Influence of biofilm surface layer protein A ( BslA ) on the gel structure of myofibril protein from chicken breast

BACKGROUND Different techniques have been applied to alter myofibril protein ( MP ) structure, which further promotes protein–protein interactions and influencing the MP gelling characteristics. Influence of BslA from natto food (protein concentration, 30 mg mL −1 ; at 0.001, 0.005, 0.01, 0.05 and 0.1 g kg −1 ) on the characteristics of MP gel of chicken breast was investigated. RESULTS Results show that cooking loss significantly ( P < 0.05) decreased with increased percentage of BslA . Hardness of MP gel did not significantly change at 0.01 g kg −1 BslA . Differential scanning calorimetry disclosed that MP was modified by the addition of BslA . Moreover, BslA produced a high value of storage modulus ( G ′) and low value of phase angle (tan δ ) during heating, especially at 0.01 g kg −1 . Analysis by sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis proved the formation of higher‐molecular‐weight polymers by developing non‐disulfide covalent bonds between MP at 0.01 g kg −1 BslA . Surface hydrophobicity of the MP gel was decreased with increased percentage of BslA . Scanning electron microscopy confirmed the increasing number of uniform cavities of MP gel with the increased percentage of BslA . CONCLUSION Addition of 0.01 g kg −1 BslA significantly improved the water holding capacity and rheological properties of MP by developing non‐disulfide covalent bonds. © 2017 Society of Chemical Industry