title: Trypsin inhibitory activity and gel-enhancing effect of sarcoplasmic proteins from common carp.
abstract: Proteinase inhibitory activity of sarcoplasmic protein (SP) extracted from common carp (Cyprinus carpio) muscle and its gel-improving ability were investigated. SPs displayed 89% and 54% inhibitory activity toward trypsin at 40 and 65 °C, respectively. Protein bands with molecular mass of 69, 50, 44, 41, and 35 kDa appeared on trypsin inhibitory activity staining under nonreducing condition when incubated at 40 °C, while 2 protein bands at 54 and 35 kDa were observed at 65 °C. Addition of SP at 0.18 g protein/100 g increased textural properties of threadfin bream surimi gel. However, when SP was added in combination with various CaCl(2) concentrations (0.1% to 0.5%) it did not further improve textural properties as compared to the addition of SP alone. Retention of myosin heavy chain of threadfin bream surimi was greater with the addition of SP. These results indicated that the gel-enhancing effect of common carp SP was due to the inhibitory activity toward endogenous trypsin-like proteinases in threadfin bream surimi.
  
  
  CONCLUSIONS
  Sarcoplasmic protein from common carp muscle could be used as a functional protein ingredient that minimizes muscle proteolysis and improves textural properties of surimi containing trypsin-like endogenous proteinases.
authors.affiliation: Food Protein Research Unit, School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
authors.forename: Siriphon
authors.initials: S
authors.lastname: Siriangkanakun
authors.forename: Jirawat
authors.initials: J
authors.lastname: Yongsawatdigul
mesh_terms: D000818:Animals; D002347:Carps / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D029941:Fish Proteins / Q000378:metabolism*; D005782:Gels / Q000737:chemistry*; D009132:Muscles / Q000201:enzymology; D018995:Myosin Heavy Chains / Q000378:metabolism; D059748:Proteolysis; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D014361:Trypsin Inhibitors / Q000378:metabolism*
chemical_list: D029941:Fish Proteins; D005782:Gels; D014361:Trypsin Inhibitors; D018995:Myosin Heavy Chains