Structuring chicken breast analogs via high moisture extrusion of dairy-plant proteins blends

• Published in: International journal of biological macromolecules 2024-12, Vol.283 (Pt 1), p.137368, Article 137368
• Main Authors: Tan, Hui Ru, Wong, Yao Xing, Sow, Cedric Wee Jian, Halim, Fatin Natasha Binte Abdul, Chin, Jeremy Tak Gun, Taheri, Afsaneh, Juan, Du
• Format: Article
• Language: English
• Subjects: Animals; Chickens; Food Handling - methods; Glutens - chemistry; High moisture extrusion; Hybrid dairy-plant based meat analog; Hydrophobic and Hydrophilic Interactions; Meat - analysis; Pea protein; Plant Proteins - chemistry; Plant-based meat analog; Protein chemistry; Protein Structure, Secondary; Soy protein; Soybean Proteins - chemistry; Water - chemistry; Whey protein; Whey Proteins - chemistry
• ISSN: 0141-8130; 1879-0003; 1879-0003
• DOI: 10.1016/j.ijbiomac.2024.137368

Chicken analogs were structured using binary blends of soy protein isolate (SPI) and wheat gluten (WG) or whey protein concentrate (WPC), as well as trinary blends of SPI-WG-WPC via high moisture extrusion. Chicken analogs with anisotropic structures were achieved (anisotropic index >1). Although adding WPC increased hardness, by varying the ratio of SPI to WG in the trinary blends, comparable texture profile properties as cooked chicken breast were achieved. The drivers of the fiber structure formation were non-covalent protein-protein interactions like hydrogen bonds and hydrophobic interactions, and to a lesser extent, inter-protein disulfide bonds formation. β-sheets were the dominant secondary structure, and adding WPC increased the proportion of α-helix while adding WG increased the proportion of β-turns in the meat analog (MA). This study offered strategies on structuring extruded chicken analogs with WPC, a high-quality protein source, and provided insights into mechanisms underlying the formation of fiber structures. •Chicken analogs structured via high moisture extrusion of plant and dairy proteins.•Addition of WG decreased hardness, chewiness, and springiness of chicken analogs.•Non-covalent bonds were the main drivers of structure formation in chicken analogs.•Adding WPC resulted in more compact, but WG resulted in looser protein networks.