FOOD SCIENCE ›› 2019, Vol. 40 ›› Issue (1): 92-101.doi: 10.7506/spkx1002-6630-20171222-281

• Food Engineering • Previous Articles     Next Articles

Effects of Ultra-high Pressure Processing and Sodium Tripolyphosphate Contents on Water-Holding Capacity of Myosin Gel and Its Heat-Induced Gelation Process

QIAN Chang, XUE Siwen, XU Xinglian*, ZHOU Guanghong*   

  1. National Center of Meat Quality and Safety Control, Key Laboratory of Meat Processing and Quality Control, Ministry of Education, Key Laboratory of Meat Products Processing, Ministry of Agriculture, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing Agricultural University, Nanjing 210095, China
  • Online:2019-01-15 Published:2019-01-22

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Abstract: To investigate the effect of ultra-high pressure (UHP) processing and sodium tripolyphosphate (STPP) contents on the water-holding capacity (WHC) of myosin gel and the heat-induced gelation process, rabbit Psoas major myosin dialyzed against different STPP concentrations (0%, 0.15%, 0.30% or 0.45%) were subjected to UHP treatments (25 ℃, 9 min) at different pressure levels (100, 200 and 300 MPa) before programmed heating (1 ℃/min) to form gels. Unpressurized myosin containing 0.30% STPP was set as the control. The WHC was measured to filter the parameters that had significant effects on gel properties. The protein solubility and ATPase activity and changes in the secondary structure content, surface hydrophobicity, reactive sulfhydryl group content, and rheological properties as well as the gel microstructure during heating were measured. The results indicated that the solubility of myosin containing 0.15% STPP decreased, while its ATPase activity increased significantly (P < 0.05) after pressure treatments below 200 MPa, which indicates that 0.15% STPP could counteract pressure-induced changes in functional properties of myosin. The denaturation and agglomeration process were hindered as well. The counteractive effect was diminished with the increase in STPP content up to 0.30%. The protein underwent sufficient unfolding as well as rapid exposure of buried residues during gelling, which resulted in an elastic, compact and ordered gel network structure and a significant increase in WHC (P < 0.05). The ATPase of myosin was inactivated under 300 MPa, and its solubility decreased as well. The extent of protein denaturation was reduced and intermolecular cross-linking was weakened. As a result, the WHC decreased significantly (P < 0.05). STPP appears to affect the structure and physiochemical properties of myosin, leading to alteration in its denaturation rate and cross-linking pattern during heating and consequently change in WHC eventually.

Key words: myosin, ultra-high pressure, sodium tripolyphosphate, water-holding capacity, gel

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