Contribution of sarcoplasmic proteins to gel formation of fish meat.

Morioka, Katsuji; Shimizu, Yutaka

doi:10.2331/suisan.56.929

Cited by 22 publications

(16 citation statements)

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“…Our results, however, where SPs positively contribute to myosin gelation, were supported by several studies (Morioka and Shimizu 1990; Morioka et al. 1997, 1998).…”

Section: Resultssupporting

confidence: 91%

“…Okada (1964) also reported that SPs inhibit the gel formation of myofibrillar proteins. On the other hand, other studies indicated that water‐soluble SPs from mackerel actually increase gel strength (Morioka and Shimizu 1990). The addition of SPs also improved the thermal gelation of milkfish, and has a positive effect on suwari and a restrictive effect on modori (gel softening at 40C) (Ko and Hwang 1995).…”

Section: Introductionmentioning

confidence: 99%

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Characteristics of Sarcoplasmic Proteins and Their Interaction With Myofibrillar Proteins

Kim

Yongsawatdigul

Park

et al. 2005

J Food Biochemistry

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The protein solubility and molecular‐weight distribution of freeze‐dried sarcoplasmic proteins (SPs) from rockfish treated under low and high pH as well as various NaCl concentrations were elucidated. The solubility of SPs was significantly suppressed at an acidic pH (2.0–4.0) and in the presence of high salt concentration (0.5 M NaCl). The least amount of protein was lost when SPs were treated at pH 2.0 or 3.0 followed by precipitation at pH 5.5. The interaction of SPs with Alaska pollock surimi (myofibrillar proteins) was also investigated. The addition of SPs appeared to delay the thermal denaturation of myosin and actin. The SPs positively contributed to the gelation of myofibrillar proteins as judged by breaking force.

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“…Our results, however, where SPs positively contribute to myosin gelation, were supported by several studies (Morioka and Shimizu 1990; Morioka et al. 1997, 1998).…”

Section: Resultssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Characteristics of Sarcoplasmic Proteins and Their Interaction With Myofibrillar Proteins

Kim

Yongsawatdigul

Park

et al. 2005

J Food Biochemistry

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“…For example, by adding only 5% Sp‐ P, the gel strength was improved by approximately 300% compared with the control (Table 2), whereas after adding 35% Sp‐ P, the gel strength increased to approximately 88 g.mm which was 388% greater than the gel strength of the surimi with 5% added Sp‐P (Table 2). The positive effect of added Sp‐P on the surimi gel was reported by Morioka and Shimizu (1990) who carried out an experiment involving the addition of Sp‐P from Pacific mackerel into threadfin bream myofibril at a ratio of 1:3 (Sp‐P: Mf‐P). The resultant kamaboko (Table 3) had greater ( ca.…”

Section: Resultsmentioning

confidence: 65%

“…The increased presence of Sp‐ P is cited as the main cause for weaker gels from fish with a higher degree of dark muscle compared with gels from fish that has a lower degree of dark muscle (Nakagawa and others 1989). On the other hand, some other researchers believe in the enhancive effect of Sp‐ P on the viscoelstic properties of resultant kamaboko, either by retaining Sp‐ P or adding them back to the surimi gel matrix (Macfarlane and others 1977; Nakagawa and Nagayama 1988; Morioka and Shimizu 1990; Park and others 2003; Kim and others 2005a). The inhibitory or enhancive role of Sp‐ P on the gel characteristics of surimi and kamaboko has been reviewed by Gorczyca and Jafarpour (2008).…”

Section: Introductionmentioning

confidence: 99%

Characteristics of Sarcoplasmic Proteins and Their Interaction with Surimi and Kamaboko Gel

Jafarpour¹,

Gorczyca²

2009

Journal of Food Science

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This study examined the effect of adding common carp sarcoplasmic proteins (Sp-P) on the gel characteristics of threadfin bream surimi and kamaboko while maintaining constant moisture and myofibrillar levels. Based on the temperature sweep test, which is involved in heating of surimi gel from 10 to 80• C to monitor the viscoelastic properties, at temperature range of 40 to 50 • C, the decrease level (depth of valley) in storage modulus (G ) thermograph was in proportion to the concentration of added Sp-P. Storage modulus (G ) showed greater elasticity after adding Sp-P compared with the control without Sp-P. Furthermore, the breaking force and distance and consequently gel strength of the resultant kamaboko were improved significantly (P > 0.05). Thus, added Sp-P did not interfere with myofibrillar proteins during sol-gel transition phase but associated with textural quality enhancement of resultant kamaboko; however, addition of Sp-P from the dark muscle of the carp decreased the whiteness of the resultant surimi. Furthermore, according to the SEM micrographs, the gel strength could not be associated with either the number of polygonal structures/mm 2 or the area of the polygonal structures in the kamaboko gel microstructure.

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“…One distinguishing attribute of these processes is that the sarcoplasmic protein of fish muscle is retained. The functions of sarcoplasmic proteins in regards to the formation of myofibrillar protein gels are not clear as to whether they work positively or negatively (Shimizu and Nishioka, 1974;Morioka and Shimizu, 1990). The gelling mechanism of protein recovered from acidic and alkaline processes is quite different from that in conventional surimi production because the recovered protein is denatured at extremely low and high pH values.…”

Section: Introductionmentioning

confidence: 96%

Fish protein recovered using ph shifting method and its physicochemical properties

Choi

Kim

2005

J Ocean Univ. China

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The solubility of meat protein of croaker and jack mackerel was significantly affected by pH shifting. The protein yield of alkali-aided processing is higher than those of conventional and acid-aided processing. The addition of sarcoplasmic protei.n increases the breaking force and deformation value. The breaking force of recovered protein gel from alkali-aided processing is decreased by the addition of NaCI. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed that fish protein of alkali is similar to that at pH 7.0. Alkali-aided processing for recovering fish protein is a valuable method for increasing the utilization of frozen and pelagic fishes and for making kamaboko products.

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Contribution of sarcoplasmic proteins to gel formation of fish meat.

Cited by 22 publications

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Characteristics of Sarcoplasmic Proteins and Their Interaction With Myofibrillar Proteins

Characteristics of Sarcoplasmic Proteins and Their Interaction With Myofibrillar Proteins

Characteristics of Sarcoplasmic Proteins and Their Interaction with Surimi and Kamaboko Gel

Fish protein recovered using ph shifting method and its physicochemical properties

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