2012
DOI: 10.1016/j.lwt.2012.04.025
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Effect of high pressure on the interactions of myofibrillar proteins from abalone (Haliotis rufencens) containing several food additives

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Cited by 25 publications
(9 citation statements)
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“…The proximal analysis data were comparable with the results reported by Barrios‐Peralta et al . () in fresh red abalone ( H. rufescens ) as well as other abalone species such as H. discus (Gao et al . ), H. midae (Britz and Hecht ) and H. rubra and H. laevigata (Grubert et al .…”
Section: Resultsmentioning
confidence: 99%
“…The proximal analysis data were comparable with the results reported by Barrios‐Peralta et al . () in fresh red abalone ( H. rufescens ) as well as other abalone species such as H. discus (Gao et al . ), H. midae (Britz and Hecht ) and H. rubra and H. laevigata (Grubert et al .…”
Section: Resultsmentioning
confidence: 99%
“…Recently, there have been growing demands for healthier meat products with reduced fat and sodium contents, but the functional properties of the reduced-fat and reduced-salt meat products were affected negatively (Barrios-Peralta, Perez-Won, Tabilo-Munizaga, & Briones-Labarca, 2012). Normally, reducing fat in meat products can be achieved by using leaner meat parts, increasing the amount of water and/or other substances, such as fat replacers being either protein-or carbohydrate-based, whereas reducing salt of NaCl can be achieved by using other kinds of additives as taste enhancers, protein binders and preservatives (Tomaschunas, Zorb, Fischer, Kohn, Hinrichs, & Busch-Stockfisch, 2013).…”
Section: Introductionmentioning
confidence: 99%
“…The solubilization of myofibrillar proteins increased with increasing temperature, especially from 40 °C to 60 °C, and 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 [95]. Barriosperalta et al (2012) [96] found that myofibrillar proteins from abalone and starch interaction increases the emulsifying capacity at pressures over 350 MPa applied for 3~5 min, myofibrillar proteins and egg white interactions at pressures higher than 450 MPa for 5~10 min formed coagulation, decreasing the emulsifying capacity. The reason is that myosin of pressure-induced surimi gelation denaturation and concomitant disulfide bond formation at 300 MPa, 5 °C for 30 min.…”
Section: Effect Of High Pressure On the Water Holding Capacity Of Myomentioning
confidence: 94%