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Effect of mungbean [ V igna radiata (L.) Wilczek] protein isolates on the microbial transglutaminase‐mediated porcine myofibrillar protein gels at various salt concentrations
Author(s) -
Lee Hong C.,
Kang Iksoon,
Chin Koo B.
Publication year - 2014
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.12504
Subject(s) - myofibril , salt (chemistry) , chemistry , gel electrophoresis , microstructure , food science , breaking strength , chromatography , nuclear chemistry , biochemistry , materials science , organic chemistry , crystallography , composite material
Summary This study was performed to investigate the effects of mungbean protein isolates ( MPI ) as a meat/water binder on the MTGase‐mediated porcine myofibrillar protein ( MP ) gels at 0.15, 0.3, and 0.45 m salt concentrations. The general property of MP gel was evaluated by pH, cooking loss ( CL ) (%) and gel strength (gf). Protein–protein interactions among MPI , MTG ase, and MP during cooking were also assessed using gel electrophoresis, thermal analysis and microstructure. When salt content was reduced, gel CL (%; P < 0.05) was increased while pH and gel strength (gf) values were decreased ( P < 0.05). Addition of MTG ase to MP increased pH, CL (%), and gel strength (gf) values, while co‐addition of MTGase and MPI induced synergistic effects on the MP gel strength (gf; ≥0.3 m salt concentration; P < 0.05). In scanning electron micrograph images, increase of salt concentrations made MP gels more swollen and interwoven or conglomerated, regardless of treatment. In conclusion, addition of MPI and MTG ase strengthened gel‐forming ability and improved cooking yield of MP gel at salt concentration (≥0.3 m ).