Heat-Coagulation Property of Fish Sarcoplasmic Proteins.

Morioka, Katsuji; Shimizu, Yutaka

doi:10.2331/suisan.58.1529

Cited by 10 publications

(15 citation statements)

References 2 publications

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“…Most protein bands observed in the raw meat filtrate were well detected when the meat was heated up to 50°C, but gradually disappeared with increasing heating temperature. These results are similar to those of Morioka and Shimizu 31 in different fish species. The intensity of the band with a molecular weight of around 31 kDa did not change at 65°C during 30 min holding time and gradually decreased with increasing holding time at 67°C.…”

Section: Resultssupporting

confidence: 91%

Coagulation test for determining end-point temperature of heated blue marlin meat

2000

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SUMMARY: Applicability of a coagulation test was evaluated for the determination of the previous heat condition of heated blue marlin meat. Meat blocks were heated at different temperatures between 50 and 70°C. Proteins were extracted with different concentrations of NaCl, then subsequently subjected to the coagulation test. The coagulation method was able to determine the end‐point temperature (EPT) of heated blue marlin meat within a range of 1–2°C, up to 67°C. The best correspondence between the actual EPT and coagulation temperature of the filtrates was found when proteins were extracted with 0.9% saline solution. Within the range of 50–67°C, sample preparation methods and holding times had no significant effect on the coagulation temperature of the filtrates. Protein bands of the filtrates on sodium dodecylsulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) gel gradually disappeared with increasing temperature. One band with a molecular weight of about 31 kDa was detected in 67°C‐, but not in 70°C‐heated meat. This protein component was responsible for coagulation at 67°C and was found to be lactate dehydrogenase from the analyses by gel filtration, SDS‐PAGE, and enzyme activity.

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Section: Resultssupporting

confidence: 91%

Coagulation test for determining end-point temperature of heated blue marlin meat

2000

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“…SDS‐PAGE pattern of the filtrates prepared from heated red sea bream meat was quite similar to that from skipjack tuna (data not shown). Comparable observations have also been reported on other fish meats 12,20,21 . It is evident that the SDS‐PAGE patterns of the filtrates from heated fish meats were closely related to the results of the coagulation method (Table 1), suggesting that SDS‐PAGE could detect EPT of heated skipjack tuna and red sea bream meats up to 65°C.…”

Section: Resultssupporting

confidence: 82%

“…This might be due to the insufficient concentration of soluble proteins to produce a visible coagulum 16 . Similar observations were also reported in other fish meats 20,21 . It should be noted that there is an inverse relationship between protein solubility and heating temperature of heated meats 12,16 …”

Section: Resultssupporting

confidence: 65%

Assessing the end-point temperature of heated fish and shellfish meats

et al. 2002

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Attempts have been made to assess the end‐point temperature (EPT) of heated fish and shellfish meats by using the coagulation method together with sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS‐PAGE) analysis and enzyme activity determination. Unfrozen and frozen fish and shellfish meats were heat‐treated at different selected temperatures with 0, 15 or 30 min holding times. Proteins were extracted with NaCl solution. The coagulation method was able to determine EPT of heated fish and shellfish meats between 60 and 67°C. SDS‐PAGE patterns of the filtrates from heated meats were closely related to the results of the coagulation method and enzyme activity determination. Two proteins responsible for producing coagulum of fish meat extracts seem to be lactate dehydrogenase (LDH) and glyceraldehyde phosphate dehydrogenase (GAPDH). End‐point temperatures determined by these methods were not significantly different between unfrozen and frozen samples. On the contrary, a highly thermostable protein with a molecular mass of 35 kDa was detected in heated shellfish meats up to 108°C. In scallop adductor muscle, this highly thermostable protein was found to be the tropomyosin subunit from its amino acid composition and their partial sequences. Tropomyosin could be used as an EPT indicator up to 108°C for heated shellfish meats.

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“…The changes in polygonal structures as a result of added Sp‐ P may be attributed to cross‐linking between Sp‐ P and Mf‐P. As mentioned previously, Morioka and Shimizu (1992) associated improved gelling in threadfin bream surimi to the binding of Sp‐ P to Mf‐P. Nowsad and others (1995) also related the improvement in the gel strength of the suwari gels to the presence of Sp‐ P specifically transglutaminase which mediate (catalyzed) the cross‐linking of myosin heavy chain (MHC) during setting.…”

Section: Resultsmentioning

confidence: 60%

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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Heat-Coagulation Property of Fish Sarcoplasmic Proteins.

Cited by 10 publications

References 2 publications

Coagulation test for determining end-point temperature of heated blue marlin meat

Coagulation test for determining end-point temperature of heated blue marlin meat

Assessing the end-point temperature of heated fish and shellfish meats

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

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