메뉴 건너뛰기




Volumn 8, Issue 2, 2007, Pages 269-278

Comparative study of gelation and cross-link formation during enzymatic texturisation of leguminous proteins

Author keywords

Cross linking; HPLC MS; o Phthaldialdehyde derivatisation; Texture analysis; Texturised vegetable protein; Transglutaminase

Indexed keywords

CHEMICAL BONDS; CROSSLINKING; ENZYME KINETICS; GELATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETERS;

EID: 34147113294     PISSN: 14668564     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ifset.2007.01.005     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 0242516975 scopus 로고
    • Functional roles of heat induced protein gelation in processed meat
    • Kinsella J.E., and Soucie W.G. (Eds), AOCS, Champaign, IL
    • Acton J.C., and Dick R.L. Functional roles of heat induced protein gelation in processed meat. In: Kinsella J.E., and Soucie W.G. (Eds). Food proteins (1989), AOCS, Champaign, IL 195-209
    • (1989) Food proteins , pp. 195-209
    • Acton, J.C.1    Dick, R.L.2
  • 6
    • 85052700473 scopus 로고    scopus 로고
    • Thermal denaturation and coagulation of proteins
    • Damodaran S., and Paraf A. (Eds), Marcel Dekker, New York
    • Boye J.I., Ma C.-Y., and Harwalkar V.R. Thermal denaturation and coagulation of proteins. In: Damodaran S., and Paraf A. (Eds). Food proteins and their applications (1997), Marcel Dekker, New York 25-56
    • (1997) Food proteins and their applications , pp. 25-56
    • Boye, J.I.1    Ma, C.-Y.2    Harwalkar, V.R.3
  • 8
    • 1542708368 scopus 로고    scopus 로고
    • Recent advances in enzymatic modifications of food proteins for improving their functional properties
    • Chobert J.M., Briand L., Guéguen J., Popineau Y., Larré C., and Haertlé T. Recent advances in enzymatic modifications of food proteins for improving their functional properties. Nahrung 40 4 (1996) 177-182
    • (1996) Nahrung , vol.40 , Issue.4 , pp. 177-182
    • Chobert, J.M.1    Briand, L.2    Guéguen, J.3    Popineau, Y.4    Larré, C.5    Haertlé, T.6
  • 10
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: Impact on food applications
    • De Jong G.A.H., and Koppelman S.J. Transglutaminase catalyzed reactions: Impact on food applications. Journal of Food Science 67 8 (2002) 2798-2806
    • (2002) Journal of Food Science , vol.67 , Issue.8 , pp. 2798-2806
    • De Jong, G.A.H.1    Koppelman, S.J.2
  • 11
    • 0031259385 scopus 로고    scopus 로고
    • Enzymic crosslinking as a tool for colloid rheology control and interfacial stabilization
    • Dickinson E. Enzymic crosslinking as a tool for colloid rheology control and interfacial stabilization. Trends in Food Science and Technology 8 (1997) 334-339
    • (1997) Trends in Food Science and Technology , vol.8 , pp. 334-339
    • Dickinson, E.1
  • 12
    • 0036348648 scopus 로고    scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for the determination of transglutaminase activity on casein
    • Dinnella C., Gargaro M.T., Rossano R., and Monteleone E. Spectrophotometric assay using o-phthaldialdehyde for the determination of transglutaminase activity on casein. Food Chemistry 78 3 (2002) 363-368
    • (2002) Food Chemistry , vol.78 , Issue.3 , pp. 363-368
    • Dinnella, C.1    Gargaro, M.T.2    Rossano, R.3    Monteleone, E.4
  • 13
    • 34147132669 scopus 로고    scopus 로고
    • Dube, M., Schäfer, C., Neidhart, S., & Carle, R. (2006). Texturisation and modification of vegetable proteins for food applications using microbial transglutaminase. European Food Research and Technology, published online 30.06.2006 [http://www.springerlink.com/(mmc45345h4strg55jjmhih45)/app/home/issue.asp].
  • 14
    • 0242720522 scopus 로고    scopus 로고
    • Characterisation and quantification of the reaction(s) catalysed by transglutaminase using the o-phthaldialdehyde reagent
    • Flanagan J., and FitzGerald R.J. Characterisation and quantification of the reaction(s) catalysed by transglutaminase using the o-phthaldialdehyde reagent. Nahrung/Food 47 3 (2003) 207-212
    • (2003) Nahrung/Food , vol.47 , Issue.3 , pp. 207-212
    • Flanagan, J.1    FitzGerald, R.J.2
  • 15
    • 0033281905 scopus 로고    scopus 로고
    • Lysinoalanine in food and in antimicrobial proteins
    • Impact of processing on food safety. Jackson L.S., Knize M.G., and Morgan J.N. (Eds), Kluwer Academic/Plenum Publishers, New York, NY
    • Friedman M. Lysinoalanine in food and in antimicrobial proteins. In: Jackson L.S., Knize M.G., and Morgan J.N. (Eds). Impact of processing on food safety. Advances in Experimental Medicine and Biology Series Vol. 459 (1999), Kluwer Academic/Plenum Publishers, New York, NY 145-159
    • (1999) Advances in Experimental Medicine and Biology Series , vol.459 , pp. 145-159
    • Friedman, M.1
  • 16
    • 0023944341 scopus 로고
    • OPA method modified by use of N,N-dimethyl-2-mercaptoethylammonium chloride as thiol component
    • Frister H., Meisel H., and Schlimme E. OPA method modified by use of N,N-dimethyl-2-mercaptoethylammonium chloride as thiol component. Fresenius' Journal of Analytical Chemistry 330 (1988) 631-633
    • (1988) Fresenius' Journal of Analytical Chemistry , vol.330 , pp. 631-633
    • Frister, H.1    Meisel, H.2    Schlimme, E.3
  • 19
    • 0017175313 scopus 로고
    • Mechanisms of heat damage in proteins. 7. The significance of lysine-containing isopeptides and of lanthionine in heated proteins
    • Hurrell R.F., Carpenter K.J., Sinclair W.J., Otterburn M.S., and Asquith R.S. Mechanisms of heat damage in proteins. 7. The significance of lysine-containing isopeptides and of lanthionine in heated proteins. British Journal of Nutrition 35 3 (1976) 383-395
    • (1976) British Journal of Nutrition , vol.35 , Issue.3 , pp. 383-395
    • Hurrell, R.F.1    Carpenter, K.J.2    Sinclair, W.J.3    Otterburn, M.S.4    Asquith, R.S.5
  • 21
    • 1542787221 scopus 로고    scopus 로고
    • The usefulness of transglutaminase for food processing
    • Biotechnology for improved foods and flavors. Takeoka G.R. (Ed), American Chemical Society, Washington, DC
    • Kuraishi C., Sakamoto J., and Soeda T. The usefulness of transglutaminase for food processing. In: Takeoka G.R. (Ed). Biotechnology for improved foods and flavors. ACS Symposium Series Vol. 637 (1996), American Chemical Society, Washington, DC 29-38
    • (1996) ACS Symposium Series , vol.637 , pp. 29-38
    • Kuraishi, C.1    Sakamoto, J.2    Soeda, T.3
  • 22
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: its utilization in the food industry
    • Kuraishi C., Yamazaki K., and Susa Y. Transglutaminase: its utilization in the food industry. Food Reviews International 17 2 (2001) 221-246
    • (2001) Food Reviews International , vol.17 , Issue.2 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 25
    • 0042736339 scopus 로고    scopus 로고
    • On the influence of non-enzymatic crosslinking of caseins on the gel strength of yoghurt
    • Lauber S., Klostermeyer H., and Henle T. On the influence of non-enzymatic crosslinking of caseins on the gel strength of yoghurt. Nahrung/Food 45 3 (2001) 215-217
    • (2001) Nahrung/Food , vol.45 , Issue.3 , pp. 215-217
    • Lauber, S.1    Klostermeyer, H.2    Henle, T.3
  • 26
    • 34147173689 scopus 로고
    • Thermal aggregation and gelation of oat globulin
    • Visser H. (Ed), VCH Verlagsgesellschaft, Weinheim, Germany
    • Ma C.-Y., and Harwalkar V.R. Thermal aggregation and gelation of oat globulin. In: Visser H. (Ed). Protein interactions (1992), VCH Verlagsgesellschaft, Weinheim, Germany 269-292
    • (1992) Protein interactions , pp. 269-292
    • Ma, C.-Y.1    Harwalkar, V.R.2
  • 29
    • 0000633489 scopus 로고    scopus 로고
    • Recent research trends in transglutaminase technology for food processing
    • Motoki M., and Kumazawa Y. Recent research trends in transglutaminase technology for food processing. Food Science and Technology Research 6 3 (2000) 151-160
    • (2000) Food Science and Technology Research , vol.6 , Issue.3 , pp. 151-160
    • Motoki, M.1    Kumazawa, Y.2
  • 30
    • 0031690193 scopus 로고    scopus 로고
    • Transglutaminase and its use for food processing
    • Motoki M., and Seguro K. Transglutaminase and its use for food processing. Trends in Food Science and Technology 9 5 (1998) 204-210
    • (1998) Trends in Food Science and Technology , vol.9 , Issue.5 , pp. 204-210
    • Motoki, M.1    Seguro, K.2
  • 31
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • Nielsen P.M., Petersen D., and Dambmann C. Improved method for determining food protein degree of hydrolysis. Journal of Food Science 66 5 (2001) 642-646
    • (2001) Journal of Food Science , vol.66 , Issue.5 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambmann, C.3
  • 33
    • 0001245817 scopus 로고
    • Isopeptides: The occurrence and significance of natural and xenobiotic crosslinks in proteins
    • Otterburn M.S. Isopeptides: The occurrence and significance of natural and xenobiotic crosslinks in proteins. ACS Symposium Series Xenobiotic Foods Feeds 234 (1983) 221-232
    • (1983) ACS Symposium Series Xenobiotic Foods Feeds , vol.234 , pp. 221-232
    • Otterburn, M.S.1
  • 35
    • 0344444635 scopus 로고    scopus 로고
    • Relations between rheological properties and network structure of soy protein gels
    • Renkema J.M.S. Relations between rheological properties and network structure of soy protein gels. Food Hydrocolloids 18 1 (2004) 39-47
    • (2004) Food Hydrocolloids , vol.18 , Issue.1 , pp. 39-47
    • Renkema, J.M.S.1
  • 36
    • 27444447737 scopus 로고    scopus 로고
    • Enhancement of transglutaminase-induced protein cross-linking by preheat treatment of cows' milk: A statistical approach
    • Rodriguez-Nogales J.M. Enhancement of transglutaminase-induced protein cross-linking by preheat treatment of cows' milk: A statistical approach. International Dairy Journal 16 (2006) 26-32
    • (2006) International Dairy Journal , vol.16 , pp. 26-32
    • Rodriguez-Nogales, J.M.1
  • 37
    • 0028139777 scopus 로고
    • Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions
    • Sakamoto H., Kumazawa Y., and Motoki M. Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. Journal of Food Science 59 4 (1994) 866-871
    • (1994) Journal of Food Science , vol.59 , Issue.4 , pp. 866-871
    • Sakamoto, H.1    Kumazawa, Y.2    Motoki, M.3
  • 38
    • 84986467761 scopus 로고
    • ε-(γ-Glutamyl) lysine crosslink distribution in foods as determined by improved method
    • Sakamoto H., Kumazawa Y., Kawajiri H., and Motoki M. ε-(γ-Glutamyl) lysine crosslink distribution in foods as determined by improved method. Journal of Food Science 60 2 (1995) 416-419
    • (1995) Journal of Food Science , vol.60 , Issue.2 , pp. 416-419
    • Sakamoto, H.1    Kumazawa, Y.2    Kawajiri, H.3    Motoki, M.4
  • 39
    • 0000281272 scopus 로고
    • Improved method for identification and determination of ε-(γ-glutamyl) lysine cross-link in protein using proteolytic digestion and derivatisation with phenyl isothiocyanate followed by high-performance liquid chromatography separation
    • Sato K., Tsukamasa Y., Imai C., Ohtsuki K., Shimizu Y., and Kawabata M. Improved method for identification and determination of ε-(γ-glutamyl) lysine cross-link in protein using proteolytic digestion and derivatisation with phenyl isothiocyanate followed by high-performance liquid chromatography separation. Journal of Agricultural and Food Chemistry 40 (1992) 806-810
    • (1992) Journal of Agricultural and Food Chemistry , vol.40 , pp. 806-810
    • Sato, K.1    Tsukamasa, Y.2    Imai, C.3    Ohtsuki, K.4    Shimizu, Y.5    Kawabata, M.6
  • 40
    • 17144368764 scopus 로고    scopus 로고
    • Identification and quantification of ε-(γ-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS)
    • Schäfer C., Schott M., Brandl F., Neidhart S., and Carle R. Identification and quantification of ε-(γ-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS). Journal of Agricultural and Food Chemistry 53 (2005) 2830-2837
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 2830-2837
    • Schäfer, C.1    Schott, M.2    Brandl, F.3    Neidhart, S.4    Carle, R.5
  • 41
    • 0041865238 scopus 로고
    • Heat and alkaline damage to proteins: Racemization and lysinoalanine formation
    • Schwass D.E., and Finley J.W. Heat and alkaline damage to proteins: Racemization and lysinoalanine formation. Journal of Agricultural and Food Chemistry 32 (1984) 1377-1382
    • (1984) Journal of Agricultural and Food Chemistry , vol.32 , pp. 1377-1382
    • Schwass, D.E.1    Finley, J.W.2
  • 42
    • 0041524989 scopus 로고    scopus 로고
    • Legume protein structure and interaction. Reflections about the functional potential of legume proteins - a review
    • Schwenke K.D. Legume protein structure and interaction. Reflections about the functional potential of legume proteins - a review. Nahrung/Food 45 6 (2001) 377-381
    • (2001) Nahrung/Food , vol.45 , Issue.6 , pp. 377-381
    • Schwenke, K.D.1
  • 43
    • 0342488842 scopus 로고    scopus 로고
    • Proteins
    • Sikorski Z.E. (Ed), Technomic Publishing Company, Lancaster, PA, USA
    • Sikorski Z.E. Proteins. In: Sikorski Z.E. (Ed). Chemical and functional properties of food components (1997), Technomic Publishing Company, Lancaster, PA, USA 119-160
    • (1997) Chemical and functional properties of food components , pp. 119-160
    • Sikorski, Z.E.1
  • 44
    • 34147155186 scopus 로고
    • Conformation of globular proteins from pea investigated by infrared spectroscopy
    • Schwenke K.D., and Mothes R. (Eds), VCH Verlagsgesellschaft, Weinheim, Germany
    • Subirade M., Pezolet M., and Gueguen J. Conformation of globular proteins from pea investigated by infrared spectroscopy. In: Schwenke K.D., and Mothes R. (Eds). Food proteins, structure and functionality (1993), VCH Verlagsgesellschaft, Weinheim, Germany 158-162
    • (1993) Food proteins, structure and functionality , pp. 158-162
    • Subirade, M.1    Pezolet, M.2    Gueguen, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.