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Volumn 72, Issue , 2018, Pages 134-143

Crosslinking of food proteins mediated by oxidative enzymes – A review

Author keywords

Laccase; Peroxidase; Protein crosslinking; Texture; Tyrosinase

Indexed keywords

ENZYMES; GELS; TEXTURES;

EID: 85039927416     PISSN: 09242244     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tifs.2017.12.011     Document Type: Review
Times cited : (115)

References (74)
  • 1
    • 84949236007 scopus 로고    scopus 로고
    • Stabilization of biopolymer microgels formed by electrostatic complexation: Influence of enzyme (laccase) cross-linking on pH, thermal, and mechanical stability
    • Azarikia, F., Wu, B.-c., Abbasi, S., McClements, D.J., Stabilization of biopolymer microgels formed by electrostatic complexation: Influence of enzyme (laccase) cross-linking on pH, thermal, and mechanical stability. Food Research International 78 (2015), 18–26.
    • (2015) Food Research International , vol.78 , pp. 18-26
    • Azarikia, F.1    Wu, B.-C.2    Abbasi, S.3    McClements, D.J.4
  • 2
    • 85019613693 scopus 로고    scopus 로고
    • Review: Nutrient density and nutritional value of meat products and non-meat foods high in protein
    • Bohrer, B.M., Review: Nutrient density and nutritional value of meat products and non-meat foods high in protein. Trends in Food Science & Technology 65 (2017), 103–112.
    • (2017) Trends in Food Science & Technology , vol.65 , pp. 103-112
    • Bohrer, B.M.1
  • 5
    • 84883010738 scopus 로고    scopus 로고
    • Milk processing as a tool to reduce cow's milk allergenicity: A mini-review
    • Bu, G., Luo, Y., Chen, F., Liu, K., Zhu, T., Milk processing as a tool to reduce cow's milk allergenicity: A mini-review. Dairy Science & Technology 93 (2013), 211–223.
    • (2013) Dairy Science & Technology , vol.93 , pp. 211-223
    • Bu, G.1    Luo, Y.2    Chen, F.3    Liu, K.4    Zhu, T.5
  • 6
    • 84903197398 scopus 로고    scopus 로고
    • Quality attributes of the set-style yoghurt from whole bovine milk as affected by an enzymatic oxidative cross-linking
    • Chang, C.-H., Kong, B.-H., Zhao, X.-H., Quality attributes of the set-style yoghurt from whole bovine milk as affected by an enzymatic oxidative cross-linking. CyTA - Journal of Food 12 (2014), 249–255.
    • (2014) CyTA - Journal of Food , vol.12 , pp. 249-255
    • Chang, C.-H.1    Kong, B.-H.2    Zhao, X.-H.3
  • 7
    • 85008199794 scopus 로고    scopus 로고
    • Covalent conjugation of bovine serum album and sugar beet pectin through Maillard reaction/laccase catalysis to improve the emulsifying properties
    • Chen, H., Ji, A., Qiu, S., Liu, Y., Zhu, Q., Yin, L., Covalent conjugation of bovine serum album and sugar beet pectin through Maillard reaction/laccase catalysis to improve the emulsifying properties. Food Hydrocolloids 76 (2018), 173–183.
    • (2018) Food Hydrocolloids , vol.76 , pp. 173-183
    • Chen, H.1    Ji, A.2    Qiu, S.3    Liu, Y.4    Zhu, Q.5    Yin, L.6
  • 8
    • 84862831549 scopus 로고    scopus 로고
    • Formation and microstructural characterization of whey protein isolate/beet pectin coacervations by laccase catalyzed cross-linking
    • Chen, B., Li, H., Ding, Y., Suo, H., Formation and microstructural characterization of whey protein isolate/beet pectin coacervations by laccase catalyzed cross-linking. Lebensmittel-Wissenschaft und -Technologie- Food Science and Technology 47 (2012), 31–38.
    • (2012) Lebensmittel-Wissenschaft und -Technologie- Food Science and Technology , vol.47 , pp. 31-38
    • Chen, B.1    Li, H.2    Ding, Y.3    Suo, H.4
  • 10
    • 84884714189 scopus 로고    scopus 로고
    • Controlled formation of protein nanoparticles by enzymatic cross-linking of α-lactalbumin with horseradish peroxidase
    • Dhayal, S.K., Gruppen, H., de Vries, R., Wierenga, P.A., Controlled formation of protein nanoparticles by enzymatic cross-linking of α-lactalbumin with horseradish peroxidase. Food Hydrocolloids 36 (2014), 53–59.
    • (2014) Food Hydrocolloids , vol.36 , pp. 53-59
    • Dhayal, S.K.1    Gruppen, H.2    de Vries, R.3    Wierenga, P.A.4
  • 12
    • 83455171950 scopus 로고    scopus 로고
    • Enzymatic cross-linking of β-lactoglobulin in solution and at air–water interface: Structural constraints
    • Ercili-Cura, D., Partanen, R., Husband, F., Ridout, M., Macierzanka, A., Lille, M., et al. Enzymatic cross-linking of β-lactoglobulin in solution and at air–water interface: Structural constraints. Food Hydrocolloids 28 (2012), 1–9.
    • (2012) Food Hydrocolloids , vol.28 , pp. 1-9
    • Ercili-Cura, D.1    Partanen, R.2    Husband, F.3    Ridout, M.4    Macierzanka, A.5    Lille, M.6
  • 13
    • 78649451634 scopus 로고    scopus 로고
    • Cross-linking and immobilisation of different proteins with recombinant Verrucomicrobium spinosum tyrosinase
    • Fairhead, M., Thöny-Meyer, L., Cross-linking and immobilisation of different proteins with recombinant Verrucomicrobium spinosum tyrosinase. Journal of Biotechnology 150 (2010), 546–551.
    • (2010) Journal of Biotechnology , vol.150 , pp. 546-551
    • Fairhead, M.1    Thöny-Meyer, L.2
  • 14
    • 84855812531 scopus 로고    scopus 로고
    • Bacterial tyrosinases: Old enzymes with new relevance to biotechnology
    • Fairhead, M., Thöny-Meyer, L., Bacterial tyrosinases: Old enzymes with new relevance to biotechnology. New Biotech 29 (2012), 183–191.
    • (2012) New Biotech , vol.29 , pp. 183-191
    • Fairhead, M.1    Thöny-Meyer, L.2
  • 16
    • 79961159849 scopus 로고    scopus 로고
    • Effects of tyrosinase and laccase on oat proteins and quality parameters of gluten-free oat breads
    • Flander, L., Holopainen, U., Kruus, K., Buchert, J., Effects of tyrosinase and laccase on oat proteins and quality parameters of gluten-free oat breads. Journal of Agricultural and Food Chemistry 59 (2011), 8385–8390.
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , pp. 8385-8390
    • Flander, L.1    Holopainen, U.2    Kruus, K.3    Buchert, J.4
  • 17
    • 84881226821 scopus 로고    scopus 로고
    • Crystal structures of copper-depleted and copper-bound fungal pro-tyrosinase: Insights into endogenous cysteine-dependent copper incorporation
    • Fujieda, N., Yabuta, S., Ikeda, T., Oyama, T., Muraki, N., Kurisu, G., et al. Crystal structures of copper-depleted and copper-bound fungal pro-tyrosinase: Insights into endogenous cysteine-dependent copper incorporation. Journal of Biological Chemistry 288 (2013), 22128–22140.
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 22128-22140
    • Fujieda, N.1    Yabuta, S.2    Ikeda, T.3    Oyama, T.4    Muraki, N.5    Kurisu, G.6
  • 18
    • 0036980061 scopus 로고    scopus 로고
    • Protein–protein crosslinking in food: Methods, consequences, applications
    • Gerrard, J.A., Protein–protein crosslinking in food: Methods, consequences, applications. Trends in Food Science & Technology 13 (2002), 391–399.
    • (2002) Trends in Food Science & Technology , vol.13 , pp. 391-399
    • Gerrard, J.A.1
  • 19
    • 33646347450 scopus 로고    scopus 로고
    • Protein cross-linking in food: Mechanisms, consequences, applications
    • Gerrard, J.A., Brown, P.K., Protein cross-linking in food: Mechanisms, consequences, applications. International Congress Series 1245 (2002), 211–215.
    • (2002) International Congress Series , vol.1245 , pp. 211-215
    • Gerrard, J.A.1    Brown, P.K.2
  • 22
    • 84905233254 scopus 로고    scopus 로고
    • Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins
    • Goldfeder, M., Kanteev, M., Isaschar-Ovdat, S., Adir, N., Fishman, A., Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins. Nature Communications, 5, 2014, 4505.
    • (2014) Nature Communications , vol.5 , pp. 4505
    • Goldfeder, M.1    Kanteev, M.2    Isaschar-Ovdat, S.3    Adir, N.4    Fishman, A.5
  • 23
    • 84961198136 scopus 로고    scopus 로고
    • Properties of bovine gelatin cross-linked by a mixture of two oxidases (horseradish peroxidase and glucose oxidase) and glucose
    • Han, Y.-P., Zhao, X.-H., Properties of bovine gelatin cross-linked by a mixture of two oxidases (horseradish peroxidase and glucose oxidase) and glucose. CyTA - Journal of Food 14 (2016), 457–464.
    • (2016) CyTA - Journal of Food , vol.14 , pp. 457-464
    • Han, Y.-P.1    Zhao, X.-H.2
  • 27
    • 85039936494 scopus 로고    scopus 로고
    • Chapter 1-Protein-rich by-products: Production statistics, legislative restrictions, and management options in Protein Byproducts
    • 1st ed. Academic Press
    • Hicks, T.M., Verbeek, C.J.R., Chapter 1-Protein-rich by-products: Production statistics, legislative restrictions, and management options in Protein Byproducts. 1st ed., 2016, Academic Press.
    • (2016)
    • Hicks, T.M.1    Verbeek, C.J.R.2
  • 30
    • 85017557080 scopus 로고    scopus 로고
    • Mechanistic insights into tyrosinase-mediated crosslinking of soy glycinin derived peptides
    • Isaschar-Ovdat, S., Fishman, A., Mechanistic insights into tyrosinase-mediated crosslinking of soy glycinin derived peptides. Food Chemistry 232 (2017), 587–594.
    • (2017) Food Chemistry , vol.232 , pp. 587-594
    • Isaschar-Ovdat, S.1    Fishman, A.2
  • 31
    • 84908461537 scopus 로고    scopus 로고
    • Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin
    • Isaschar-Ovdat, S., Rosenberg, M., Lesmes, U., Fishman, A., Characterization of oil-in-water emulsions stabilized by tyrosinase-crosslinked soy glycinin. Food Hydrocolloids 43 (2015), 493–500.
    • (2015) Food Hydrocolloids , vol.43 , pp. 493-500
    • Isaschar-Ovdat, S.1    Rosenberg, M.2    Lesmes, U.3    Fishman, A.4
  • 32
    • 79959257956 scopus 로고    scopus 로고
    • Crystal structure of Agaricus bisporus mushroom tyrosinase: Identity of the tetramer subunits and interaction with tropolone
    • Ismaya, W.T., Rozeboom, H.J., Weijn, A., Mes, J.J., Fusetti, F., Wichers, H.J., et al. Crystal structure of Agaricus bisporus mushroom tyrosinase: Identity of the tetramer subunits and interaction with tropolone. Biochemistry 50 (2011), 5477–5486.
    • (2011) Biochemistry , vol.50 , pp. 5477-5486
    • Ismaya, W.T.1    Rozeboom, H.J.2    Weijn, A.3    Mes, J.J.4    Fusetti, F.5    Wichers, H.J.6
  • 37
    • 84950121186 scopus 로고    scopus 로고
    • Structure–function correlations in tyrosinases
    • Kanteev, M., Goldfeder, M., Fishman, A., Structure–function correlations in tyrosinases. Protein Science 24 (2015), 1360–1369.
    • (2015) Protein Science , vol.24 , pp. 1360-1369
    • Kanteev, M.1    Goldfeder, M.2    Fishman, A.3
  • 38
    • 79551478887 scopus 로고    scopus 로고
    • Potential applications of laccase-mediated coupling and grafting reactions: A review
    • Kudanga, T., Nyanhongo, G.S., Guebitz, G.M., Burton, S., Potential applications of laccase-mediated coupling and grafting reactions: A review. Enzyme and Microbial Technology 48 (2011), 195–208.
    • (2011) Enzyme and Microbial Technology , vol.48 , pp. 195-208
    • Kudanga, T.1    Nyanhongo, G.S.2    Guebitz, G.M.3    Burton, S.4
  • 39
    • 84887341130 scopus 로고    scopus 로고
    • The 2013 FAO report on dietary protein quality evaluation in human nutrition: Recommendations and implications
    • Leser, S., The 2013 FAO report on dietary protein quality evaluation in human nutrition: Recommendations and implications. Nutrition Bulletin 38 (2013), 421–428.
    • (2013) Nutrition Bulletin , vol.38 , pp. 421-428
    • Leser, S.1
  • 40
    • 84913533810 scopus 로고    scopus 로고
    • Peroxidase-mediated conjugation of corn fiber gum and bovine serum albumin to improve emulsifying properties
    • Liu, Y., Qiu, S., Li, J., Chen, H., Tatsumi, E., Yadav, M., et al. Peroxidase-mediated conjugation of corn fiber gum and bovine serum albumin to improve emulsifying properties. Carbohydrate Polymers 118 (2015), 70–78.
    • (2015) Carbohydrate Polymers , vol.118 , pp. 70-78
    • Liu, Y.1    Qiu, S.2    Li, J.3    Chen, H.4    Tatsumi, E.5    Yadav, M.6
  • 41
    • 79951737545 scopus 로고    scopus 로고
    • Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers
    • Ma, H., Forssell, P., Partanen, R., Buchert, J., Boer, H., Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers. Journal of Agricultural and Food Chemistry 59 (2011), 1406–1414.
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , pp. 1406-1414
    • Ma, H.1    Forssell, P.2    Partanen, R.3    Buchert, J.4    Boer, H.5
  • 42
    • 84961878117 scopus 로고    scopus 로고
    • Structure modification of stirred fermented milk gel due to laccase-catalysed protein crosslinking in a post-processing step
    • Mokoonlall, A., Pfannstiel, J., Struch, M., Berger, R.G., Hinrichs, J., Structure modification of stirred fermented milk gel due to laccase-catalysed protein crosslinking in a post-processing step. Innovative Food Science & Emerging Technologies 33 (2016), 563–570.
    • (2016) Innovative Food Science & Emerging Technologies , vol.33 , pp. 563-570
    • Mokoonlall, A.1    Pfannstiel, J.2    Struch, M.3    Berger, R.G.4    Hinrichs, J.5
  • 43
    • 84961727423 scopus 로고    scopus 로고
    • A feasibility study on the application of a laccase-mediator system in stirred yoghurt at the pilot scale
    • Mokoonlall, A., Sykora, L., Pfannstiel, J., Nöbel, S., Weiss, J., Hinrichs, J., A feasibility study on the application of a laccase-mediator system in stirred yoghurt at the pilot scale. Food Hydrocolloids 60 (2016), 119–127.
    • (2016) Food Hydrocolloids , vol.60 , pp. 119-127
    • Mokoonlall, A.1    Sykora, L.2    Pfannstiel, J.3    Nöbel, S.4    Weiss, J.5    Hinrichs, J.6
  • 44
    • 84931091565 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of latent, active and recombinantly expressed aurone synthase, a polyphenol oxidase, from Coreopsis grandiflora
    • Molitor, C., Mauracher, S.G., Rompel, A., Crystallization and preliminary crystallographic analysis of latent, active and recombinantly expressed aurone synthase, a polyphenol oxidase, from Coreopsis grandiflora. Acta Crystallographica Section F 71 (2015), 746–751.
    • (2015) Acta Crystallographica Section F , vol.71 , pp. 746-751
    • Molitor, C.1    Mauracher, S.G.2    Rompel, A.3
  • 46
    • 79959908730 scopus 로고    scopus 로고
    • Loosening of globular structure under alkaline pH affects accessibility of β-lactoglobulin to tyrosinase-induced oxidation and subsequent cross-linking
    • Partanen, R., Torkkeli, M., Hellman, M., Permi, P., Serimaa, R., Buchert, J., et al. Loosening of globular structure under alkaline pH affects accessibility of β-lactoglobulin to tyrosinase-induced oxidation and subsequent cross-linking. Enzyme and Microbial Technology 49 (2011), 131–138.
    • (2011) Enzyme and Microbial Technology , vol.49 , pp. 131-138
    • Partanen, R.1    Torkkeli, M.2    Hellman, M.3    Permi, P.4    Serimaa, R.5    Buchert, J.6
  • 49
    • 84876709843 scopus 로고    scopus 로고
    • Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking
    • Salvachúa, D., Prieto, A., Mattinen, M.-L., Tamminen, T., Liitiä, T., Lille, M., et al. Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking. Enzyme and Microbial Technology 52 (2013), 303–311.
    • (2013) Enzyme and Microbial Technology , vol.52 , pp. 303-311
    • Salvachúa, D.1    Prieto, A.2    Mattinen, M.-L.3    Tamminen, T.4    Liitiä, T.5    Lille, M.6
  • 50
    • 84877132980 scopus 로고    scopus 로고
    • Nanostructure development during peroxidase catalysed cross-linking of α-lactalbumin
    • Saricay, Y., Wierenga, P., de Vries, R., Nanostructure development during peroxidase catalysed cross-linking of α-lactalbumin. Food Hydrocolloids 33 (2013), 280–288.
    • (2013) Food Hydrocolloids , vol.33 , pp. 280-288
    • Saricay, Y.1    Wierenga, P.2    de Vries, R.3
  • 51
    • 84924390285 scopus 로고    scopus 로고
    • Changes in protein conformation and surface hydrophobicity upon peroxidase-catalyzed cross-linking of apo-α-lactalbumin
    • Saricay, Y., Wierenga, P.A., de Vries, R., Changes in protein conformation and surface hydrophobicity upon peroxidase-catalyzed cross-linking of apo-α-lactalbumin. Journal of Agricultural and Food Chemistry 62 (2014), 9345–9352.
    • (2014) Journal of Agricultural and Food Chemistry , vol.62 , pp. 9345-9352
    • Saricay, Y.1    Wierenga, P.A.2    de Vries, R.3
  • 52
    • 84931268629 scopus 로고    scopus 로고
    • Cross-linking proteins by laccase: Effects on the droplet size and rheology of emulsions stabilized by sodium caseinate
    • Sato, A.C.K., Perrechil, F.A., Costa, A.A.S., Santana, R.C., Cunha, R.L., Cross-linking proteins by laccase: Effects on the droplet size and rheology of emulsions stabilized by sodium caseinate. Food Research International 75 (2015), 244–251.
    • (2015) Food Research International , vol.75 , pp. 244-251
    • Sato, A.C.K.1    Perrechil, F.A.2    Costa, A.A.S.3    Santana, R.C.4    Cunha, R.L.5
  • 55
    • 84961241056 scopus 로고    scopus 로고
    • Recent trends in fungal laccase for various industrial applications: An eco-friendly approach - a review
    • Senthivelan, T., Kanagaraj, J., Panda, R.C., Recent trends in fungal laccase for various industrial applications: An eco-friendly approach - a review. Biotechnology and Bioprocess Engineering 21 (2016), 19–38.
    • (2016) Biotechnology and Bioprocess Engineering , vol.21 , pp. 19-38
    • Senthivelan, T.1    Kanagaraj, J.2    Panda, R.C.3
  • 57
    • 84903848519 scopus 로고    scopus 로고
    • Cross-linking of β-lactoglobulin enhances allergic sensitization through changes in cellular uptake and processing
    • Stojadinovic, M., Pieters, R., Smit, J., Velickovic, T.C., Cross-linking of β-lactoglobulin enhances allergic sensitization through changes in cellular uptake and processing. Toxicological Sciences 140 (2014), 224–235.
    • (2014) Toxicological Sciences , vol.140 , pp. 224-235
    • Stojadinovic, M.1    Pieters, R.2    Smit, J.3    Velickovic, T.C.4
  • 59
    • 84930959264 scopus 로고    scopus 로고
    • Laccase-catalysed cross-linking of a yoghurt-like model system made from skimmed milk with added food-grade mediators
    • Struch, M., Linke, D., Mokoonlall, A., Hinrichs, J., Berger, R.G., Laccase-catalysed cross-linking of a yoghurt-like model system made from skimmed milk with added food-grade mediators. International Dairy Journal 49 (2015), 89–94.
    • (2015) International Dairy Journal , vol.49 , pp. 89-94
    • Struch, M.1    Linke, D.2    Mokoonlall, A.3    Hinrichs, J.4    Berger, R.G.5
  • 61
    • 77957857745 scopus 로고    scopus 로고
    • Digestibility and allergenicity of β-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics
    • Tantoush, Z., Stanic, D., Stojadinovic, M., Ognjenovic, J., Mihajlovic, L., Atanaskovic-Markovic, M., et al. Digestibility and allergenicity of β-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. Food Chemistry 125 (2011), 84–91.
    • (2011) Food Chemistry , vol.125 , pp. 84-91
    • Tantoush, Z.1    Stanic, D.2    Stojadinovic, M.3    Ognjenovic, J.4    Mihajlovic, L.5    Atanaskovic-Markovic, M.6
  • 63
    • 85012953903 scopus 로고    scopus 로고
    • Bioprospecting and biotechnological applications of fungal laccase
    • Upadhyay, P., Shrivastava, R., Agrawal, P.K., Bioprospecting and biotechnological applications of fungal laccase. 3 Biotech, 6, 2016, 15.
    • (2016) 3 Biotech , vol.6 , pp. 15
    • Upadhyay, P.1    Shrivastava, R.2    Agrawal, P.K.3
  • 64
    • 84949908349 scopus 로고    scopus 로고
    • Combined effect of squid ink tyrosinase and tannic acid on heat induced aggregation of natural actomyosin from sardine
    • Vate, N.K., Benjakul, S., Combined effect of squid ink tyrosinase and tannic acid on heat induced aggregation of natural actomyosin from sardine. Food Hydrocolloids 56 (2016), 62–70.
    • (2016) Food Hydrocolloids , vol.56 , pp. 62-70
    • Vate, N.K.1    Benjakul, S.2
  • 65
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: A modern view of a classic enzyme
    • Veitch, N.C., Horseradish peroxidase: A modern view of a classic enzyme. Phytochemistry 65 (2004), 249–259.
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Veitch, N.C.1
  • 68
    • 84973596890 scopus 로고    scopus 로고
    • Crosslinking of peanut allergen Ara h 2 by polyphenol oxidase: Digestibility and potential allergenicity assessment
    • Wu, Z., Lian, J., Han, Y., Zhou, N., Li, X., Yang, A., et al. Crosslinking of peanut allergen Ara h 2 by polyphenol oxidase: Digestibility and potential allergenicity assessment. Journal of the Science of Food and Agriculture 96 (2016), 3567–3574.
    • (2016) Journal of the Science of Food and Agriculture , vol.96 , pp. 3567-3574
    • Wu, Z.1    Lian, J.2    Han, Y.3    Zhou, N.4    Li, X.5    Yang, A.6
  • 69
    • 84962898729 scopus 로고    scopus 로고
    • Development of tyrosinase-aided crosslinking procedure for stabilizing protein nanoparticles
    • Xu, R., Teng, Z., Wang, Q., Development of tyrosinase-aided crosslinking procedure for stabilizing protein nanoparticles. Food Hydrocolloids 60 (2016), 324–334.
    • (2016) Food Hydrocolloids , vol.60 , pp. 324-334
    • Xu, R.1    Teng, Z.2    Wang, Q.3
  • 70
    • 80053502326 scopus 로고    scopus 로고
    • Cross-linking of interfacial layers affects the salt and temperature stability of multilayered emulsions consisting of fish gelatin and sugar beet pectin
    • Zeeb, B., Fischer, L., Weiss, J., Cross-linking of interfacial layers affects the salt and temperature stability of multilayered emulsions consisting of fish gelatin and sugar beet pectin. Journal of Agricultural and Food Chemistry 59 (2011), 10546–10555.
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , pp. 10546-10555
    • Zeeb, B.1    Fischer, L.2    Weiss, J.3
  • 71
    • 80053554913 scopus 로고    scopus 로고
    • Crosslinking of interfacial layers in multilayered oil-in-water emulsions using laccase: Characterization and pH-stability
    • Zeeb, B., Gibis, M., Fischer, L., Weiss, J., Crosslinking of interfacial layers in multilayered oil-in-water emulsions using laccase: Characterization and pH-stability. Food Hydrocolloids 27 (2012), 126–136.
    • (2012) Food Hydrocolloids , vol.27 , pp. 126-136
    • Zeeb, B.1    Gibis, M.2    Fischer, L.3    Weiss, J.4
  • 73
    • 84901048243 scopus 로고    scopus 로고
    • Impact of heat and laccase on the pH and freeze-thaw stability of oil-in-water emulsions stabilized by adsorbed biopolymer nanoparticles
    • Zeeb, B., Salminen, H., Fischer, L., Weiss, J., Impact of heat and laccase on the pH and freeze-thaw stability of oil-in-water emulsions stabilized by adsorbed biopolymer nanoparticles. Food Biophysics 9 (2014), 125–137.
    • (2014) Food Biophysics , vol.9 , pp. 125-137
    • Zeeb, B.1    Salminen, H.2    Fischer, L.3    Weiss, J.4
  • 74
    • 84973642076 scopus 로고    scopus 로고
    • Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity
    • Zhang, Y.-H., Wang, H., Liu, Y.-L., Zhao, X.-H., Two horseradish peroxidase-based modifications result in two milk protein products with ordered secondary structure and enhanced in vitro antigenicity. CyTA - Journal of Food 14 (2016), 572–577.
    • (2016) CyTA - Journal of Food , vol.14 , pp. 572-577
    • Zhang, Y.-H.1    Wang, H.2    Liu, Y.-L.3    Zhao, X.-H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.