Relationship between Molecular Structure and Heat-Induced Gel Properties of Duck Myofibrillar Proteins Affected by the Addition of Pea Protein Isolate
Xueshen Zhu,
Jiaxin Zhang,
Shaohua Liu,
Ying Gu,
Xiaobo Yu,
Feng Gao,
Renlei Wang
Affiliations
Xueshen Zhu
Key Lab of Biological Functional Molecules of Jiangsu Province, College of Life Science and Chemistry, Jiangsu Second Normal University, Nanjing 211200, China
Jiaxin Zhang
Key Lab of Biological Functional Molecules of Jiangsu Province, College of Life Science and Chemistry, Jiangsu Second Normal University, Nanjing 211200, China
Shaohua Liu
Key Lab of Biological Functional Molecules of Jiangsu Province, College of Life Science and Chemistry, Jiangsu Second Normal University, Nanjing 211200, China
Ying Gu
Key Lab of Biological Functional Molecules of Jiangsu Province, College of Life Science and Chemistry, Jiangsu Second Normal University, Nanjing 211200, China
Xiaobo Yu
College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
Feng Gao
College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
Renlei Wang
Key Lab of Biological Functional Molecules of Jiangsu Province, College of Life Science and Chemistry, Jiangsu Second Normal University, Nanjing 211200, China
This paper investigates the relationship between the molecular structure and thermally induced gel properties of duck myofibrillar protein isolate (DMPI) as influenced by the addition of pea protein isolate (PPI). The results showed that b* value of the gels increased; however, a* value decreased with the increase of PPI content (p p p < 0.05), while the storage modulus and loss modulus of the gels were also found to increase, accompanied by the transformation of the α-helix structure into β-sheet, resulting in better dynamics of gel formation. These results indicated the gel-forming ability of DMPI, including water retention and textural properties, improves with increasing PPI addition. Principal component analysis verified these interrelationships. Thus, pea protein could improve the properties of duck myofibrillar protein gels to some extent and improve their microstructure, potentially facilitating the transition from a weak to a non-aggregated, rigid structure.
