메뉴 건너뛰기




Volumn 58, Issue 6, 2010, Pages 3580-3585

Model studies on chemical and textural modifications in gelatin films by reaction with glyoxal and glycolaldehyde

Author keywords

Biopolymer film; Chemical modification; Gelatin; Glycolaldehyde; Glyoxal; Glyoxal derlved lysine dlmer; N carboxymethyllysln; Young's modulus

Indexed keywords

ACETALDEHYDE; DRUG DERIVATIVE; GELATIN; GLYCOLALDEHYDE; GLYOXAL;

EID: 77949796947     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf9039827     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 0000407561 scopus 로고
    • The Maillard reaction in food and in the human body-New results in chemistry, biochemistry and medicine
    • Ledl, F.; Schleicher, E. The Maillard reaction in food and in the human body-New results in chemistry, biochemistry and medicine. Angew. Chem. 1990, 102, 597-626.
    • (1990) Angew. Chem. , vol.102 , pp. 597-626
    • Ledl, F.1    Schleicher, E.2
  • 2
    • 33646377677 scopus 로고    scopus 로고
    • Creating proteins with novel functionality via the Maillard reaction: A review
    • Oliver, C. M.; Melton, L. D.; Stanley, R. A. Creating proteins with novel functionality via the Maillard reaction: A review. Crit. Rev. Food Sci. 2006, 46, 337-350.
    • (2006) Crit. Rev. Food Sci. , vol.46 , pp. 337-350
    • Oliver, C.M.1    Melton, L.D.2    Stanley, R.A.3
  • 3
    • 0028934990 scopus 로고
    • Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction
    • Glomb, M. A.; Monnier, V. M. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction. J. Biol. Chem.. 1995, 270, 10017-10026.
    • (1995) J. Biol. Chem.. , vol.270 , pp. 10017-10026
    • Glomb, M.A.1    Monnier, V.M.2
  • 5
    • 0033492137 scopus 로고    scopus 로고
    • Cross-linking of proteins by maillard processes: Characterization and detection of lysine-arginine crosslinks derived from glyoxal and methylglyoxal
    • Lederer, M. O.; Klaiber, R. G. Cross-linking of proteins by maillard processes: Characterization and detection of lysine-arginine crosslinks derived from glyoxal and methylglyoxal. Bioore. Med. Chem. 1999, 7, 2499-2507.
    • (1999) Bioore. Med. Chem. , vol.7 , pp. 2499-2507
    • Lederer, M.O.1    Klaiber, R.G.2
  • 6
    • 0020770393 scopus 로고
    • Reaction of glycolaldehyde with proteins-Latent crosslinking potential of α-hydroxyaldehydes
    • Acharya, A. S.; Manning, J. M. Reaction of glycolaldehyde with proteins-Latent crosslinking potential of α-hydroxyaldehydes. Proe. Natl. Acad. Sci. U.S.A. 1983, 80, 3590-3594.
    • (1983) Proe. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 3590-3594
    • Acharya, A.S.1    Manning, J.M.2
  • 7
    • 0032968519 scopus 로고    scopus 로고
    • Studies on radical intermediates in the early stage of the nonenzymatic browning reaction of carbohydrates and amino acids
    • Hofmann, T.; Bors, W.; Stettmaier, K. Studies on radical intermediates in the early stage of the nonenzymatic browning reaction of carbohydrates and amino acids. J. Agric. Food Chem. 1999, 47, 379-390.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 379-390
    • Hofmann, T.1    Bors, W.2    Stettmaier, K.3
  • 8
    • 0034826534 scopus 로고    scopus 로고
    • Isolation and characterization of glyoxalarginine modifications
    • Glomb, M. A.; Lang, G. Isolation and characterization of glyoxalarginine modifications. J. Agric. Food Chem. 2001, 49,1493-1501.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1493-1501
    • Glomb, M.A.1    Lang, G.2
  • 9
    • 60249095273 scopus 로고    scopus 로고
    • Importance of size and charge of carbohydrate chains in the preparation of functional glycoproteins with excellent emulsifying properties from tofu whey
    • Matemu, A. O.; Kayahara, H.; Murasawa, H.; Nakamura, S. Importance of size and charge of carbohydrate chains in the preparation of functional glycoproteins with excellent emulsifying properties from tofu whey. Food Chem. 2009, 114, 1328-1334.
    • (2009) Food Chem. , vol.114 , pp. 1328-1334
    • Matemu, A.O.1    Kayahara, H.2    Murasawa, H.3    Nakamura, S.4
  • 10
    • 52949111347 scopus 로고    scopus 로고
    • The effect of glycation on foam and structural properties of a-lactoelobulin
    • Medrano, A.; Abirached, C.; Panizzolo, L.; Moyna, P.; Anon, M. C. The effect of glycation on foam and structural properties of a-lactoelobulin. Food Chem. 2009, 113, 127-133.
    • (2009) Food Chem. , vol.113 , pp. 127-133
    • Medrano, A.1    Abirached, C.2    Panizzolo, L.3    Moyna, P.4    Anon, M.C.5
  • 11
    • 63049126034 scopus 로고    scopus 로고
    • Preparation, characterisation and selected functional properties of sodium caseinate-maltodextrin conjugates
    • O'Regan, J.; Mulvihill, D. M. Preparation, characterisation and selected functional properties of sodium caseinate-maltodextrin conjugates. Food Chem. 2009, 115, 1257-1267.
    • (2009) Food Chem. , vol.115 , pp. 1257-1267
    • O'Regan, J.1    Mulvihill, D.M.2
  • 12
    • 0033789735 scopus 로고    scopus 로고
    • Effects of sugars on whey protein isolate gelation
    • Rich, L. M.; Foegeding, E. A. Effects of sugars on whey protein isolate gelation. J. Agric. Food. Chem. 2000, 48, 5046-5052.
    • (2000) J. Agric. Food. Chem. , vol.48 , pp. 5046-5052
    • Rich, L.M.1    Foegeding, E.A.2
  • 13
    • 47349126199 scopus 로고    scopus 로고
    • Influence of a rare sugar, D-psicose, on the physicochemical and functional properties of an aerated food system containing egg albumen
    • Sun, Y.; Hayakawa, S.; Ogawa, M.; Fukada, K.; Izumori, K. Influence of a rare sugar, D-psicose, on the physicochemical and functional properties of an aerated food system containing egg albumen. J. Agric, Food Chem. 2008, 56, 4789-4796.
    • (2008) J. Agric, Food Chem. , vol.56 , pp. 4789-4796
    • Sun, Y.1    Hayakawa, S.2    Ogawa, M.3    Fukada, K.4    Izumori, K.5
  • 14
    • 42249114051 scopus 로고    scopus 로고
    • 1st ed.; Wiley-VHC Verlag GmbH and Co. KG: Weinheim, Germany
    • Schrieber, R.; Gareis, H. Gelatine Handbook, 1st ed.; Wiley-VHC Verlag GmbH and Co. KG: Weinheim, Germany, 2007.
    • (2007) Gelatine Handbook
    • Schrieber, R.1    Gareis, H.2
  • 15
    • 0029250912 scopus 로고
    • Determination of the renaturation level in gelatin films
    • Achet, D.; He, X. W. Determination of the renaturation level in gelatin films. Polymer 1995, 36, 787-791.
    • (1995) Polymer , vol.36 , pp. 787-791
    • Achet, D.1    He, X.W.2
  • 16
    • 2542482901 scopus 로고    scopus 로고
    • Relationship between triple-helix content and mechanical properties of gelatin films
    • Bigi, A.; Panzavolta, S.; Rubini, K. Relationship between triple-helix content and mechanical properties of gelatin films. Biomaterials 2004, 25, 5675-5680.
    • (2004) Biomaterials , vol.25 , pp. 5675-5680
    • Bigi, A.1    Panzavolta, S.2    Rubini, K.3
  • 17
    • 33646156622 scopus 로고    scopus 로고
    • The effect of crystallinity and aging enthalpy on the mechanical properties of gelatin films
    • Dai, C. A.; Liu, M. W. The effect of crystallinity and aging enthalpy on the mechanical properties of gelatin films. Mater. Sci. Eng., A 2006, 423, 121-127.
    • (2006) Mater. Sci. Eng., A , vol.423 , pp. 121-127
    • Dai, C.A.1    Liu, M.W.2
  • 18
    • 67349143415 scopus 로고    scopus 로고
    • Characterization of gelatin films prepared from, under-utilized blue shark (Prionace glauca) skin
    • Limpisophon, K.; Tanaka, M.; Weng, W. Y.; Abe, S.; Osako, K. Characterization of gelatin films prepared from, under-utilized blue shark (Prionace glauca) skin. Food Hydrocolloids 2009, 23, 1993-2000.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1993-2000
    • Limpisophon, K.1    Tanaka, M.2    Weng, W.Y.3    Abe, S.4    Osako, K.5
  • 19
    • 0035122037 scopus 로고    scopus 로고
    • Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking
    • Bigi, A.; Cojazzi, G.; Panzavolta, S.; Rubini, K.; Roveri, N. Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking. Biomaterials 2001, 22, 763768.
    • (2001) Biomaterials , vol.22 , pp. 763768
    • Bigi, A.1    Cojazzi, G.2    Panzavolta, S.3    Rubini, K.4    Roveri, N.5
  • 20
    • 0036888749 scopus 로고    scopus 로고
    • Stabilization of gelatin films by crosslinking with genipin
    • Bigi, A.; Cojazzi, G.; Panzavolta, S.; Roveri, N.; Rubini, K. Stabilization of gelatin films by crosslinking with genipin. Biomaterials 2002, 23, 4827-4832.
    • (2002) Biomaterials , vol.23 , pp. 4827-4832
    • Bigi, A.1    Cojazzi, G.2    Panzavolta, S.3    Roveri, N.4    Rubini, K.5
  • 21
    • 0030130294 scopus 로고    scopus 로고
    • Evaluation of different chemical methods for crosslinking collagen gel, films and sponges
    • Rault, I.; Frei, V.; Herbage, D.; Abdul-Malak, N.; Hue, A. Evaluation of different chemical methods for crosslinking collagen gel, films and sponges. J. Mater. Sci.; Mater, Med. 1996, 7, 215-221.
    • (1996) J. Mater. Sci.; Mater, Med. , vol.7 , pp. 215-221
    • Rault, I.1    Frei, V.2    Herbage, D.3    Abdul-Malak, N.4    Hue, A.5
  • 22
    • 0035834748 scopus 로고    scopus 로고
    • Amides are novel protein modifications formed by physiological sugars
    • Glomb, M. A.; Pfahler, C. Amides are novel protein modifications formed by physiological sugars. J. Biol. Chem. 2001, 276, 41638-41647.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41638-41647
    • Glomb, M.A.1    Pfahler, C.2
  • 23
    • 0035188656 scopus 로고    scopus 로고
    • Detection of α-dicarbonyl compounds in Maillard reaction systems and in vivo
    • Glomb, M. A.; Tschirnich, R. Detection of α-dicarbonyl compounds in Maillard reaction systems and in vivo. J. Agric. Food Chem. 2001, 49, 5543-5550.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 5543-5550
    • Glomb, M.A.1    Tschirnich, R.2
  • 24
    • 34047248365 scopus 로고    scopus 로고
    • Preparation and physical properties of soy protein isolate and gelatin composite films
    • Cao, N.; Fu, Y. H.; He, J. H. Preparation and physical properties of soy protein isolate and gelatin composite films. Food Hydroeolloids 2007, 21, 1153-1162.
    • (2007) Food Hydroeolloids , vol.21 , pp. 1153-1162
    • Cao, N.1    Fu, Y.H.2    He, J.H.3
  • 25
    • 0033006573 scopus 로고    scopus 로고
    • Radical-assisted melanoidin formation during thermal processing of foods as well as under physiological conditions
    • Hofmann, T.; Bors, W.; Stettmaier, K. Radical-assisted melanoidin formation during thermal processing of foods as well as under physiological conditions. J. Agric. Food Chem. 1999, 47, 391-396.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 391-396
    • Hofmann, T.1    Bors, W.2    Stettmaier, K.3
  • 27
    • 42549164542 scopus 로고    scopus 로고
    • Model studies on protein glycation: Influence of cysteine on the reactivity of arginine and lysine residues toward glyoxal
    • Schwarzenbolz, U.; Mende, S.; Henle, T. Model studies on protein glycation: influence of cysteine on the reactivity of arginine and lysine residues toward glyoxal. Ann. N. Y. Acad. Sci. 2008, 1126, 248-252.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1126 , pp. 248-252
    • Schwarzenbolz, U.1    Mende, S.2    Henle, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.