Food-grade Pickering stabilizers obtained from a protein-rich lupin cultivar (AluProt-CGNA®): Chemical characterization and emulsifying properties

被引:55
作者
Burgos-Diaz, Cesar [1 ]
Wandersleben, Traudy [2 ]
Olivos, Marcos [1 ]
Lichtin, Nicole [1 ]
Bustamante, Mariela [3 ,4 ]
Solans, Conxita [5 ,6 ]
机构
[1] CGNA, Agriaquaculture Nutr Genom Ctr, Temuco, Chile
[2] Univ La Frontera, Dept Chem Sci & Nat Resources, Temuco, Chile
[3] Univ La Frontera, BIOREN, Ctr Food Biotechnol & Bioseparat Sci & Technol Bi, Temuco, Chile
[4] Univ La Frontera, Dept Chem Engn, Temuco, Chile
[5] CSIC, Inst Adv Chem Catalonia, Spanish Natl Res Council, IQAC, Barcelona, Spain
[6] CIBER BBN, Barcelona, Spain
关键词
Pickering emulsions; AluProt-CGNA (R); Emulsifying properties; Lupin protein isolate; Pickering stabilizers; Protein-rich; IN-WATER EMULSIONS; DIFFERENTIAL SCANNING FLUOROMETRY; HIGH-PRESSURE HOMOGENIZATION; HEAT-DENATURED WHEY; SOY PROTEIN; POTENTIAL APPLICATIONS; IONIC-STRENGTH; SALT ADDITION; ALUPROT-CGNA; PARTICLES;
D O I
10.1016/j.foodhyd.2018.09.018
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Pickering stabilizers exhibit unique interfacial properties; however, only limited types of these particles are available for the food industry. Therefore, the main aim of this study was to develop a food-grade Pickering stabilizer using a protein isolate obtained from the protein-rich lupin variety AluProt-CGNA (R) (LPIA). Lupin protein aggregate particles (LP-APs), obtained from LPIA, were produced through a facile and scalable technology based on heat-induced particle formation. LP-APs with high surface charge and partial wettability were effective for stabilizing O/W emulsions. These emulsions were prepared by using high-speed homogenization with LP-APs dispersions. The creaming index, microstructure and physicochemical properties of Pickering emulsions were investigated. The results showed that LP-APs exhibit great potential to perform as stabilizers for O/W Pickering emulsions (O/W). Additionally, LP-APs exhibited much better interfacial and emulsifying properties than did the unheated LPIA. Heating greatly improved the emulsification performance of protein particles, especially at high concentrations (> 3%, w/v). The formed emulsions were highly stable against creaming upon storage over 14 days. These findings are of great importance for the formulation of LP-APs-based emulsions with improved properties (e.g., stable against creaming and coalescence) and will also significantly extend the application of lupin proteins in the food industry.
引用
收藏
页码:847 / 857
页数:11
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