2008
DOI: 10.1007/s11947-008-0088-4
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The Acid and Alkaline Solubilization Process for the Isolation of Muscle Proteins: State of the Art

Abstract: The acid and alkaline solubilization processes for isolating muscle protein from ground fish raw materials are investigated by scrutinizing the literature. Following an introduction to the processes, with some underlying chemistry, patents related to the acid and alkaline solubilization process are described together with previously patented methods for processing of protein isolates. Focus is then placed on comparing a range of factors important in fish muscle protein isolation between the acid and alkaline s… Show more

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Cited by 206 publications
(167 citation statements)
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“…However, they also demonstrated that the ISP process increased the surface hydrophobicity and exposed the reactive-SH groups in the myosin head (Kristinsson & Hultin, 2003a). For this reason, the refolding phenomenon in the myosin head in the ISP process as caused by pH contributes to the gel strength of recovered proteins (Nolsøe & Undeland, 2009;Raghavan & Kristinsson, 2008). Additionally, Raghavan and Kristinsson (2008) reported that the ISP-treated myosin from catfish exhibited higher hydrophobicity when NaCl was added after refolding than the control did.…”
Section: Textural Propertiesmentioning
confidence: 99%
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“…However, they also demonstrated that the ISP process increased the surface hydrophobicity and exposed the reactive-SH groups in the myosin head (Kristinsson & Hultin, 2003a). For this reason, the refolding phenomenon in the myosin head in the ISP process as caused by pH contributes to the gel strength of recovered proteins (Nolsøe & Undeland, 2009;Raghavan & Kristinsson, 2008). Additionally, Raghavan and Kristinsson (2008) reported that the ISP-treated myosin from catfish exhibited higher hydrophobicity when NaCl was added after refolding than the control did.…”
Section: Textural Propertiesmentioning
confidence: 99%
“…In addition, the ISPC-gels with 1% NaCl and the CON did not differ in terms of hardness and chewiness. The conformation of muscle proteins is changed by ISP, which modifies properties (Kristinsson & Hultin, 2003b;Nolsøe & Undeland, 2009). The comprehensive disruption of muscle structure by ISP may also be important in aligning proteins for gel formation during heating, thus reducing NaCl demand to induce the same effect (Chang, Feng, & Hultin, 2001;Wright & Lanier, 2005).…”
Section: Textural Propertiesmentioning
confidence: 99%
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“…With the growing awareness that marine resources are fi nite, numerous efforts are underway to improve the utilization of species of low commercial value (NOLSOE & UNDELAND, 2009). Obtaining fi sh protein isolates is an alternative method to diversify and improve the use of these species.…”
mentioning
confidence: 99%