2019
DOI: 10.1016/j.jfoodeng.2019.06.013
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Effects of low voltage electrostatic field thawing on the changes in physicochemical properties of myofibrillar proteins of bovine Longissimus dorsi muscle

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Cited by 116 publications
(68 citation statements)
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“…The solubility of myofibrillar protein increased with the aging period up to day 7 and then did not change significantly. This is related to the characteristics of myofibrillar proteins [ 38 , 39 ]. During aging, myofibrillar protein bonds were weakened and more protein hydrolysis was released, which resulted in higher MPS [ 40 ].…”
Section: Resultsmentioning
confidence: 99%
“…The solubility of myofibrillar protein increased with the aging period up to day 7 and then did not change significantly. This is related to the characteristics of myofibrillar proteins [ 38 , 39 ]. During aging, myofibrillar protein bonds were weakened and more protein hydrolysis was released, which resulted in higher MPS [ 40 ].…”
Section: Resultsmentioning
confidence: 99%
“…T 21 represents the bound water tightly combined with macromolecules, T 22 represents the non-flowing water fixed in the myofibrils, and T 23 represents the free water outside the myofibrils. [35] The amplitude of T 2 reflects the bonding strength between water and muscle tissue, and a large signal density indicates high water mobility. [16] It can be seen from the figure that with the extension of storage time, T 21 remained basically unchanged, T 22 decreased significantly, and T 23 increased significantly.…”
Section: Low-field Nuclear Magnetic Resonance (Lf-nmr) Relaxation Time (T 2 ) and Moisture Distributionmentioning
confidence: 99%
“…Due to heavy absorption of salt, the losses of water in salted meat products were primarily due to immobilized water [23,25]. In addition, it was previously reported that the binding capacity between protein and water was effectively retained under low voltage electrostatic field (2.5 kv) [26]. In the current study, the results showed that enhanced water release during storage was supposed to be the result of protein denaturation, which causes meat products to lose their ability to retain water [27], especially when stored for longer periods.…”
Section: Moisture Contentmentioning
confidence: 99%