2008
DOI: 10.1016/j.foodhyd.2007.11.005
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Enzymatic modification of protein preparation obtained from water-washed mechanically recovered poultry meat

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Cited by 23 publications
(11 citation statements)
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References 40 publications
(38 reference statements)
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“…The values observed for the frankfurter-type sausage with 100% whitemouth croaker meat surimi (E) are in accordance with the results published elsewhere for sausages made with geelbeck croaker surimi (Rahman, Al-Waili, Guizani, & Kasapis, 2007). In this way, it seems that the utilization of the higher quality protein from surimi and the enzymatic modification of this preparation makes it possible to increase the desirable and uniform functional properties due to the increased association of water molecules with the proteins of surimi (Stangierski, Baranowska, Rezler, & Kijowski, 2008).…”
Section: Texture Analysissupporting
confidence: 89%
“…The values observed for the frankfurter-type sausage with 100% whitemouth croaker meat surimi (E) are in accordance with the results published elsewhere for sausages made with geelbeck croaker surimi (Rahman, Al-Waili, Guizani, & Kasapis, 2007). In this way, it seems that the utilization of the higher quality protein from surimi and the enzymatic modification of this preparation makes it possible to increase the desirable and uniform functional properties due to the increased association of water molecules with the proteins of surimi (Stangierski, Baranowska, Rezler, & Kijowski, 2008).…”
Section: Texture Analysissupporting
confidence: 89%
“…In this way, it seems that the utilization of the higher quality protein from surimi increases the desirable functional properties of the frankfurter due to the increased association of water molecules with the proteins of surimi (Stangierski et al. ).…”
Section: Resultsmentioning
confidence: 99%
“…The increase in hardness could be explained by the transglutaminase enhancing protein cross-linking (Herrero et al, 2008). The MTG-catalyzed reaction results in the formation of covalent bonds, which are about 20 times stronger than hydrogen and hydrophobic bonds (Stangierski, Baranowska, Rezler, & Kijowski, 2008). Since covalent bonds possess high binding energy and the ability to crosslink muscle proteins, it is believed to be an important process in building structure in muscle foods; therefore, it is reasonable to speculate that such crosslinks in pork myofibrillar protein will impart improved textural attributes in restructured meat products (Akamittath & Ball, 1992).…”
Section: Textural Propertiesmentioning
confidence: 99%