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Volumn 14, Issue 3, 2016, Pages 457-464

Properties of bovine gelatin cross-linked by a mixture of two oxidases (horseradish peroxidase and glucose oxidase) and glucose;Propiedades de la gelatina bovina con enlaces cruzados mediante una mezcla compuesta de dos oxidasas (peroxidasa de rábano picante y glucosa oxidasa) y glucosa

Author keywords

Bovine gelatin; cross linking; functional property; glucose oxidase; horseradish peroxidase; secondary structure

Indexed keywords

DICHROISM; FOOD PRODUCTS; GELATION; GLUCOSE; GLUCOSE SENSORS; MAMMALS; MIXTURES; STABILIZATION;

EID: 84961198136     PISSN: 19476337     EISSN: 19476345     Source Type: Journal    
DOI: 10.1080/19476337.2015.1134671     Document Type: Article
Times cited : (16)

References (41)
  • 2
    • 0003895440 scopus 로고    scopus 로고
    • 4th Revised and Extended, Berlin, Germany: Springer Verlag
    • H.D.Belitz,, W.Grosch,, & P.Schieberle, (2009). Food Chemistry (4th Revised and Extended ed.). Berlin, Germany: Springer Verlag.
    • (2009) Food Chemistry
    • Belitz, H.D.1    Grosch, W.2    Schieberle, P.3
  • 3
    • 25144436480 scopus 로고    scopus 로고
    • Gelatin hydrogels cross-linked by γ-ray irradiation: Materials for absorption and release of dye
    • M.Bessho,, M.Furuta,, T.Kojima,, S.Okuda,, & M.Hara, (2005). Gelatin hydrogels cross-linked by γ-ray irradiation: Materials for absorption and release of dye. Journal of Biomaterials Science Polymer Edition, 16, 715–724. doi:10.1163/1568562053992478
    • (2005) Journal of Biomaterials Science Polymer Edition , vol.16 , pp. 715-724
    • Bessho, M.1    Furuta, M.2    Kojima, T.3    Okuda, S.4    Hara, M.5
  • 4
    • 56149125912 scopus 로고    scopus 로고
    • Ultraviolet irradiation improves gel strength of fish gelatin
    • R.Bhat,, & A.A.Karim, (2009). Ultraviolet irradiation improves gel strength of fish gelatin. Food Chemistry, 113, 1160–1164. doi:10.1016/j.foodchem.2008.08.039
    • (2009) Food Chemistry , vol.113 , pp. 1160-1164
    • Bhat, R.1    Karim, A.A.2
  • 5
    • 0036888749 scopus 로고    scopus 로고
    • Stabilization of gelatin films by crosslinking with genipin
    • A.Bigi,, G.Cojazzi,, S.Panzavolta,, N.Roveria,, & K.Rubini, (2002). Stabilization of gelatin films by crosslinking with genipin. Biomaterials, 23, 4827–4832. doi:10.1016/S0142-9612(02)00235-1
    • (2002) Biomaterials , vol.23 , pp. 4827-4832
    • Bigi, A.1    Cojazzi, G.2    Panzavolta, S.3    Roveria, N.4    Rubini, K.5
  • 6
    • 0035122037 scopus 로고    scopus 로고
    • Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking
    • A.Bigi,, G.Cojazzi,, S.Panzavolta,, K.Rubini,, & N.Roveri, (2001). Mechanical and thermal properties of gelatin films at different degrees of glutaraldehyde crosslinking. Biomaterials, 22, 763–768. doi:10.1016/S0142-9612(00)00236-2
    • (2001) Biomaterials , vol.22 , pp. 763-768
    • Bigi, A.1    Cojazzi, G.2    Panzavolta, S.3    Rubini, K.4    Roveri, N.5
  • 7
    • 72049102340 scopus 로고    scopus 로고
    • Chemico-physical characterization of gelatin films modified with oxidized alginate
    • E.Boanini,, K.Rubini,, S.Panzavolta,, & A.Bigi, (2010). Chemico-physical characterization of gelatin films modified with oxidized alginate. Acta Biomaterialia, 6, 383–388. doi:10.1016/j.actbio.2009.06.015
    • (2010) Acta Biomaterialia , vol.6 , pp. 383-388
    • Boanini, E.1    Rubini, K.2    Panzavolta, S.3    Bigi, A.4
  • 8
    • 33846292554 scopus 로고    scopus 로고
    • Mechanical properties of gelatin films cross-linked, respectively, by ferulic acid and tannin acid
    • N.Cao,, Y.Fu,, & J.He, (2007). Mechanical properties of gelatin films cross-linked, respectively, by ferulic acid and tannin acid. Food Hydrocolloids, 21, 575–584. doi:10.1016/j.foodhyd.2006.07.001
    • (2007) Food Hydrocolloids , vol.21 , pp. 575-584
    • Cao, N.1    Fu, Y.2    He, J.3
  • 9
    • 84866297305 scopus 로고    scopus 로고
    • In vitro digestibility and rheological properties of caseinates treated by an oxidative system containing horseradish peroxidase, glucose oxidase and glucose
    • C.-H.Chang,, & X.-H.Zhao, (2012). In vitro digestibility and rheological properties of caseinates treated by an oxidative system containing horseradish peroxidase, glucose oxidase and glucose. International Dairy Journal, 27, 47–52. doi:10.1016/j.idairyj.2012.07.004
    • (2012) International Dairy Journal , vol.27 , pp. 47-52
    • Chang, C.-H.1    Zhao, X.-H.2
  • 10
    • 0036838127 scopus 로고    scopus 로고
    • Gelation properties of soya and whey protein isolate mixtures
    • S.Comfort,, & N.K.Howell, (2002). Gelation properties of soya and whey protein isolate mixtures. Food Hydrocolloids, 16, 661–672. doi:10.1016/S0268-005X(02)00033-4
    • (2002) Food Hydrocolloids , vol.16 , pp. 661-672
    • Comfort, S.1    Howell, N.K.2
  • 11
    • 84861429878 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate
    • S.Damodaran,, & K.K.Agyare, (2013). Effect of microbial transglutaminase treatment on thermal stability and pH-solubility of heat-shocked whey protein isolate. Food Hydrocolloids, 30, 12–18. doi:10.1016/j.foodhyd.2012.04.012
    • (2013) Food Hydrocolloids , vol.30 , pp. 12-18
    • Damodaran, S.1    Agyare, K.K.2
  • 12
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radical. II. Modification of amino acids
    • K.J.Davies,, M.E.Delsignore,, & S.W.Lin, (1987). Protein damage and degradation by oxygen radical. II. Modification of amino acids. Journal of Biological Chemistry, 262, 9902–9907.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 9902-9907
    • Davies, K.J.1    Delsignore, M.E.2    Lin, S.W.3
  • 13
    • 3042541063 scopus 로고    scopus 로고
    • Characterization of gelatin based films modified with transglutaminase, glyoxal and formaldehyde
    • R.A.De Carvalho,, & C.R.F.Grosso, (2004). Characterization of gelatin based films modified with transglutaminase, glyoxal and formaldehyde. Food Hydrocolloids, 18, 717–726. doi:10.1016/j.foodhyd.2003.10.005
    • (2004) Food Hydrocolloids , vol.18 , pp. 717-726
    • De Carvalho, R.A.1    Grosso, C.R.F.2
  • 15
    • 0033797890 scopus 로고    scopus 로고
    • Rheological characterisation of gelatins from mammalian and marine sources
    • P.M.Gilsenan,, & S.B.Ross-Murphy, (2000). Rheological characterisation of gelatins from mammalian and marine sources. Food Hydrocolloids, 14, 191–195. doi:10.1016/S0268-005X(99)00050-8
    • (2000) Food Hydrocolloids , vol.14 , pp. 191-195
    • Gilsenan, P.M.1    Ross-Murphy, S.B.2
  • 16
    • 0342502122 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on the functional properties of megrim (Lepidorhombus boscii) skin gelatin
    • M.C.Gómez-Guillén,, A.I.Sarabia,, M.T.Solas,, & P.Montero, (2001). Effect of microbial transglutaminase on the functional properties of megrim (Lepidorhombus boscii) skin gelatin. Journal of the Science of Food & Agriculture, 81, 665–673. doi:10.1002/jsfa.865
    • (2001) Journal of the Science of Food & Agriculture , vol.81 , pp. 665-673
    • Gómez-Guillén, M.C.1    Sarabia, A.I.2    Solas, M.T.3    Montero, P.4
  • 17
    • 0036132846 scopus 로고    scopus 로고
    • Structural and physical properties of gelatin extracted from different marine species: A comparative study
    • M.C.Gómez-Guillén,, J.Turnay,, M.D.Fernández-Díaz,, N.Ulmo,, M.A.Lizarbe,, & P.Montero, (2002). Structural and physical properties of gelatin extracted from different marine species: A comparative study. Food Hydrocolloids, 16, 25–34. doi:10.1016/S0268-005X(01)00035-2
    • (2002) Food Hydrocolloids , vol.16 , pp. 25-34
    • Gómez-Guillén, M.C.1    Turnay, J.2    Fernández-Díaz, M.D.3    Ulmo, N.4    Lizarbe, M.A.5    Montero, P.6
  • 19
    • 84904489295 scopus 로고    scopus 로고
    • Gelation and in vitro Digestibility of Soybean Protein Isolate Treated by a Ternary System Containing Horseradish Peroxidase, Glucose Oxidase, and Glucose
    • P.Jiang,, & X.-H.Zhao, (2014). Gelation and in vitro Digestibility of Soybean Protein Isolate Treated by a Ternary System Containing Horseradish Peroxidase, Glucose Oxidase, and Glucose. International Journal of Food Properties, 17, 2284–2297. doi:10.1080/10942912.2013.798737
    • (2014) International Journal of Food Properties , vol.17 , pp. 2284-2297
    • Jiang, P.1    Zhao, X.-H.2
  • 20
    • 33748192961 scopus 로고    scopus 로고
    • Skin gelatin from bigeye snapper and brownstripe red snapper: Chemical compositions and effect of microbial transglutaminase on gel properties
    • A.Jongjareonrak,, S.Benjakul,, W.Visessanguan,, & M.Tanaka, (2006). Skin gelatin from bigeye snapper and brownstripe red snapper: Chemical compositions and effect of microbial transglutaminase on gel properties. Food Hydrocolloids, 20, 1216–1222. doi:10.1016/j.foodhyd.2006.01.006
    • (2006) Food Hydrocolloids , vol.20 , pp. 1216-1222
    • Jongjareonrak, A.1    Benjakul, S.2    Visessanguan, W.3    Tanaka, M.4
  • 21
    • 84900825685 scopus 로고    scopus 로고
    • The interaction of polymer-coated magnetic nanoparticles with seawater
    • E.Kadar,, Í.L.Batalha,, A.Fisher,, & A.C.A.Roque, (2014). The interaction of polymer-coated magnetic nanoparticles with seawater. Science of the Total Environment, 487, 771–777. doi:10.1016/j.scitotenv.2013.11.082
    • (2014) Science of the Total Environment , vol.487 , pp. 771-777
    • Kadar, E.1    Batalha, Í.L.2    Fisher, A.3    Roque, A.C.A.4
  • 22
    • 84873719462 scopus 로고    scopus 로고
    • Molecular and functional properties of gelatin from the skin of unicorn leatherjacket as affected by extracting temperatures
    • P.Kaewruang,, S.Benjakul,, & T.Prodpran, (2013). Molecular and functional properties of gelatin from the skin of unicorn leatherjacket as affected by extracting temperatures. Food Chemistry, 138, 1431–1437. doi:10.1016/j.foodchem.2012.09.114
    • (2013) Food Chemistry , vol.138 , pp. 1431-1437
    • Kaewruang, P.1    Benjakul, S.2    Prodpran, T.3
  • 23
    • 54049111758 scopus 로고    scopus 로고
    • Fish gelatin: Properties, challenges, and prospects as an alternative to mammalian gelatins
    • A.A.Karim,, & R.Bhat, (2009). Fish gelatin: Properties, challenges, and prospects as an alternative to mammalian gelatins. Food Hydrocolloids, 23, 563–576. doi:10.1016/j.foodhyd.2008.07.002
    • (2009) Food Hydrocolloids , vol.23 , pp. 563-576
    • Karim, A.A.1    Bhat, R.2
  • 25
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: Its utilization in the food industry
    • C.Kuraishi,, K.Yamazaki,, & Y.Susa, (2001). Transglutaminase: Its utilization in the food industry. Food Reviews International, 17, 221–246. doi:10.1081/FRI-100001258
    • (2001) Food Reviews International , vol.17 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K.Laemmli, (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685. doi:10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 84894615140 scopus 로고    scopus 로고
    • The effect of pH and heat pre-treatments on the physicochemical and emulsifying properties of β-lactoglobulin
    • R.S.H.Lam,, & M.T.Nickerson, (2014). The effect of pH and heat pre-treatments on the physicochemical and emulsifying properties of β-lactoglobulin. Food Biophysics, 9, 20–28. doi:10.1007/s11483-013-9313-4
    • (2014) Food Biophysics , vol.9 , pp. 20-28
    • Lam, R.S.H.1    Nickerson, M.T.2
  • 28
    • 84942890467 scopus 로고    scopus 로고
    • Caseinate-gelatin and caseinate-hydrolyzed gelatin composites formed via transglutaminase: Chemical and functional properties
    • Z.L.Luo,, & X.H.Zhao, (2014). Caseinate-gelatin and caseinate-hydrolyzed gelatin composites formed via transglutaminase: Chemical and functional properties. Journal of the Science of Food & Agriculture. doi:10.1002/jsfa.7042
    • (2014) Journal of the Science of Food & Agriculture
    • Luo, Z.L.1    Zhao, X.H.2
  • 30
    • 0342578231 scopus 로고
    • The use of the Coulter Counter for investigating the coagulation kinetics of mixed monodisperse particulate systems
    • B.A.Matthews,, & C.T.Rhodes, (1968). The use of the Coulter Counter for investigating the coagulation kinetics of mixed monodisperse particulate systems. Journal of Colloid & Interface Science, 28, 71–81. doi:10.1016/0021-9797(68)90209-9
    • (1968) Journal of Colloid & Interface Science , vol.28 , pp. 71-81
    • Matthews, B.A.1    Rhodes, C.T.2
  • 31
    • 84872370187 scopus 로고    scopus 로고
    • Optimization of gelatine gel preparation from New Zealand hoki (Macruronus novaezelandiae) skins and the effect of transglutaminase enzyme on the gel properties
    • N.F.Mohtar,, C.O.Perera,, S.-Y.Quek,, & Y.Hemar, (2013). Optimization of gelatine gel preparation from New Zealand hoki (Macruronus novaezelandiae) skins and the effect of transglutaminase enzyme on the gel properties. Food Hydrocolloids, 31, 204–209. doi:10.1016/j.foodhyd.2012.10.011
    • (2013) Food Hydrocolloids , vol.31 , pp. 204-209
    • Mohtar, N.F.1    Perera, C.O.2    Quek, S.-Y.3    Hemar, Y.4
  • 32
    • 2142849929 scopus 로고    scopus 로고
    • Extraction and physico-chemical characterisation of Nile perch (Lates niloticus) skin and bone gelatine
    • J.H.Muyonga,, C.G.B.Cole,, & K.G.Duodu, (2004). Extraction and physico-chemical characterisation of Nile perch (Lates niloticus) skin and bone gelatine. Food Hydrocolloids, 18, 581–592. doi:10.1016/j.foodhyd.2003.08.009
    • (2004) Food Hydrocolloids , vol.18 , pp. 581-592
    • Muyonga, J.H.1    Cole, C.G.B.2    Duodu, K.G.3
  • 33
    • 0035891178 scopus 로고    scopus 로고
    • Influence of the molecular-weight distribution of gelatin on emulsion stability
    • J.Olijve,, F.Mori,, & Y.Toda, (2001). Influence of the molecular-weight distribution of gelatin on emulsion stability. Journal of Colloid & Interface Science, 243, 476–482. doi:10.1006/jcis.2001.7816
    • (2001) Journal of Colloid & Interface Science , vol.243 , pp. 476-482
    • Olijve, J.1    Mori, F.2    Toda, Y.3
  • 36
    • 0035187664 scopus 로고    scopus 로고
    • Mechanical, water vapor barrier and thermal properties of gelatin based edible films
    • P.J.A.Sobral,, F.C.Menegalli,, M.D.Hubinger,, & M.A.Roques, (2001). Mechanical, water vapor barrier and thermal properties of gelatin based edible films. Food Hydrocolloids, 15, 423–432. doi:10.1016/S0268-005X(01)00061-3
    • (2001) Food Hydrocolloids , vol.15 , pp. 423-432
    • Sobral, P.J.A.1    Menegalli, F.C.2    Hubinger, M.D.3    Roques, M.A.4
  • 37
    • 0017403490 scopus 로고
    • Cross linking of proteins in vitro by peroxidase
    • M.A.Stahmann,, A.K.Spencer,, & G.R.Honold, (1977). Cross linking of proteins in vitro by peroxidase. Biopolymers, 16, 1307–1318. doi:10.1002/(ISSN)1097-0282
    • (1977) Biopolymers , vol.16 , pp. 1307-1318
    • Stahmann, M.A.1    Spencer, A.K.2    Honold, G.R.3
  • 38
    • 20644440389 scopus 로고    scopus 로고
    • Glucose Oxidase Effects on Gluten and Water Solubles 1
    • V.Vemulapalli,, & R.C.Hoseney, (1998). Glucose Oxidase Effects on Gluten and Water Solubles 1. Cereal Chemistry, 75, 859–862. doi:10.1094/CCHEM.1998.75.6.859
    • (1998) Cereal Chemistry , vol.75 , pp. 859-862
    • Vemulapalli, V.1    Hoseney, R.C.2
  • 39
    • 0033992170 scopus 로고    scopus 로고
    • Desolvation process and surface characterisation of protein nanoparticles
    • C.Weber,, C.Coester,, J.Kreuter,, & K.Langer, (2000). Desolvation process and surface characterisation of protein nanoparticles. International Journal of Pharmaceutics, 194, 91–102. doi:10.1016/S0378-5173(99)00370-1
    • (2000) International Journal of Pharmaceutics , vol.194 , pp. 91-102
    • Weber, C.1    Coester, C.2    Kreuter, J.3    Langer, K.4
  • 40
    • 33847285539 scopus 로고    scopus 로고
    • Interaction between proteins and cationic gemini surfactant
    • D.Wu,, G.Xu,, Y.Sun,, H.Zhang,, H.Mao,, & Y.Feng, (2007). Interaction between proteins and cationic gemini surfactant. Biomacromolecules, 8, 708–712. doi:10.1021/bm061033v
    • (2007) Biomacromolecules , vol.8 , pp. 708-712
    • Wu, D.1    Xu, G.2    Sun, Y.3    Zhang, H.4    Mao, H.5    Feng, Y.6
  • 41
    • 68849119830 scopus 로고    scopus 로고
    • Synthesis of gelatin-stabilized gold nanoparticles and assembly of carboxylic single-walled carbon nanotubes/Au composites for cytosensing and drug uptake
    • J.-J.Zhang,, M.-M.Gu,, T.-T.Zheng,, & J.-J.Zhu, (2009). Synthesis of gelatin-stabilized gold nanoparticles and assembly of carboxylic single-walled carbon nanotubes/Au composites for cytosensing and drug uptake. Analytical Chemistry, 81, 6641–6648. doi:10.1021/ac900628y
    • (2009) Analytical Chemistry , vol.81 , pp. 6641-6648
    • Zhang, J.-J.1    Gu, M.-M.2    Zheng, T.-T.3    Zhu, J.-J.4


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