title: Influence of biofilm surface layer protein A (BslA) on the gel structure of myofibril protein from chicken breast.
abstract: 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-1BslA. 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-1BslA. 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.
  
  
  CONCLUSIONS
  Addition of 0.01 g kg-1BslA significantly improved the water holding capacity and rheological properties of MP by developing non-disulfide covalent bonds. © 2017 Society of Chemical Industry.
authors.affiliation: College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi, China.|Department of Human Nutrition, The University Of Agriculture Peshawar, Khyber, Pakhtunkhwa, Pakistan.
authors.forename: Niamat
authors.initials: N
authors.lastname: Ullah
authors.affiliation: College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi, China.
authors.forename: Xuejiao
authors.initials: X
authors.lastname: Wang
authors.affiliation: College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi, China.
authors.forename: Lin
authors.initials: L
authors.lastname: Chen
authors.affiliation: Key Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.
authors.forename: Xinglian
authors.initials: X
authors.lastname: Xu
authors.affiliation: College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi, China.
authors.forename: Zhixi
authors.initials: Z
authors.lastname: Li
authors.affiliation: College of Food Science and Engineering, Northwest A&F University, Yangling, Shaanxi, China.
authors.forename: Xianchao
authors.initials: X
authors.lastname: Feng
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000494:pharmacology*; D018441:Biofilms; D002152:Calorimetry, Differential Scanning; D055598:Chemical Phenomena; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D005782:Gels / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008460:Meat / Q000032:analysis; D008855:Microscopy, Electron, Scanning; D009124:Muscle Proteins / Q000737:chemistry* / Q000187:drug effects; D009210:Myofibrils / Q000737:chemistry*; D012212:Rheology; D014867:Water / Q000032:analysis
chemical_list: D001426:Bacterial Proteins; D005782:Gels; D009124:Muscle Proteins; C070683:surface layer protein A, Bacteria; D014867:Water
keywords: biofilm surface layer protein A; myofibrillar protein; non-disulfide covalent bond; rheological property; water holding capacity