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Free and cationic inulin-coated nanoliposomal forms of BET\u002FCAR were incorporated into the gluten films at 0, 5, and 10% (w\u002Fw) gluten concentrations. Fourier-transform infrared spectroscopy was used to detect the formation of new hydrogen bonds between gluten, CHNF, and nanoliposomes (NLPs). Differential scanning calorimetry analysis revealed that the addition of free BET\u002FCAR reduced the endothermic transition temperature of films as compared to the unfortified film; however, the addition of NLPs had no effect on the thermal profile. Similar changes were observed in the crystallinity of films as determined by X-ray powder diffraction analysis. FE-SEM results showed that the incorporation of CHNF and BET\u002FCAR NLPs did not alter the morphology of films but the free BET\u002FCAR induced aggregates formation on the films' surface. CHNF addition enhanced the mechanical, water barrier, and wettability of films. Among the films tested, those containing BET\u002FCAR NLPs had the highest antioxidant potential. However, the encapsulated BET\u002FCAR in inulin-coated NLPs had an improved antimicrobial activity. The films containing the nanoliposomal form of BET\u002FCAR indicated a controlled release behavior.",{"EN":130,"VI":131},"Gluten\u002Fchitosan Nanofiber-based Films Activated by Cationic Inulin-coated Betanin and Carvone Co-loaded Nanoliposomes: Preparation and Characterization","Màng trên cơ sở sợi nano gluten\u002Fchitosan được hoạt hóa bằng các nanoliposome đồng nạp betanin và carvone phủ inulin cation: Điều chế và đặc trưng hoá",{"VOID":133},"S. Sharma, S. Barkauskaite, B. Du, A.K. Jaiswal, S. Jaiswal, Foods 9, 1117 (2020)\nM. Soofi, A. Alizadeh, H. Hamishehkar, H. Almasi, L. Roufegarinejad, Int. J. Biol. Macromol. 169, 352 (2021)\nS.P. Bangar, S.S. Purewal, M. Trif, S. Maqsood, M. Kumar, V. Manjunatha, A.V. Rusu, Foods 10, 2181 (2021)\nM.A. Sani, M. Azizi-lalabadi, M. Tavassoli, K. Mohammadi, D.J. Mcclements, Nanomaterials 11, 13331 (2021)\nS. Amjadi, H. Almasi, B. Pourfathi, S. Ranjbaryan, J. Polym. Environ. 29, 3068 (2021)\nS. Shaikh, M. Yaqoob, P. Aggarwal, Curr. Res. Food Sci. 4, 503 (2021)\nT.J. Gutiérrez, J.R. Mendieta, R. Ortega-Toro, Food Hydrocoll. 111, 106255 (2021)\nF.M. Fakhouri, S.M. Martelli, T. Caon, J.I. Velasco, R.C. Buontempo, A.P. Bilck, L.H. Innocentini Mei, LWT - Food Sci. Technol. 87, 293 (2018)\nV. Bagheri, B. Ghanbarzadeh, A. Ayaseh, A. Ostadrahimi, A. Ehsani, M. Alizadeh-Sani, P.A. Adun, Polym. Testing 78, 105989 (2019)\nP. Jagadeesh, M. Puttegowda, Y.G.T. Girijappa, S.M. Rangappa, S. Siengchin, Polym. Compos. 43, 160 (2022)\nJ. Pires, C.D. de Paula, V.G.L. Souza, A.L. Fernando, C. Isabel, Polymers 13, 1 (2021)\nS. Amjadi, M. Nazari, S. A. Alizadeh, and H. Hamishehkar, Meat Sci. 373, 131403 (2020)\nZ. Ghasempour, S. Khodaeivandi, H. Ahangari, H. Hamishehkar, S. Amjadi, E. Moghaddas Kia, A. Ehsani, J. Polym. Environ. 30, 2800 (2022)\nS. Amjadi, H. Almasi, H. Hamishehkar, M. Alizadeh Khaledabad, and L. T. Lim, Food Chemistry 373, 131403 (2022)\nA. Etxabide, J.I. Mat, P.A. Kilmartin, Food Hydrocoll. 115, 106593 (2021)\nA.M. Holban, E. Andronescu, V. Grumezescu, A.E. Oprea, A.M. Grumezescu, G. Socol, M.C. Chifiriuc, V. Lazar, F. Iordache, J. Sol-Gel Sci. Technol. 73, 605 (2015)\nK. Li, J. Nam, S. Kang, Y. Liu, J. Lee, Food Chem. 374, 131630 (2022)\nP. Homayounpour, N. Shariatifar, M. Alizadeh-Sani, Food Sci. Nutrition 9, 553 (2021)\nS. G. G. Aziz and H. Almasi, Food Bioprocess Technol. 11, 1552 (2018)\nA. Mehdizadeh, S.A. Shahidi, N. Shariatifar, M. Shiran, A. Ghorbani-HasanSaraei, J. Food Meas. Charact. 16, 1252 (2022)\nM. Mahdi, H. Rostami, S. Mahdi, M. Fathi, Food Biosci. 40, 100857 (2021)\nM. Soofi, S.F. Hosseini, M. Rezaei, Food Chem. 345, 128865 (2021)\nF. Afinjuomo, S. Abdella, S.H. Youssef, Pharmaceuticals 14, 855 (2021)\nS. Amjadi, H. Almasi, H. Hamishehkar, M. Alizadeh Khaledabad, L.T. Lim, Colloids Surf. B Biointerfaces 213, 112401 (2022)\nL. Jiang, F. Liu, F. Wang, H. Zhang, and M. Kang, Food Packag. Shelf Life 31, 100810 (2022)\nS. Amjadi, H. Almasi, A. Ghadertaj, L. Mehryar, J. Food Process. Preserv. 45, e15196 (2021)\nS. Amjadi, S. Gholizadeh, A. Ebrahimi, H. Almasi, H. Hamishehkar, R. Ali, Ind. Crop Prod. 183, 114964 (2022)\nS. Amjadi, S. Nouri, R.A. Yorghanlou, L. Roufegarinejad, J. Thermoplast. Compos. Mater. 35, 2354 (2020)\nS. Ardebilchi Marand, H. Almasi, N. Ardebilchi Marand, Int. J. Biol. Macromol. 190, 667 (2021)\nV. Guna, M. Ilangovan, D. Nataraj, N. Reddy, J. Appl. Polym. Sci. 135, 1 (2018)\nL. Jiang, F. Wang, X. Xie, C. Xie, A. Li, N. Xia, X. Gong, H. Zhang, Int. J. Biol. Macromol. 209, 1307 (2022)\nT. Sartori, G. Feltre, P. J. do Amaral Sobral, R. Lopes da Cunha, and F. C. Menegalli, Food Packag. Shelf Life 18, 221 (2018)\nD. Nataraj, S. Sakkara, M. HN, and N. Reddy, Ind. Crops Prod. 124, 265 (2018).\nM. Alizadeh-Sani, A. Khezerlou, A. Ehsani, Ind. Crops Prod. 124, 300 (2018)\nE. Fortunati, F. Luzi, A. Jiménez, D.A. Gopakumar, D. Puglia, S. Thomas, J.M. Kenny, A. Chiralt, L. Torre, Carbohydr. Polym. 149, 357 (2016)\nN.A. El-Wakil, E.A. Hassan, R.E. Abou-Zeid, A. Dufresne, Carbohydr. Polym. 124, 337 (2015)\nW. Yang, J.M. Kenny, D. Puglia, Ind. Crops Prod. 74, 348 (2015)\nS. Sherafatkhah Azari, A. Alizadeh, L. Roufegarinejad, N. Asefi, H. Hamishehkar, J. Polym. Environ. 29, 1143 (2021)\nS. S. Azari, A. Alizadeh, L. Roufegarinejad, N. Asef, and H. Hamishehkar J. Polym. Environ. 29, 1143 (2021)\nD.B. Lee, D.W. Kim, Y. Shchipunov, C.S. Ha, Polymer Int. 65, 1039 (2016)\nJ. Wu, H. Liu, S. Ge, S. Wang, Z. Qin, L. Chen, Q. Zheng, Q. Liu, Q. Zhang, Food Hydrocoll. 43, 427 (2015)\nP. Montero, M. Mosquera, D. Marín-Peñalver, A. Alemán, Ó. Martínez-Álvarez, M.C. Gómez-Guillén, J. Food Eng. 244, 47 (2019)\nA. Alemán, I. Mastrogiacomo, M.E. López-Caballero, B. Ferrari, M.P. Montero, M.C. 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Esfandyari-Manesh, Z. Ghaedi, M. Asemi, M. Khanavi, A. Manayi, H. Jamalifar, F. Atyabi, R. Dinarvand, J. Pharm. 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Gholizadeh","ARTICLE",{"url":142,"publisher":239,"properties":297},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":240,"slug":10,"properties":241,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":245,"manageAffiliations":266,"indexDatabases":277,"url":108,"thumbnailPath":20,"statistic":292,"gsStatistic":20,"type":115,"analyzePriority":20},[],{"issn":242,"title":243,"eissn":244},{"VOID":13},{"EN":15},{"VOID":17},[246,250,254,258,262],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":247,"label":248,"description":249,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":251,"label":252,"description":253,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":255,"label":256,"description":257,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":259,"label":260,"description":261,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},{"id":48,"createTime":20,"updateTime":20,"relativeEntities":263,"label":264,"description":265,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":51},{},[267,272],{"id":55,"createTime":20,"updateTime":20,"relativeEntities":268,"slug":20,"properties":269,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":271,"statistic":20},[],{"title":270},{"EN":59},[61],{"id":63,"createTime":20,"updateTime":20,"relativeEntities":273,"slug":20,"properties":274,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":276,"statistic":20},[],{"title":275},{"EN":67},[],[278,285],{"id":71,"indexDatabase":279,"url":84,"indexYears":20,"academicFieldIds":284,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":280,"label":281,"description":282,"key":80,"publicationTags":283,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86],{"id":88,"indexDatabase":286,"url":99,"indexYears":100,"academicFieldIds":291,"indexDatabaseRanking":107},{"id":90,"createTime":20,"updateTime":20,"relativeEntities":287,"label":288,"description":289,"key":96,"publicationTags":290,"standard":20},[],{"EN":93,"VI":93},{"EN":93,"VI":95},[98],[102,103,104,105,106],{"impactFactor":21,"impactFactorByYear":293,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":111,"totalPublicationByYear":294,"totalCitation":21,"totalCitationByYear":295,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":296,"hindexLast5Year":21,"hindex":21},{},{"2021":111},{},{},{"pages":298},{"VOID":299},"1-13","2023-12-21",2023,[82,107],false,{"id":305,"createTime":306,"updateTime":307,"relativeEntities":308,"slug":309,"properties":310,"entityType":136,"verifyStatus":137,"verifyTime":320,"verifyNote":139,"languages":20,"translateLanguages":321,"viewCount":111,"primaryUrl":322,"fullTextUrl":20,"authors":323,"publicationType":237,"publisherRelationship":354,"citationCount":20,"citationInfo":20,"publishDate":418,"publishYear":419,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":420,"openAccess":20,"references":20,"isForceReanalyzing":303},"10b9c97c-6738-4cf6-b15a-c7e9e6f08ec7","2024-02-13T04:43:57.037+00:00","2026-09-06T11:11:36.782+00:00",[],"Phase-Behavior-of-the-%CE%B9-Carrageenan-Maltodextrin-Water-System-at-Different-Potassium-Chloride-Concentrations-and-Temperatures",{"abstract":311,"title":313,"references":316,"doi":318},{"EN":312},"Equilibrium phase diagrams of the ι-carrageenan\u002Fmaltodextrin\u002Fwater system have been established at potassium chloride (KCl) concentrations of 0.1, 0.2, and 0.3 M and 80, 85 and 90°C. All pseudo-binary phase diagrams of ι-carrageenan\u002Fmaltodextrin mixtures suggested classic segregative phase separation. The binodal was heavily skewed toward the maltodextrin axis. The high asymmetry of the ι-carrageenan\u002Fmaltodextrin\u002Fwater phase diagram determined by the phase-volume-ratio method was consistent with the compositional analysis of phase-separated ι-carrageenan\u002Fmaltodextrin samples and can be explained in terms of the Flory–Huggins interaction parameter, reflecting a higher water-binding ability of the charged ι-carrageenan than neutral maltodextrin. Increasing the concentration of ι-carrageenan-gel-promoting KCl from 0.1 to 0.3 M at 80°C enlarged the two-phase domain, whereas increasing temperature from 80 to 90°C at 0.3 M KCl enhanced biopolymer compatibility. The effects of salt concentration and temperature have been related to the differences in the Flory–Huggins interaction parameters of the two biopolymers with water as well as the helix formation of ι-carrageenan in the presence of KCl through the changes in the slopes of tie lines of phase-separated samples.",{"EN":314,"VI":315},"Phase Behavior of the ι-Carrageenan\u002FMaltodextrin\u002FWater System at Different Potassium Chloride Concentrations and Temperatures","Hành vi pha của hệ ι-carrageenan\u002Fmaltodextrin\u002Fnước ở các nồng độ kali clorua và nhiệt độ khác nhau",{"VOID":317},"S. Kasapis, I.M. Al-Marhoobi, Biomacromolecules 6, 14–23 (2005). doi:10.1021\u002Fbm0400473\nY. Fang, L. Li, C. Inoue, L. Lundin, I. Appelqvist, Langmuir 22, 9532–9537 (2006). doi:10.1021\u002Fla061865e\nS. Kasapis, Int. J. Food Sci. Technol. 30, 693–710 (1995)\nE. Scholten, L.M.C. Sagis, E. van der Linden, Macromolecules 38, 3515–3518 (2005). doi:10.1021\u002Fma047705w\nL. Piculell, B. Lindman, Adv. Colloid Interface Sci. 41, 149–178 (1992). doi:10.1016\u002F0001-8686(92)80011-L\nM.T. Nickerson, A.T. Paulson, E. Wagar, R. Farnworth, S.M. Hodge, D. Rousseau, Food Hydrocoll. 20, 1072–1079 (2006). doi:10.1016\u002Fj.foodhyd.2005.12.003\nM.F. Butler, Biomacromolecules 3, 676–683 (2002). doi:10.1021\u002Fbm025501m\nS. Kasapis, E.R. Morris, I.T. Norton, M.J. Gidley, Carbohydr. Polym. 21, 249–259 (1993). doi:10.1016\u002F0144-8617(93)90056-A\nN. Lorén, A.-M. Hermansson, Int. J. Biol. Macromol. 27, 249–262 (2000). doi:10.1016\u002FS0141-8130(00)00127-6\nParis L U.S. Patent 6,331,205 (2001)\nOng MH, Whitehouse AS U.S. Patent 6,592,926 (2003)\nF. van de Velde, A.S. Antipova, H.S. Rollema, T.V. Burova, N.V. Grinberg, L. Pereira, P.M. Gilsenan, R.H. Tromp, B. Rudolph, V.Y. Grinberg, Carbohydr. Res. 340, 1113–1129 (2005). doi:10.1016\u002Fj.carres.2005.02.015\nH. Nakashima, Y. Kido, N. Kobayashi, Y. Motoki, M. Neushul, N. Yamamoto, Antimicrob. Agents Chemother. 31, 1524–1528 (1987)\nG. Marcelo, E. Saiz, M.P. Tarazona, Biophys. Chem. 113, 201–208 (2005). doi:10.1016\u002Fj.bpc.2004.09.005\nM. Watase, K. Nishinari, Makromol. Chem. 188, 2213–2221 (1987). doi:10.1002\u002Fmacp.1987.021880918\nC.M. Durrani, D.A. Pryrtupa, A.M. Donald, A.H. Clark, Macromolecules 26, 981–987 (1993). doi:10.1021\u002Fma00057a016\nA. Pohu, V. Planchot, J.L. Putaux, P. Colonna, A. Buléon, Biomacromolecules 5, 1792–1798 (2004). doi:10.1021\u002Fbm049881i\nC. Loret, S. Schumm, P.D.A. Pudney, W.J. Frith, P.J. Fryer, Food Hydrocoll. 19, 557–565 (2005). doi:10.1016\u002Fj.foodhyd.2004.10.030\nG.R. Ziegler, S.S.H. Rizvi, J. Food Sci. 54, 430–436 (1989). doi:10.1111\u002Fj.1365-2621.1989.tb03100.x\nV.I. Polyakov, V.Y. Grinberg, V.B. Tolstoguzov, Polym. Bull. 2, 757–760 (1980). doi:10.1007\u002FBF00255893\nM. Darder, M. López-Blanco, P. Aranda, F. Leroux, E. Ruiz-Hitzky, Chem. Mater. 17, 1969–1977 (2005). doi:10.1021\u002Fcm0483240\nK. Bongaerts, S. Paoletti, B. Denef, K. Vanneste, F. Cuppo, H. Reynaers, Macromolecules 33, 8709–8719 (2000). doi:10.1021\u002Fma000996y\nK.B. Guiseley, N.F. Stanley, P.A. Whitehouse, Handbook of water-soluble gums and resins, in Carrageenan, ed. by R.L. Davidson (McGraw-Hill, New York, 1980)\nA. Cesàro, F. Cuppo, D. Fabri, F. Sussich, Thermochim. Acta 328, 143–153 (1999). doi:10.1016\u002FS0040-6031(98)00635-2\nD.Z. Icoz, J.L. Kokini, Carbohydr. Polym. 70, 181–191 (2007). doi:10.1016\u002Fj.carbpol.2007.03.012\nP.J. Flory, Principles of polymer chemistry (Cornell University Press, Ithaca, NY, 1953)\nC.C. Hsu, J.M. Prausnitz, Macromolecules 7, 320–324 (1974). doi:10.1021\u002Fma60039a012\nH. Hinsken, W. Borchard, Colloid Polym. Sci. 273, 913–925 (1995). doi:10.1007\u002FBF00660368\nS. Radosta, F. Schierbaum, F. Reuther, H. Anger, Starch\u002FStärke 41, 395–401 (1989)\nT.S. Nordmark, G.R. Ziegler, Food Hydrocoll. 14, 579–590 (2000). doi:10.1016\u002FS0268-005X(00)00037-0\nV. Normand, P.D.A. Pudney, P. Aymard, I.T. Norton, J. Appl. Polym. Sci. 77, 1465–1477 (2000). doi:10.1002\u002F1097-4628(20000815) 77:7\u003C1465::AID-APP8>3.0.CO;2-F\nF. van de Velde, H.S. Rollema, N.V. Grinberg, T.V. Burova, V.Y. Grinberg, R.H. Tromp, Biopolymers 65, 299–312 (2002). doi:10.1002\u002Fbip.10250\nL. Piculell, K. Bergfeldt, Biopolymer mixtures, in Factors determining phase behaviour of multi component polymer systems, ed. by S.E. Harding, S. Hill, J.R. Mitchell (Nottingham University Press, Manor Farm, Main Street, Thrumpton, Nottingham, NG11 0AX, UK, 1995)\nK.S. Hossain, K. Miyanaga, H. Maeda, N. Nemoto, Biomacromolecules 2, 442–449 (2001). doi:10.1021\u002Fbm000117f\nN. Lorén, A.-M. Hermansson, M.A.K. Williams, L. Lundin, T.J. Foster, C.D. Hubbard, A.H. Clark, I.T. Norton, E.T. Bergström, D.M. Goodall, Macromolecules 34, 289–297 (2001). doi:10.1021\u002Fma0013051\nL. Piculell, C. Rochas, Carbohydr. Res. 208, 127–138 (1990). doi:10.1016\u002F0008-6215(90)80092-H\nL. Piculell, S. Nilsson, P. Muhrbeck, Carbohydr. Polym. 18, 199–208 (1992). doi:10.1016\u002F0144-8617(92)90064-W\nV.Y. Grinberg, N.V. Grinberg, A.I. Usov, N.P. Shusharina, A.R. Khokhlov, K.G. de Kruif, Biomacromolecules 2, 864–873 (2001). doi:10.1021\u002Fbm0100460",{"VOID":319},"10.1007\u002Fs11483-009-9108-9","2025-02-20T11:06:53.490+00:00",[141],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11483-009-9108-9",[324,339],{"id":325,"sortIndex":21,"researcher":20,"roles":326,"affiliations":327,"properties":336,"displayName":338,"givenName":20,"familyName":20},"344132f1-bd65-4888-9870-1ab07e83c608",[147],[328],{"id":329,"sortIndex":21,"affiliation":330,"properties":20},"ca98b2ef-d895-4425-9d22-e444ea349fcf",{"id":329,"createTime":20,"updateTime":20,"relativeEntities":331,"slug":20,"properties":332,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":335,"statistic":20},[],{"title":333},{"VI":334},"School of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai, China",[],{"title":337},{"VI":338},"Xiaoyong Wang",{"id":340,"sortIndex":111,"researcher":20,"roles":341,"affiliations":342,"properties":351,"displayName":353,"givenName":20,"familyName":20},"4dacd491-43bf-44b3-aba7-4566e3e99172",[147],[343],{"id":344,"sortIndex":21,"affiliation":345,"properties":20},"83ed3091-5ea9-4345-93b1-fab6f2c48bd1",{"id":344,"createTime":20,"updateTime":20,"relativeEntities":346,"slug":20,"properties":347,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":350,"statistic":20},[],{"title":348},{"VI":349},"Department of Food Science, Penn State University, University Park, USA",[],{"title":352},{"VI":353},"Gregory R. Ziegler",{"url":322,"publisher":355,"properties":413},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":356,"slug":10,"properties":357,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":361,"manageAffiliations":382,"indexDatabases":393,"url":108,"thumbnailPath":20,"statistic":408,"gsStatistic":20,"type":115,"analyzePriority":20},[],{"issn":358,"title":359,"eissn":360},{"VOID":13},{"EN":15},{"VOID":17},[362,366,370,374,378],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":363,"label":364,"description":365,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":367,"label":368,"description":369,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":371,"label":372,"description":373,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":375,"label":376,"description":377,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},{"id":48,"createTime":20,"updateTime":20,"relativeEntities":379,"label":380,"description":381,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":51},{},[383,388],{"id":55,"createTime":20,"updateTime":20,"relativeEntities":384,"slug":20,"properties":385,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":387,"statistic":20},[],{"title":386},{"EN":59},[61],{"id":63,"createTime":20,"updateTime":20,"relativeEntities":389,"slug":20,"properties":390,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":392,"statistic":20},[],{"title":391},{"EN":67},[],[394,401],{"id":71,"indexDatabase":395,"url":84,"indexYears":20,"academicFieldIds":400,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":396,"label":397,"description":398,"key":80,"publicationTags":399,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86],{"id":88,"indexDatabase":402,"url":99,"indexYears":100,"academicFieldIds":407,"indexDatabaseRanking":107},{"id":90,"createTime":20,"updateTime":20,"relativeEntities":403,"label":404,"description":405,"key":96,"publicationTags":406,"standard":20},[],{"EN":93,"VI":93},{"EN":93,"VI":95},[98],[102,103,104,105,106],{"impactFactor":21,"impactFactorByYear":409,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":111,"totalPublicationByYear":410,"totalCitation":21,"totalCitationByYear":411,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":412,"hindexLast5Year":21,"hindex":21},{},{"2021":111},{},{},{"pages":414,"volume":416},{"VOID":415},"119-125",{"VOID":417},"4","2009-04-29",2009,[82,107],{"id":422,"createTime":423,"updateTime":424,"relativeEntities":425,"slug":426,"properties":427,"entityType":136,"verifyStatus":137,"verifyTime":438,"verifyNote":139,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":439,"fullTextUrl":20,"authors":440,"publicationType":237,"publisherRelationship":531,"citationCount":21,"citationInfo":595,"publishDate":598,"publishYear":596,"citationAnalyzeStatus":599,"lastCitationAnalyze":600,"indexDatabases":601,"openAccess":20,"references":20,"isForceReanalyzing":303},"b47bf365-8c4c-4358-8120-b320c76e18c4","2024-02-05T17:39:44.810+00:00","2026-07-24T08:28:14.851+00:00",[],"Multiple-Effects-of-Viscosity-Water-Activity-and-Glass-Transition-Temperature-on-Peroxidase-Activity-in-Binary-and-Ternary-Carbohydrate-Solutions",{"abstract":428,"title":430,"gsPaper":432,"references":434,"doi":436},{"EN":429},"The individual and combined effects of water activity (aw), bulk viscosity and glass transition temperature (Tg’) on the activity of horseradish peroxidase (HRP) in buffered sugars (glucose, trehalose and maltose) and maltodextrin solutions were investigated. Viscosity was the most important factor in the inhibition of HRP activity; however, when Tg’ was changed by the using solutes with different molecular weight, it became a key factor in the modulation of enzyme activity. Viscosity being equal, the sugar addition to maltodextrin solution lowered aw and lowered Tg’ causing an increase of the enzymatic activity. Nevertheless, an inhibition of the HRP activity occurred when aw values of 0.87 were reached due to the addition of glucose, which, among the tested sugars, showed the lowest molecular weight. Among disaccharides, maltose was more effective than trehalose in impairing the enzyme activity both in binary and ternary systems, and this is due to a non competitive biochemical inhibition exerted by this sugar on HRP. When compared to glucose, maltose and trehalose were more effective in reducing HRP activity only in the low viscosity range whilst in the high viscosity range (1–4 10−6 m2 s−1) glucose, despite its lower Tg’ value, was slightly more efficient than disaccharides due to its aw lowering effect.",{"EN":431},"Multiple Effects of Viscosity, Water Activity and Glass Transition Temperature on Peroxidase Activity in Binary and Ternary Carbohydrate Solutions",{"VOID":433},"[\"6575136009877444276\"]",{"VOID":435},"L. Acker, Enzyme activity at low water contents, in Recent advances in food science, ed. by J.M. Leitch, D.N. Rhodes, 3rd edn. (Butterworths, London, 1962), pp. 239–347\nR.B. Drapron, Ann. Technol. Agr. 21, 487 (1972)\nK.L. Parkin, Environmental effects in enzyme activity, in Enzymes in food processing, ed. by T. Nagodawithana, G. Reed (Academic, London, 1993), pp. 39–69\nR.W. Farwell, E. Ackerman, Biophys. J. 86, 479–491 (1963)\nL. Acker, Food Technol. 23, 1257–1270 (1969)\nS. 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Torreggiani, G. Sacchetti, J. Food Eng. 101, 289–295 (2010)\nL. Neri, P. Pittia, G. Bertolo, D. Torreggiani, G. Sacchetti, Food Biophys. 6, 281–287 (2011)\nT. Furuki, Carbohydr. Res. 337, 441–450 (2002)\nJ.G. Sampedro, S. Uribe, Mol. Cell. Biochem. 256\u002F257, 319–327 (2004)\nA. Lerbret, P. Bordat, F. Affouard, A. Hédoux, Y. Guinet, M. Descamps, J. Phys. Chem. B 111, 9410–9420 (2007)\nA. Lerbret, F. Affouard, P. Bordat, A. Hédoux, Y. Guinet, M. Descamps, Chem. Phys. 345, 276–274 (2008)\nN.K. Jain, I. Roy, Protein Sci. 18, 24–36 (2009)\nM. Sola Penna, J.R. Meyer-Fernandes, Z. Naturforsch. C 49, 327–330 (1994)\nF.S. Burnette, J. Food Sci. 42, 1–6 (1977)\nF. Pizzocaro, R. Aggujaro, G. Bertolo, Riv. Sci. Alim. 22, 279–284 (1993)\nL.M.M. Tijskens, P.S. Rodis, M.L.A.T.M. Hertog et al., J. Food Eng. 34, 355–370 (1997)\nY. Roos, M. Karel, Biotechnol. Prog. 7, 49–53 (1991)\nE.F. Morales-Blancas, V.E. Chandia, L. Cisneros-Zevallos, J. Food Sci. 67, 146–154 (2002)\nG. Blond, D. Simatos, Food Hydrocoll. 12, 133–139 (1998)\nD. Torreggiani, E. Forni, I. Guercilena et al., Food Res. Int. 32, 441–446 (1999)\nD.S. Reid, Water activity: fundamentals and relationships, in Water activity in foods. Fundamentals and applications, ed. by G.V. Barbosa-Cánovas, A.J. Fontana Jr., S.J. Schmidt, T.P. Labuza (Blackwell Publishing, Oxford, 2007), pp. 15–28\nW.L. Kerr, M.H. Lim, D.S. Reid, H. Chen, J. Sci. Food Agric. 61, 51–56 (1993)\nL. Slade, H. Levine, Crit. Rev. Food Sci. Nutr. 30, 115–360 (1991)\nT. Chen, A. Fowler, M. Toner, Cryobiology 40, 277–282 (2000)\nM. Gordon, J.S. Taylor, J. Appl. Chem. 2, 493–500 (1952)\nM.L. Williams, R.F. Landel, J.D. Ferry, J. Am. Chem. Soc. 77, 3701–3707 (1955)\nG. Sacchetti, L. Neri, L. Laghi, F. Capozzi, D. Mastrocola, P. Pittia, Food Chem. 144, 36–43 (2014)\nM.T. Cicerone, C.L. Soles, Biophys. J. 86, 3836–3845 (2004)\nM. Sola Penna, J.R. Meyer-Fernandes, Arch. Biochem. Biophys. 360, 10–14 (1998)\nC. Branca, S. Magazù, G. Maisano, F. Migliardo, P. Migliardo, G. Romeo, J. Phys. Chem. B 105, 10140–10145 (2001)\nF. Migliardo, S. Magazù, M. Migliardo, J. Mol. Liq. 110, 11–13 (2003)",{"VOID":437},"10.1007\u002Fs11483-014-9348-1","2024-06-23T01:17:44.856+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11483-014-9348-1",[441,458,473,488,503,518],{"id":442,"sortIndex":21,"researcher":20,"roles":443,"affiliations":444,"properties":453,"displayName":455,"givenName":20,"familyName":20},"a277ebba-ed87-4362-b56d-cff2b87b1e34",[147],[445],{"id":446,"sortIndex":21,"affiliation":447,"properties":20},"1a5c289f-2151-42a9-90b2-e7068da3f8b3",{"id":446,"createTime":20,"updateTime":20,"relativeEntities":448,"slug":20,"properties":449,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":452,"statistic":20},[],{"title":450},{"VI":451},"Faculty of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, Mosciano S. Angelo, Italy",[],{"title":454,"gsAuthor":456},{"VI":455},"Lilia Neri",{"VOID":457},"[\"TQSBT2oAAAAJ\"]",{"id":459,"sortIndex":111,"researcher":20,"roles":460,"affiliations":461,"properties":468,"displayName":470,"givenName":20,"familyName":20},"058226a9-62e0-4576-9d1e-82e7bdf60102",[147],[462],{"id":446,"sortIndex":21,"affiliation":463,"properties":20},{"id":446,"createTime":20,"updateTime":20,"relativeEntities":464,"slug":20,"properties":465,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":467,"statistic":20},[],{"title":466},{"VI":451},[],{"title":469,"gsAuthor":471},{"VI":470},"Paola 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appearance of a food significantly affects consumer’s liking and buying decisions. For next-generation plant-based foods, consumers expect them to have the same appearance (color and opacity) as the animal-based products they replace. Therefore, matching the color of plant-based foods to their conventional animal-based counterparts could increase their liking and acceptance by consumers. In this study, three plant-derived food colorants, red beet (red), turmeric (yellow), and butterfly pea flower (blue), were blended to match the color of raw meat, cooked meat, cooked whole egg, and cheddar cheese. Initially, the pigments were incorporated into three separate emulsions representing the three primary colors (red, yellow, and blue). The Kubelka-Munk and color matching theories were then used to determine the amount of each emulsion required to match the spectral reflectance of the animal-based products. Our results show that color matching theory could be used to formulate plant-based emulsions with similar optical properties to animal-based products, including chroma and lightness. However, some discrepancies were observed, which may have been due to differences in the scattering of light by the complex food matrices in animal-based products. The color matching approach developed in this study could be useful for the development of plant-based food products with improved appearances, thereby expanding their consumer appeal.",{"EN":612},"Optimizing the Appearance of Plant-based Foods Using Natural Pigments and Color Matching Theory",{"VOID":614},"[\"10111970186045786083\"]",{"VOID":616},"W. Willett, J. Rockström, B. Loken et al., The Lancet. 393(10170), 447–492 (2019)\nS. Clune, E. Crossin, K. Verghese, J. Clean. Prod. 140, 766–783 (2017)\nD. Tilman, M. Clark, Nature. 515(7528), 518– (2014)\nE. Hallstrom, A. Carlsson-Kanyama, P. Borjesson, J. Clean. Prod. 91, 1–11 (2015)\nD.J. McClements, L. Grossmann, Compr. Rev. Food Sci. F. 20(4), 4049–4100 (2021)\nS.M. Lee, K.T. Lee, S.H. Lee, J.K. Song, J. Food Eng. 119(3), 508–515 (2013)\nJ.B. Hutchings, Food Color and Appearance, 2nd edn. (Aspen Publishers, Gaithersburg, Md., 1999)\nS.P. Suman, P. Joseph, Annu. Rev. Food Sci. T. 4, 79–99 (2013)\nB. Bateman, J.O. Warner, E. Hutchinson et al., Arch. Dis. Child. 89(6), 506–511 (2004)\nD. McCann, A. Barrett, A. Cooper et al., Lancet. 370(9598), 1560–1567 (2007)\nM. Oplatowska-Stachowiak, C.T. Elliott, Crit. Rev. Food Sci. 57(3), 524–548 (2017)\nM.M. Yallapu, P.K.B. Nagesh, M. Jaggi, S.C. Chauhan, Aaps J. 17(6), 1341–1356 (2015)\nT. Esatbeyoglu, A.E. Wagner, V.B. Schini-Kerth, G. Rimbach, Mol. Nutr. Food Res. 59(1), 36–47 (2015)\nH.E. Khoo, A. Azlan, S.T. Tang, S.M. Lim, Food Nutr. Res. 61, 1–21 (2017)\nD. Wannasin, D.J. McClements, Food Biophys. 18, 289–301 (2023)\nP. Kubelka, J. Opt. Soc. Am. 38(5), 448–457 (1948)\nD.B. MacDougall, Woodhead Publ Text. 103, 312–342 (2010)\nD.J. McClements, W. Chantrapornchai, F. Clydesdale, J. Food Sci. 63(6), 935–939 (1998)\nH.R. Davidson, H. Hemmendinger, J. Opt. Soc. Am. 56, 1102–1109 (1966)\nW.J. Zhu, Q.Z. Li, F.Y. Zhang, X.K. Jin, C.Y. Zhu, J. Fiber Sci. Technol. 76(10), 335–342 (2020)\nD.J. McClements, L. Grossmann, Next-Generation Plant-based Foods: Design, Production, and Properties, 1st 2022. ed. (Springer International Publishing, 2022)\nC. Masia, P.E. Jensen, I.L. Petersen, P. Buldo, Foods 11 (2) (2022)\nS.E.S. Michel, R. Scheermeijer, M. Ambuhl, J. Food Eng. 335 (2022)\nX.Y. Hu, H.L. Zhou, D.J. McClements, Food Struct-Neth 33 (2022)\nP.P. Purslow, R.D. Warner, F.M. Clarke, J.M. Hughes, Meat Sci. 159 (2020)\nW. Hergert, T. Wriedt, The MIE Theory (Springer, New York, 2012)\nJ.M. Hughes, F.M. Clarke, P.P. Purslow, R.D. Warner, Compr. Rev. Food Sci. F. 19(1), 44–63 (2020)\nW. Chantrapornchai, F. Clydesdale, D.J. McClements, Colloid Surf. A 155(2–3), 373–382 (1999)\nD. Wannasin, D.J. McClements, Food Biophysics (2022)\nR. Chanamai, D.J. McClements, Food Hydrocolloid. 15(1), 83–91 (2001)\nD.J. McClements, Adv. Colloid Interfac. 97(1–3), 63–89 (2002)\nR.S. Berns, M. Mohammadi, Color. Res. Appl. 32(3), 201–207 (2007)\nP. Koirala, M. Hauta-Kasari, B. Martinkauppi, J. Hiltunen, Color. Res. Appl. 33(6), 461–469 (2008)\nQ.Z. Li, F.Y. Zhang, X.K. Jin, S.C. Zhang, C.Y. Zhu, Sen-I Gakkaishi. 70(9), 218–224 (2014)\nS. Walsh, D. Diamond, Talanta. 42(4), 561–572 (1995)\nR. Barati, KSCE J. Civ. Eng. 17(5), 1139–1148 (2013)\nB.H. Saluena, C.S. Gamasa, J.M.D. Rubial, C.A. Odriozola, Meat Sci. 157 (2019)\nS. Juric, M. Juric, Z. Krol-Kilinska et al., Food Rev. Int. 38(8), 1735–1790 (2022)\nF.J. Francis, F. Clydesdale, Food Colorimetry: Theory and Applications (Avi Pub. Co, Westport, Conn, 1975)\nR. Baixauli, A. Salvador, S.M. Fiszman, Eur. Food Res. Technol. 226(3), 523–530 (2008)\nJ.A. Martinez, M. Melgosa, M.M. Perez, E. Hita, A.I. Negueruela, Food Sci. Technol. Int. 7(5), 439–444 (2001)\nC.H. Trinderup, A. Dahl, K. Jensen, J.M. Carstensen, K. Conradsen, Meat Sci. 102, 1–7 (2015)\nM. Cierach, J. Niedźwiedź, Eur. Food Res. Technol. 239(3), 377–383 (2014)",{"VOID":618},"10.1007\u002Fs11483-023-09809-3","2024-06-25T15:58:18.931+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11483-023-09809-3",[622,639,654],{"id":623,"sortIndex":21,"researcher":20,"roles":624,"affiliations":625,"properties":634,"displayName":636,"givenName":20,"familyName":20},"dec4e385-40b7-4b01-b405-df9d9043e98c",[147],[626],{"id":627,"sortIndex":21,"affiliation":628,"properties":20},"8250f87a-12f4-40cb-90e0-1ddea4dd3f93",{"id":627,"createTime":20,"updateTime":20,"relativeEntities":629,"slug":20,"properties":630,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":633,"statistic":20},[],{"title":631},{"VI":632},"Department of Food Science, University of Massachusetts, Amherst, USA",[],{"title":635,"gsAuthor":637},{"VI":636},"Donpon Wannasin",{"VOID":638},"[\"qOSMdDAAAAAJ\"]",{"id":640,"sortIndex":111,"researcher":20,"roles":641,"affiliations":642,"properties":649,"displayName":651,"givenName":20,"familyName":20},"6cb8a3c9-b59c-4b25-bef2-781b32304be5",[147],[643],{"id":627,"sortIndex":21,"affiliation":644,"properties":20},{"id":627,"createTime":20,"updateTime":20,"relativeEntities":645,"slug":20,"properties":646,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":648,"statistic":20},[],{"title":647},{"VI":632},[],{"title":650,"gsAuthor":652},{"VI":651},"Lutz 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Bioengineering, Zhejiang Gongshang University, Hangzhou, China",[],{"title":673,"gsAuthor":675},{"VI":674},"David Julian McClements",{"VOID":676},"[\"80jf-tkAAAAJ\"]",{"url":620,"publisher":678,"properties":736},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":679,"slug":10,"properties":680,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":684,"manageAffiliations":705,"indexDatabases":716,"url":108,"thumbnailPath":20,"statistic":731,"gsStatistic":20,"type":115,"analyzePriority":20},[],{"issn":681,"title":682,"eissn":683},{"VOID":13},{"EN":15},{"VOID":17},[685,689,693,697,701],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":686,"label":687,"description":688,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":690,"label":691,"description":692,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":694,"label":695,"description":696,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":698,"label":699,"description":700,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},{"id":48,"createTime":20,"updateTime":20,"relativeEntities":702,"label":703,"description":704,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":51},{},[706,711],{"id":55,"createTime":20,"updateTime":20,"relativeEntities":707,"slug":20,"properties":708,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":710,"statistic":20},[],{"title":709},{"EN":59},[61],{"id":63,"createTime":20,"updateTime":20,"relativeEntities":712,"slug":20,"properties":713,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":715,"statistic":20},[],{"title":714},{"EN":67},[],[717,724],{"id":71,"indexDatabase":718,"url":84,"indexYears":20,"academicFieldIds":723,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":719,"label":720,"description":721,"key":80,"publicationTags":722,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86],{"id":88,"indexDatabase":725,"url":99,"indexYears":100,"academicFieldIds":730,"indexDatabaseRanking":107},{"id":90,"createTime":20,"updateTime":20,"relativeEntities":726,"label":727,"description":728,"key":96,"publicationTags":729,"standard":20},[],{"EN":93,"VI":93},{"EN":93,"VI":95},[98],[102,103,104,105,106],{"impactFactor":21,"impactFactorByYear":732,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":111,"totalPublicationByYear":733,"totalCitation":21,"totalCitationByYear":734,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":735,"hindexLast5Year":21,"hindex":21},{},{"2021":111},{},{},{"pages":737},{"VOID":738},"1-11","2023-09-09","2026-07-22T18:00:47.490+00:00",[82,107],{"id":743,"createTime":744,"updateTime":745,"relativeEntities":746,"slug":747,"properties":748,"entityType":136,"verifyStatus":137,"verifyTime":759,"verifyNote":139,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":760,"fullTextUrl":20,"authors":761,"publicationType":237,"publisherRelationship":805,"citationCount":869,"citationInfo":870,"publishDate":873,"publishYear":871,"citationAnalyzeStatus":874,"lastCitationAnalyze":745,"indexDatabases":875,"openAccess":20,"references":20,"isForceReanalyzing":303},"18845dfa-efb6-46cd-80fd-847f03c26bfc","2023-12-12T02:45:26.258+00:00","2026-07-19T09:25:24.779+00:00",[],"Effect-of-Temperature-on-3D-Printing-of-Commercial-Potato-Puree",{"abstract":749,"title":751,"gsPaper":753,"references":755,"doi":757},{"EN":750},"The temperature and composition of food, during the printing process, maybe a key factor impacting on rheological properties. Currently, there is no evidence of authors analysing the effect of printing temperature on the characteristics of final products. The aim of this paper was to study the printability of potato puree when affected by printing variables, such as printing temperature and the composition of the potato puree. The printing temperature was studied at 10 °C, 20 °C and 30 °C, and the effect of the product composition on the printability was studied by analysing the rheological and textural properties. Viscosity-temperature profiles, flow curves and dynamic oscillation frequency analysis of potato puree were some of the techniques used in rheology analysis. Forward extrusion assays of formulated potato puree were used to study the compression force in the 3D printer. Results showed the formulation with higher content of dehydrated potato puree (38 g of dehydrated potato puree in 250 mL of whole milk) at a temperature of 30 °C were the most stable. The printability increase with the amount of the consistency index and the reduction of behaviour index. The mean force from extrusion test was correlated with printability but the effect of temperature did not help define this parameter.",{"EN":752},"Effect of Temperature on 3D Printing of Commercial Potato Puree",{"VOID":754},"[\"16705570471686898701\"]",{"VOID":756},"G. Ares, A. Giménez, A. Gámbaro, Instrumental methods to characterize nonoral texture of dulce de leche. J. Texture Stud. 37(5), 553–567 (2006). https:\u002F\u002Fdoi.org\u002F10.1111\u002Fj.1745-4603.2006.00068.x\nS. Bhattacharya, N. Vasudha, K.S. Krishna Murthy, Rheology of mustard paste: A controlled stress measurement. J. Food Eng. 41(3), 187–191 (1999). https:\u002F\u002Fdoi.org\u002F10.1016\u002FS0260-8774(99)00102-8\nF. Chuanxing, W. Qi, L. Hui, Z. Quancheng, M. Wang, Effects of pea protein on the properties of potato starch-based 3D printing materials. Int. J. Food Eng. 14(3), 1–10 (2018). https:\u002F\u002Fdoi.org\u002F10.1515\u002Fijfe-2017-0297\nI. Dankar, M. Pujolà, F. El Omar, F. Sepulcre, A. Haddarah, Impact of mechanical and microstructural properties of potato puree-food additive complexes on extrusion-based 3D printing. Food Bioprocess Technol. 11(11), 2021–2031 (2018). https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs11947-018-2159-5\nA. Derossi, R. Caporizzi, D. Azzollini, C. Severini, Application of 3D printing for customized food. A case on the development of a fruit-based snack for children. J. Food Eng. 220, 65–75 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.05.015\nF.C. Godoi, S. Prakash, B.R. Bhandari, 3d printing technologies applied for food design: Status and prospects. J. Food Eng. 179, 44–54 (2016). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2016.01.025\nC.A. Hamilton, G. Alici, M. in het Panhuis, 3D printing vegemite and marmite: Redefining “breadboards”. J. Food Eng. 220, 83–88 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.01.008\nS. Holland, T. Foster, W. MacNaughtan, C. Tuck, Design and characterisation of food grade powders and inks for microstructure control using 3D printing. J. Food Eng. 220, 12–19 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.06.008\nH.W. Kim, H. Bae, H.J. Park, Classification of the printability of selected food for 3D printing: Development of an assessment method using hydrocolloids as reference material. J. Food Eng. 215, 23–32 (2017). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.07.017\nC. Le Tohic, J.J. O’Sullivan, K.P. Drapala, V. Chartrin, T. Chan, A.P. Morrison, et al., Effect of 3D printing on the structure and textural properties of processed cheese. J. Food Eng. 220, 56–64 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.02.003\nM. Lille, A. Nurmela, E. Nordlund, S. Metsä-Kortelainen, N. Sozer, Applicability of protein and fiber-rich food materials in extrusion-based 3D printing. J. Food Eng. 220, 20–27 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.04.034\nH. Lipson, M. Kurman, Fabricated: The New World of 3D Printing (John Wiley and Sons, Inc, New York, 2013)\nJ.I. Lipton, Printable food: The technology and its application in human health. Curr. Opin. Biotechnol. 44, 198–201 (2017). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.copbio.2016.11.015\nZ. Liu, M. Zhang, B. Bhandari, Y. Wang, 3D printing: Printing precision and application in food sector. Trends Food Sci. Technol. 69, 83–94 (2017a, September). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.tifs.2017.08.018\nLiu, Z., Zhang, M., Bhandari, B., & Yang, C. (2017b). Impact of Rheological Properties of Mashed Potatoes on 3D Printing. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.04.017\nZ. Liu, M. Zhang, B. Bhandari, C. Yang, Impact of rheological properties of mashed potatoes on 3D printing. J. Food Eng. 220, 76–82 (2018a). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.04.017\nZ. Liu, M. Zhang, C.h. Yang, Dual extrusion 3D printing of mashed potatoes\u002Fstrawberry juice gel. Lwt 96(February), 589–596 (2018b). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.lwt.2018.06.014\nS. Mantihal, S. Prakash, F.C. Godoi, B. Bhandari, Optimization of chocolate 3D printing by correlating thermal and flow properties with 3D structure modeling. Innovative Food Sci. Emerg. Technol. 44(September), 21–29 (2017). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.ifset.2017.09.012\nF. Ronda, S. Pérez-Quirce, A. Angioloni, C. Collar, Impact of viscous dietary fibres on the viscoelastic behaviour of gluten-free formulated rice doughs: A fundamental and empirical rheological approach. Food Hydrocoll. 32(2), 252–262 (2013). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.foodhyd.2013.01.014\nC. Severini, A. Derossi, D. Azzollini, Variables affecting the printability of foods: Preliminary tests on cereal-based products. Innov. Food Sci. Emerg. Technol. 38, 281–291 (2016). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.ifset.2016.10.001\nC. Severini, A. Derossi, I. Ricci, R. Caporizzi, A. Fiore, Printing a blend of fruit and vegetables. New advances on critical variables and shelf life of 3D edible objects. J. Food Eng. 220, 89–100 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.08.025\nJ.R. Stokes, J.H. Telford, Measuring the yield behaviour of structured fluids. J. Non-Newtonian Fluid Mech. 124(1–3 SPEC. ISS), 137–146 (2004). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jnnfm.2004.09.001\nJ. Sun, Z. Peng, W. Zhou, J.Y.H. Fuh, G.S. Hong, A. Chiu, A review on 3D printing for customized food fabrication. Procedia Manufacturing 1, 308–319 (2015). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.promfg.2015.09.057\nJ. Sun, W. Zhou, L. Yan, D. Huang, L.y. Lin, Extrusion-based food printing for digitalized food design and nutrition control. J. Food Eng. 220, 1–11 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jfoodeng.2017.02.028\nF. Yang, M. Zhang, B. Bhandari, Recent development in 3D food printing. Crit. Rev. Food Sci. Nutr. 57(14), 3145–3153 (2017). https:\u002F\u002Fdoi.org\u002F10.1080\u002F10408398.2015.1094732\nF. Yang, M. Zhang, B. Bhandari, Y. Liu, Investigation on lemon juice gel as food material for 3D printing and optimization of printing parameters. LWT Food Sci. Technol. 87, 67–76 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.lwt.2017.08.054\nM. Zhang, A. Vora, W. Han, R.J. Wojtecki, H. Maune, A.B.A. Le, et al., Dual-responsive hydrogels for direct-write 3D printing. Macromolecules 48(18), 6482–6488 (2015). https:\u002F\u002Fdoi.org\u002F10.1021\u002Facs.macromol.5b01550\nL. Zhang, Y. Lou, M.A.I. Schutyser, 3D printing of cereal-based food structures containing probiotics. Food Struct. 18(August), 14–22 (2018). https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.foostr.2018.10.002",{"VOID":758},"10.1007\u002Fs11483-019-09576-0","2024-05-14T10:18:13.431+00:00","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs11483-019-09576-0",[762,779,792],{"id":763,"sortIndex":21,"researcher":20,"roles":764,"affiliations":765,"properties":774,"displayName":776,"givenName":20,"familyName":20},"2a355d22-ed3b-4062-9e80-719ce97c82fe",[147],[766],{"id":767,"sortIndex":21,"affiliation":768,"properties":20},"78d10e00-88d9-4d68-912b-fc8f6f43779c",{"id":767,"createTime":20,"updateTime":20,"relativeEntities":769,"slug":20,"properties":770,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":773,"statistic":20},[],{"title":771},{"VI":772},"Food Technology Department, Universitat Politècnica de València, Valencia, Spain",[],{"title":775,"gsAuthor":777},{"VI":776},"J. Martínez-Monzó",{"VOID":778},"[\"YfFZdb0AAAAJ\"]",{"id":780,"sortIndex":111,"researcher":20,"roles":781,"affiliations":782,"properties":789,"displayName":791,"givenName":20,"familyName":20},"8caed0aa-4d7d-48db-b68e-164fdab048a8",[147],[783],{"id":767,"sortIndex":21,"affiliation":784,"properties":20},{"id":767,"createTime":20,"updateTime":20,"relativeEntities":785,"slug":20,"properties":786,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":788,"statistic":20},[],{"title":787},{"VI":772},[],{"title":790},{"VI":791},"J. 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García-Segovia",{"url":760,"publisher":806,"properties":864},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":807,"slug":10,"properties":808,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":812,"manageAffiliations":833,"indexDatabases":844,"url":108,"thumbnailPath":20,"statistic":859,"gsStatistic":20,"type":115,"analyzePriority":20},[],{"issn":809,"title":810,"eissn":811},{"VOID":13},{"EN":15},{"VOID":17},[813,817,821,825,829],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":814,"label":815,"description":816,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":818,"label":819,"description":820,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":822,"label":823,"description":824,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},{"id":42,"createTime":20,"updateTime":20,"relativeEntities":826,"label":827,"description":828,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":45},{},{"id":48,"createTime":20,"updateTime":20,"relativeEntities":830,"label":831,"description":832,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":51},{},[834,839],{"id":55,"createTime":20,"updateTime":20,"relativeEntities":835,"slug":20,"properties":836,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":838,"statistic":20},[],{"title":837},{"EN":59},[61],{"id":63,"createTime":20,"updateTime":20,"relativeEntities":840,"slug":20,"properties":841,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":843,"statistic":20},[],{"title":842},{"EN":67},[],[845,852],{"id":71,"indexDatabase":846,"url":84,"indexYears":20,"academicFieldIds":851,"indexDatabaseRanking":20},{"id":73,"createTime":20,"updateTime":20,"relativeEntities":847,"label":848,"description":849,"key":80,"publicationTags":850,"standard":20},[],{"EN":76,"VI":76},{"EN":78,"VI":79},[82,83],[86],{"id":88,"indexDatabase":853,"url":99,"indexYears":100,"academicFieldIds":858,"indexDatabaseRanking":107},{"id":90,"createTime":20,"updateTime":20,"relativeEntities":854,"label":855,"description":856,"key":96,"publicationTags":857,"standard":20},[],{"EN":93,"VI":93},{"EN":93,"VI":95},[98],[102,103,104,105,106],{"impactFactor":21,"impactFactorByYear":860,"i10Index":21,"i10IndexLast5Year":21,"totalPublication":111,"totalPublicationByYear":861,"totalCitation":21,"totalCitationByYear":862,"totalCitationPerPublication":21,"totalCitationPerPublicationByYear":863,"hindexLast5Year":21,"hindex":21},{},{"2021":111},{},{},{"pages":865,"volume":867},{"VOID":866},"225-234",{"VOID":868},"14",104,{"total":869,"publishYear":871,"statisticByYear":872},2019,{},"2019-03-27","ERROR_IN_ANALYZE_CITATION",[82,107],{"id":877,"createTime":878,"updateTime":879,"relativeEntities":880,"slug":881,"properties":882,"entityType":136,"verifyStatus":137,"verifyTime":893,"verifyNote":139,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":894,"fullTextUrl":20,"authors":895,"publicationType":237,"publisherRelationship":973,"citationCount":21,"citationInfo":1037,"publishDate":1040,"publishYear":1038,"citationAnalyzeStatus":599,"lastCitationAnalyze":1041,"indexDatabases":1042,"openAccess":20,"references":20,"isForceReanalyzing":303},"289e1f90-8612-4d34-815b-f155a4875041","2023-12-29T00:21:16.210+00:00","2026-07-14T00:49:07.161+00:00",[],"Simulation-and-Neutron-Diffraction-Studies-of-Small-Biomolecules-in-Water",{"abstract":883,"title":885,"gsPaper":887,"references":889,"doi":891},{"EN":884},"Modern biophysics has benefited greatly from the use of X-ray and neutron diffraction from ordered single crystals of proteins and other macromolecules to give highly detailed pictures of these molecules in the solid state. However, the most biologically relevant environments for these molecules are liquid solutions, and their liquid state properties are sensitive to details of the liquid structuring. The best experimental method for studying such structuring is also neutron diffraction, but of course, the inherent disorder of the liquid state means that these experiments cannot hope to achieve the level of informational detail available from single crystal diffraction. Nonetheless, recent advances in neutron beam intensity, beam stability, and detector sensitivity mean that it should be possible, at least in principle, to use such measurements to extract information about structuring in much more complex systems than have previously been studied. We describe a series of neutron diffraction studies of isotopically labeled molecules in aqueous solution which, when combined with results from computer simulations, can be used to extract conformational information of the hydration of the molecules themselves, essentially opening up new avenues of investigation in structural biology.",{"EN":886},"Simulation and Neutron Diffraction Studies of Small Biomolecules in Water",{"VOID":888},"[\"8597847518780500213\"]",{"VOID":890},"F. Franks, S. Mathias (eds.), Biophysics of water (John Wiley & Sons, Chichester, 1982)\nF.H. Stillinger, Science 209, 451–457 (1980)\nJ. Israelachvili, H. Wennerstrom, Nature 379, 219–225 (1996)\nA. Geiger, P. Mausbach, J. Schnitker, R.L. Blumberg, H.E. Stanley, J. Phys. 45, 13–31 (1984)\nM. Mezei, D.L. Beveridge, J. Comput. Chem. 5, 523–527 (1984)\nR.K. Schmidt, M. Karplus, J.W. Brady, J. Am. Chem. Soc. 118, 541–546 (1996)\nV. Lounnas, B.M. Pettitt, Proteins Struct. Funct. Genet. 18, 133–147 (1994)\nH. 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Acta 27, 531 (1988)",{"doi":1828},"10.1007\u002FBF01329353",{"id":20,"text":1830,"url":20,"identifiers":1831},"P. Manoj, A.D. Watson, D.J. Hibberd et al., J. Colloid Interface Sci. 207, 294 (1998)",{"doi":1832},"10.1006\u002Fjcis.1998.5802",{"id":20,"text":1834,"url":20,"identifiers":1835},"T. Blijdenstein, Langmuir 20, 11321 (2004)",{"doi":1836},"10.1021\u002Fla048608z",{"id":1838,"createTime":1839,"updateTime":1840,"relativeEntities":1841,"slug":1842,"properties":1843,"entityType":136,"verifyStatus":137,"verifyTime":1854,"verifyNote":139,"languages":20,"translateLanguages":20,"viewCount":111,"primaryUrl":1855,"fullTextUrl":20,"authors":1856,"publicationType":237,"publisherRelationship":1915,"citationCount":20,"citationInfo":20,"publishDate":1979,"publishYear":596,"citationAnalyzeStatus":19,"lastCitationAnalyze":1840,"indexDatabases":1980,"openAccess":20,"references":20,"isForceReanalyzing":303},"f886fe9e-823c-4b7e-812c-efac75802b9e","2024-02-13T22:02:45.080+00:00","2026-05-20T13:11:12.628+00:00",[],"Rotational-Thromboelastometry-for-Characterising-Acid-Induced-Gelation-of-Cross-Linked-Casein",{"abstract":1844,"title":1846,"gsPaper":1848,"references":1850,"doi":1852},{"EN":1845},"Rotational thromboelastometry (ROTEM), a method for the clinical characterisation of blood clot formation and fibrinolysis, has been applied to study the acid-induced gelation of cross-linked casein. The results were compared to those from small amplitude oscillatory shear (SAOS) experiments that were carried out on the same samples: acid casein in phosphate buffer and reconstituted skim milk were treated with microbial transglutaminase to achieve cross-linking of casein and to obtain gels with a broad range of stiffness upon acidification with glucono-δ-lactone. Gelation onset was detected consistently 2 min later by ROTEM compared to SAOS, which my be attributed to the differences in the onset criteria of both methods. Comparison of maximum clot firmness (ROTEM) and maximum storage modulus (rheometry) as indicators for gel stiffness revealed a strong non-linear relationship, that was successfully fitted to the common model of ROTEM clot elasticity through adding a proportionality coefficient. From the results of this study it can be concluded that ROTEM might serve as a useful tool for characterising the acid-induced gelation of proteins that are available in only small quantities.",{"EN":1847},"Rotational Thromboelastometry for Characterising Acid-Induced Gelation of Cross-Linked Casein",{"VOID":1849},"[\"5019544334128176252\"]",{"VOID":1851},"J.A. Lucey, J. Dairy Sci. 85, 281 (2002)\nS. P. F. M. Roefs, Structure of acid casein gels: A study of gels formed after acidification in the cold, PhD thesis, Wageningen University (1985)\nJ.A. Lucey, T. van Vliet, K. Grolle, T. Geurts, P. Walstra, Int. Dairy J. 7, 381 (1997)\nG. Bittante, B. Contiero, A. Cecchinato, Int. Dairy J. 29, 115 (2013)\nD.J. McMahon, R.J. Brown, J. Dairy Sci. 65, 1639 (1982)\nR. Aleandri, J.C. Schneider, L.G. Buttazzoni, J. Dairy Sci. 72, 1967 (1989)\nS.M. Donahue, C.M. Otto, J. Vet. Emerg. Crit. Care 15, 9 (2005)\nD. Bolliger, M.D. Seeberger, K.A. Tanaka, Transfus. Med. Rev. 26, 1 (2012)\nK.A. Tanaka, D. 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Rohm, F. Ullrich, C. Schmidt, J. Löbner, D. Jaros, J. Texture Stud. 45, 130 (2014)\nM. Jacob, S. Nöbel, D. Jaros, H. Rohm, Food Hydrocoll. 25, 928 (2011)\nD. Jaros, J. Pätzold, U. Schwarzenbolz, H. Rohm, Food Biophys 1, 124 (2006)\nE. Dickinson, L. Matia Merino, Food Hydrocoll. 16, 321 (2002)\nA.L.M. Braga, M. Menossi, R.L. Cunha, Int. Dairy J. 16, 389 (2006)\nS. Mende, M. Peter, K. Bartels, T. Dong, H. Rohm, D. Jaros, Carbohyd Polym 98, 1389 (2013)\nS. Mende, M. Peter, K. Bartels, H. Rohm, D. 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