title: Effect of combined high pressure and thermal treatment on myofibrillar proteins solubilization of beef muscle.
abstract: The effects of high pressure (to 600 MPa) at different temperatures (20 to 60 °C) for 20 min on protein solubilization and electrophoretic pattern in beef post-rigor longissimus dorsi muscle were studied. The results showed that protein solubilization increased with increasing temperature, especially from 40 °C to 60 °C. A regular trend of protein solubilization was found when isolated myofibrils were subjected to high pressure at different temperatures, an increase was observed with increasing pressure up to about 400 MPa, solubility then decreasing to 600 MPa. Electrophoretic profiles showed that myosin light chains and actin thin filaments were sensitive to pressure, and were released from myofibrils subjected to 100 MPa and higher pressures at the different temperatures.
authors.affiliation: School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, China; E-Mails: yuxiaoling@163.com (X.Y.); prsh@hist.edu.cn (R.P.).
authors.forename: Hanjun
authors.initials: H
authors.lastname: Ma
authors.forename: Guanghong
authors.initials: G
authors.lastname: Zhou
authors.forename: David A
authors.initials: DA
authors.lastname: Ledward
authors.forename: Xiaoling
authors.initials: X
authors.lastname: Yu
authors.forename: Runshu
authors.initials: R
authors.lastname: Pan
mesh_terms: D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D008462:Meat-Packing Industry / Q000379:methods; D009124:Muscle Proteins / Q000737:chemistry*; D009210:Myofibrils / Q000737:chemistry*; D011312:Pressure; D012995:Solubility
chemical_list: D009124:Muscle Proteins