pH-Dependent Behavior and Stability of Protein-Based Particles in Aqueous Media
dc.contributor.author | Ocak, Buğra | |
dc.contributor.author | Coşkun, Alev Emine İnce | |
dc.contributor.author | Ötleş, Semih | |
dc.contributor.author | Ocak, Özgül Özdestan | |
dc.date.accessioned | 2023-01-12T20:29:17Z | |
dc.date.available | 2023-01-12T20:29:17Z | |
dc.date.issued | 2020 | |
dc.department | N/A/Department | en_US |
dc.description.abstract | This review focused on the characteristics of protein particles from different sources, namely wheyproteins, sodium caseinate and gelatin, their structural stability and the stability of dispersions atdifferent pH values. To create particles, controlled aggregation and gelation were used in severalmethods. Different chemical structures of the proteins provide different gelation properties. Wheyproteins undergo thermal denaturation above 68?C, therefore heat-set gelatin was often used for particlepreparation. When whey protein particles were prepared at the iso-electric point (IEP) of proteins, theybecame dense and small; whereas at other pH values, particles were soft and spherical due to increasedrepulsive forces between proteins. Such particles could swell when the pH of the aqueous phase wasaway from the IEP. Sodium caseinate is more heat stable compared to whey proteins; however, it is pHsensitive. When sodium caseinate particles were prepared through acidification, particles were stableagainst disintegration only around the IEP of proteins. More stable caseinate particles could be producedusing enzymatic crosslinking. On the other hand, gelatin particles, which were prepared via cold-setgelation, were stable over a wide pH range; however, as they were thermo-sensitive, particlesdisintegrated above 30?C. This review explained the chemical differences of proteins, preparation ofparticles using different methods, and stability of particles and their dispersions at different conditions.Such differences in protein particles should be carefully investigated before they are used in foodproducts, which could have complex matrix. | en_US |
dc.identifier.doi | 10.18466/cbayarfbe.624428 | |
dc.identifier.endpage | 102 | en_US |
dc.identifier.issn | 1305-130X | |
dc.identifier.issn | 1305-1385 | |
dc.identifier.issue | 1 | en_US |
dc.identifier.startpage | 95 | en_US |
dc.identifier.trdizinid | 458027 | en_US |
dc.identifier.uri | https://doi.org/10.18466/cbayarfbe.624428 | |
dc.identifier.uri | https://search.trdizin.gov.tr/yayin/detay/458027 | |
dc.identifier.uri | https://hdl.handle.net/11454/80417 | |
dc.identifier.volume | 16 | en_US |
dc.indekslendigikaynak | TR-Dizin | en_US |
dc.language.iso | en | en_US |
dc.relation.ispartof | Celal Bayar Üniversitesi Fen Bilimleri Dergisi | en_US |
dc.relation.publicationcategory | Makale - Ulusal Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.title | pH-Dependent Behavior and Stability of Protein-Based Particles in Aqueous Media | en_US |
dc.type | Article | en_US |