2006
DOI: 10.1002/jsfa.2656
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Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment

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Cited by 47 publications
(15 citation statements)
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“…Hence, HPP has been applied to increase the solubility of muscle proteins and hence improve the functional properties of certain myofibrillar proteins (Sikes et al, 2009). On the other hand, it has also been reported that HPP can induce protein denaturation and thereby result in loss of solubility of the main myofibrillar proteins (Lee, Kim, Lee, Hong, & Yamamoto, 2007). It is, thus, important to investigate the effect of HPP treatment and the two salt levels on the protein solubility in the sausages.…”
Section: Resultsmentioning
confidence: 98%
“…Hence, HPP has been applied to increase the solubility of muscle proteins and hence improve the functional properties of certain myofibrillar proteins (Sikes et al, 2009). On the other hand, it has also been reported that HPP can induce protein denaturation and thereby result in loss of solubility of the main myofibrillar proteins (Lee, Kim, Lee, Hong, & Yamamoto, 2007). It is, thus, important to investigate the effect of HPP treatment and the two salt levels on the protein solubility in the sausages.…”
Section: Resultsmentioning
confidence: 98%
“…Therefore, any treatment affecting structural changes in the muscle can cause the release of water entrapped within the muscle structures. HPP has been shown to influence the structure and function of muscle proteins (Gross & Jaenicke, 1994;Lee, Kim, Lee, Hong, & Yamamoto, 2007;Weber, 1989). With increased pressure muscle fibers become finer and more compact .…”
Section: Moisture Content Cooking Loss and Weight Reductionmentioning
confidence: 99%
“…The effect of high pressure on the noncovalent bonds promotes the dissociation, aggregation, or gelation of proteins (Lullien‐Pellerin and Balny ; Yamamoto and others ). High pressure causes the denaturation of myofibrillar proteins at nondenaturing temperatures with a different mechanism compared to the heat treatment (Fernandez‐Martin ; Lee and others ). The structural modifications of myofibrillar proteins by high pressure are strongly influenced by the pressure level, the treatment temperature, and the ionic strength (Macfarlane and McKenzie ; Yamamoto and others ; Jiménez‐Colmenero ; Chapleau and others ; Lee and others ; Cao and others ).…”
Section: Introductionmentioning
confidence: 99%