249 scopus 로고    scopus 로고
    • Emulsifying and foaming properties of transglutaminasetreated wheat gluten hydrolysate as influenced by ph, temperature and salt
    • Agyare, K.K.; Addo, K.; Xiong, Y.L. Emulsifying and foaming properties of transglutaminasetreated wheat gluten hydrolysate as influenced by pH, temperature and salt. Food Hydrocolloids 2009, 23 (1), 72-78.
    • (2009) Food Hydrocolloids , vol.23 , Issue.1 , pp. 72-78
    • Agyare, K.K.1    Addo, K.2    Xiong, Y.L.3
  • 11
    • 0035083462 scopus 로고    scopus 로고
    • Comparison of deamidation activity of transglutaminases
    • Ohtsuka, T.; Umezawa, Y.; Nio, N.; Kubota, K. Comparison of deamidation activity of transglutaminases. Journal of Food Science 2006, 66 (1), 25-29.
    • (2006) Journal of Food Science , vol.66 , Issue.1 , pp. 25-29
    • Ohtsuka, T.1    Umezawa, Y.2    Nio, N.3    Kubota, K.4
  • 12
    • 0001568038 scopus 로고
    • Functional properties of deamidated gluten obtained by treating with chymotrypsin at alkali ph
    • Matsudomi, N.; Tanaka, A.; Kato, A.; Kobayashi, K. Functional properties of deamidated gluten obtained by treating with chymotrypsin at alkali pH. Agricultural and Biological Chemistry 1986, 50 (8), 1989-1994.
    • (1986) Agricultural and Biological Chemistry , vol.50 , Issue.8 , pp. 1989-1994
    • Matsudomi, N.1    Tanaka, A.2    Kato, A.3    Kobayashi, K.4
  • 13
    • 77950340810 scopus 로고    scopus 로고
    • Effect of deamidation by proteinglutaminase on physicochemical and functional properties of skim milk
    • Miwa, N.; Yokoyama, K.; Wakabayashi, H.; Nio, N. Effect of deamidation by proteinglutaminase on physicochemical and functional properties of skim milk. International Dairy Journal 2009, 20 (6), 393-399.
    • (2009) International Dairy Journal , vol.20 , Issue.6 , pp. 393-399
    • Miwa, N.1    Yokoyama, K.2    Wakabayashi, H.3    Nio, N.4
  • 15
    • 34247634582 scopus 로고    scopus 로고
    • Dynamic viscoelastic behavior of high pressure treated soybean protein isolate dispersions
    • Ahmed, J.; Ayad, A.; Ramaswamy, H.S.; Alli, I.; Shao, Y. Dynamic viscoelastic behavior of high pressure treated soybean protein isolate dispersions. International Journal of Food Properties 2007, 10 (2), 397-411.
    • (2007) International Journal of Food Properties , vol.10 , Issue.2 , pp. 397-411
    • Ahmed, J.1    Ayad, A.2    Ramaswamy, H.S.3    Alli, I.4    Shao, Y.5
  • 16
    • 0000586235 scopus 로고    scopus 로고
    • Biochemical characterization and enzymatic hydrolysis of different commercial soybean protein isolate
    • Henn, L.; Netto, M. Biochemical characterization and enzymatic hydrolysis of different commercial soybean protein isolate. Journal of Agricultural and Food Chemistry 1998, 46 (8), 3009-3015.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.8 , pp. 3009-3015
    • Henn, L.1    Netto, M.2
  • 17
    • 33646364376 scopus 로고    scopus 로고
    • Composition and functional properties of soy protein isolate prepared using alternative defatting and extraction procedures
    • L'hocine, L.; Boye, J.; Arcand, Y. Composition and functional properties of soy protein isolate prepared using alternative defatting and extraction procedures. Journal of Food Science 2006, 71 (3), 137-145.
    • (2006) Journal of Food Science , vol.71 , Issue.3 , pp. 137-145
    • L'hocine, L.1    Boye, J.2    Arcand, Y.3
  • 18
    • 0032116216 scopus 로고    scopus 로고
    • Hydrophobicity solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration
    • Wu, U.; Hettiarachchy, S.; Qi, M. Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration. Journal of the American Oil Chemists' Society 1998, 75 (7), 845-850.
    • (1998) Journal of the American Oil Chemists' Society , vol.75 , Issue.7 , pp. 845-850
    • Wu, U.1    Hettiarachchy, S.2    Qi, M.3
  • 19
    • 84755160828 scopus 로고    scopus 로고
    • Sodium bisulfite-induced changes in the physicochemical, surface and adhesive properties of soy ß-conglycinin
    • DOI: 10.1007/s11746-009-1528-7
    • Zhang, L.; Sun, X.Z.S. Sodium bisulfite-induced changes in the physicochemical, surface and adhesive properties of soy ß-conglycinin. Journal of the American Oil Chemists' Society 2010. DOI: 10.1007/s11746-009- 1528-7.
    • Journal of the American Oil Chemists' Society , vol.2010
    • Zhang, L.1    Sun, X.Z.S.2
  • 20
    • 14844310248 scopus 로고    scopus 로고
    • Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis
    • Jung, S.; Murphy, P.A.; Johnson, LA. Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis. Journal of Food Science 2005, 70 (2), C180-C187.
    • (2005) Journal of Food Science , vol.70 , Issue.2
    • Jung, S.1    Murphy, P.A.2    Johnson, L.A.3
  • 22
    • 46049101599 scopus 로고    scopus 로고
    • Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase and maillard cross-linking
    • Gan, C.Y.; Cheng, L.H.; Easa, A.M. Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase and Maillard cross-linking. Food Research International 2008, 41 (6), 600-605.
    • (2008) Food Research International , vol.41 , Issue.6 , pp. 600-605
    • Gan, C.Y.1    Cheng, L.H.2    Easa, A.M.3
  • 23
    • 62949222414 scopus 로고    scopus 로고
    • Functional properties of soy protein isolates prepared from gas-supported screw-pressed soybean meal
    • Nazareth, Z.M.; Deak, N.A.; Johnson, L.A. Functional properties of soy protein isolates prepared from gas-supported screw-pressed soybean meal. Journal of the American Oil Chemists' Society 2009, 86 (4), 315-321.
    • (2009) Journal of the American Oil Chemists' Society , vol.86 , Issue.4 , pp. 315-321
    • Nazareth, Z.M.1    Deak, N.A.2    Johnson, L.A.3
  • 24
    • 84907421510 scopus 로고
    • The relationship between the method of preparation and the structural and functional properties of soy protein isolates. Part i: Structural and hydration properties
    • Petruccelli, S.; Añón, M.C. The relationship between the method of preparation and the structural and functional properties of soy protein isolates. Part I: Structural and hydration properties. Journal of Agricultural and Food Chemistry 1994, 42 (10), 2161-2169.
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , Issue.10 , pp. 2161-2169
    • Petruccelli, S.1    Anón, M.C.2
  • 25
    • 84860425178 scopus 로고
    • IDF. Determination of the nitrogen (Kjeldahl method) and calculation of the crude protein content. Brussels, Belgium: International Dairy Federation IDF Standard 20B
    • IDF. Determination of the nitrogen (Kjeldahl method) and calculation of the crude protein content. Brussels, Belgium: International Dairy Federation IDF Standard 20B, 1993.
    • (1993)
  • 26
    • 33947332625 scopus 로고
    • Phenol-hypochlorite reaction for determination of ammonia
    • Weatherburn, M.W. Phenol-hypochlorite reaction for determination of ammonia. Analytical Chemistry 1967, 39 (8), 971-974.
    • (1967) Analytical Chemistry , vol.39 , Issue.8 , pp. 971-974
    • Weatherburn, M.W.1
  • 27
    • 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 (5259), 680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 7444247315 scopus 로고    scopus 로고
    • First report of a glutamine-rich antifungal peptide with immunomodulatory and antiproliferative activities from family amaryllidaceae
    • Chu, K.T.; Ng, T.B. First report of a glutamine-rich antifungal peptide with immunomodulatory and antiproliferative activities from family Amaryllidaceae. Biochemical and Biophysical Research Communications 2004, 325 (1), 169-173.
    • (2004) Biochemical and Biophysical Research Communications , vol.325 , Issue.1 , pp. 169-173
    • Chu, K.T.1    Ng, T.B.2
  • 30
    • 0015384891 scopus 로고
    • Determination of protein: A modification of the lowry method that gives a linear photometric response
    • Hartree, E.F. Determination of protein: A modification of the Lowry method that gives a linear photometric response. Analytical Biochemistry 1972, 48 (2), 422-427.
    • (1972) Analytical Biochemistry , vol.48 , Issue.2 , pp. 422-427
    • Hartree, E.F.1
  • 32
    • 26244468929 scopus 로고    scopus 로고
    • Fractionation and enzymatic hydrolysis of soluble protein present in waste liquors from soy processing
    • Moure, A.; Doḿlínguez, H.; Parajó, J.C. Fractionation and enzymatic hydrolysis of soluble protein present in waste liquors from soy processing. Journal of Agricultural and Food Chemistry 2005, 53 (19), 7600-7608.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.19 , pp. 7600-7608
    • Moure, A.1    Doḿlínguez, H.2    Parajó, J.C.3
  • 33
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce, K.N.; Kinsella, J.E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 1978, 26 (3), 716-723.
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , Issue.3 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 34
    • 67650995835 scopus 로고    scopus 로고
    • Effects of different oils on the properties of soy protein isolate emulsions and gels
    • Gu, X.; Campbell, L.J.; Euston, SR. Effects of different oils on the properties of soy protein isolate emulsions and gels. Food Research International 2009, 42 (8), 925-932.
    • (2009) Food Research International , vol.42 , Issue.8 , pp. 925-932
    • Gu, X.1    Campbell, L.J.2    Euston, S.R.3
  • 36
    • 8544266059 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of a-zein
    • Yong, Y.H.; Yamaguchi, S.; Gu, Y.S.; Mori, T.; Matsumura, Y. Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of a-zein. Journal of Agricultural and Food Chemistry 2004, 52 (23), 7094-7100.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.23 , pp. 7094-7100
    • Yong, Y.H.1    Yamaguchi, S.2    Gu, Y.S.3    Mori, T.4    Matsumura, Y.5
  • 37
    • 0002125249 scopus 로고
    • Molecular basis of protein functionality. In
    • Dickinson, E.; Ed.; Blackie Academic and Professional: Glasgow, London
    • Dickinson, E.; McClements, D.J. Molecular basis of protein functionality. In: Advances in Food Colloids; Dickinson, E.; Ed.; Blackie Academic and Professional: Glasgow, London, 1995; 27-80.
    • (1995) Advances in Food Colloids , pp. 27-80
    • Dickinson, E.1    McClements, D.J.2
  • 38
    • 58149498555 scopus 로고    scopus 로고
    • Effects of succinylation and deamidation on functional properties of oat protein isolate
    • Mirmoghtadaie, L.; Kadivar, M.; Shahedi, M. Effects of succinylation and deamidation on functional properties of oat protein isolate. Food Chemistry 2009, 114 (1), 127-131.
    • (2009) Food Chemistry , vol.114 , Issue.1 , pp. 127-131
    • Mirmoghtadaie, L.1    Kadivar, M.2    Shahedi, M.3
  • 39
    • 0036812821 scopus 로고    scopus 로고
    • Food protein functionality in a liquid system: A comparison of deamidated wheat protein with dairy and soy proteins
    • Webb, M.R.; Naeem, H.A.; Schmidt, K.A. Food protein functionality in a liquid system: A comparison of deamidated wheat protein with dairy and soy proteins. Journal of Food Science 2002, 67 (8), 2896-2902.
    • (2002) Journal of Food Science , vol.67 , Issue.8 , pp. 2896-2902
    • Webb, M.R.1    Naeem, H.A.2    Schmidt, K.A.3
  • 40
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides, and proteins. In
    • 3rd Ed.; Fenema, O.R.; Ed.; Marcel Dekker, Inc.: New York
    • Damodaran, S. Amino acids, peptides, and proteins. In: Food Chemistry, 3rd Ed.; Fenema, O.R.; Ed.; Marcel Dekker, Inc.: New York, 1996; 321-430.
    • (1996) Food Chemistry , pp. 321-430
    • Damodaran, S.1
  • 41
    • 0000018277 scopus 로고    scopus 로고
    • Minerals. In
    • 3rd Ed.; Fenema, O.R.; Ed.; Marcel Dekker, Inc.: New York
    • Miller, D.D. Minerals. In: Food Chemistry, 3rd Ed.; Fenema, O.R.; Ed.; Marcel Dekker, Inc.: New York, 1996; 617-649.
    • (1996) Food Chemistry , pp. 617-649
    • Miller, D.D.1
  • 43
    • 0035136024 scopus 로고    scopus 로고
    • Caseins and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition
    • Rival, S.G.; Boeriu, C.G.;Wichers, H.J. Caseins and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition. Journal of Agricultural and Food Chemistry 2001, 49 (1), 295-302.
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.1 , pp. 295-302
    • Rival, S.G.1    Boeriu, C.G.2    Wichers, H.J.3
  • 44
    • 0036006641 scopus 로고    scopus 로고
    • Preparation of phytateremoved, deamidated soybean globulins by ion exchangers and characterization of their calcium-binding ability
    • Kumagai, H.; Ishida, S.; Koizumi, A.; Sakurai, H.; Kumagai, H. Preparation of phytateremoved, deamidated soybean globulins by ion exchangers and characterization of their calcium-binding ability. Journal of Agricultural and Food Chemistry 2002, 50 (1), 172-176.
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.1 , pp. 172-176
    • Kumagai, H.1    Ishida, S.2    Koizumi, A.3    Sakurai, H.4    Kumagai, H.5
  • 45
    • 11244351680 scopus 로고    scopus 로고
    • Enhanced calcium absorption in the small intestine by a phytate-removed deamidated soybean globulin preparation
    • Kumagai, H.; Koizumi, A.; Suda, A.; Sato, N.; Sakurai, H.; Kumagai, H. Enhanced calcium absorption in the small intestine by a phytate-removed deamidated soybean globulin preparation. Bioscience Biotechnology and Biochemistry 2004, 68 (7), 1598-1600.
    • (2004) Bioscience Biotechnology and Biochemistry , vol.68 , Issue.7 , pp. 1598-1600
    • Kumagai, H.1    Koizumi, A.2    Suda, A.3    Sato, N.4    Sakurai, H.5    Kumagai, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.