Effects of high pressure modification on conformation and gelation properties of myofibrillar protein

• Published in: Food chemistry Vol. 217; pp. 678 - 686
• Main Authors: Zhang, Ziye, Yang, Yuling, Zhou, Peng, Zhang, Xing, Wang, Jingyu
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 15.02.2017
• Subjects: actin; Actins - chemistry; Conformation; disulfide bonds; DSC; gelation; Gelation property; gels; Gels - chemistry; hardness; High pressure; Hydrophobic and Hydrophilic Interactions; hydrophobicity; microstructure; Molecular Conformation; Myofibrillar protein; Myofibrils - chemistry; myosin; Myosins - chemistry; particle size; Pressure; Protein Conformation; protein solubility; Rheology; SEM; sulfhydryl groups; Myofibrillar protein; SEM; Gelation property; DSC; High pressure; Conformation

•Higher pressures induced greater denaturation and unfolding of proteins.•Moderate high pressure (≦200MPa) strengthened protein functionality.•Stronger high pressure (⩾300MPa) weakened protein functionality.•200MPa was the optimum pressure for modification to improve functionality. The effects of hi...