Structural Changes and Dynamic Rheological Properties of Sarcoplasmic Proteins Subjected to pH-Shift Method

Tadpitchayangkoon, Panchaporn; Park, Jae W.; Mayer, Steven G.; Yongsawatdigul, Jirawat

doi:10.1021/jf903219u

Cited by 56 publications

(42 citation statements)

References 38 publications

(73 reference statements)

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“…Sarcoplasmic proteins were extracted as described by Tadpitchayangkoon and others () with some modifications. Two grams (2 g) of fish mince was homogenized with 30 mL of cold deionized water for 1 min.…”

Section: Methodsmentioning

confidence: 99%

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Han

Liu

Zhang

et al. 2015

Journal of Food Science

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To investigate the effects of chilling and partial freezing on rigor mortis changes in bighead carp (Aristichthys nobilis), pH, cathepsin B, cathepsin B+L activities, SDS-PAGE of sarcoplasmic and myofibrillar proteins, texture, and changes in microstructure of fillets at 4 °C and -3 °C were determined at 0, 2, 4, 8, 12, 24, 48, and 72 h after slaughter. The results indicated that pH of fillets (6.50 to 6.80) was appropriate for cathepsin function during the rigor mortis. For fillets that were chilled and partially frozen, the cathepsin activity in lysosome increased consistently during the first 12 h, followed by a decrease from the 12 to 24 h, which paralleled an increase in activity in heavy mitochondria, myofibrils and sarcoplasm. There was no significant difference in cathepsin activity in lysosomes between fillets at 4 °C and -3 °C (P > 0.05). Partially frozen fillets had greater cathepsin activity in heavy mitochondria than chilled samples from the 48 to 72 h. In addition, partially frozen fillets showed higher cathepsin activity in sarcoplasm and lower cathepsin activity in myofibrils compared with chilled fillets. Correspondingly, we observed degradation of α-actinin (105 kDa) by cathepsin L in chilled fillets and degradation of creatine kinase (41 kDa) by cathepsin B in partially frozen fillets during the rigor mortis. The decline of hardness for both fillets might be attributed to the accumulation of cathepsin in myofibrils from the 8 to 24 h. The lower cathepsin activity in myofibrils for fillets that were partially frozen might induce a more intact cytoskeletal structure than fillets that were chilled.

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Section: Methodsmentioning

confidence: 99%

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Han

Liu

Zhang

et al. 2015

Journal of Food Science

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show abstract

“…Water‐soluble protein was extracted according to the method of Tadpitchayangkoon et al . () with some modifications. Two grams of fish mince was homogenised with 30 mL cold deionised water using a homogeniser for 1 min.…”

Section: Methodsmentioning

confidence: 99%

Effect of previous frozen storage on quality changes of grass carp (Ctenopharyngodon idellus) fillets during short‐term chilled storage

Yin

Luo

Fan

et al. 2013

Int J of Food Sci Tech

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Summary The effect of chilled, frozen and freeze‐chilled storage on quality of grass carp fillets and soups was evaluated by sensory score, total aerobic counts and biochemical quality. Fish fillets were stored at 4 °C for 6 days (T1), −40 °C for 12 h and then at −20 °C for 5 days (T2), −40 °C for 12 h and then at −20 °C for 5 days, followed by at 4 °C for 4 days (T3). T1 showed higher sensory score, salt‐soluble protein content, better colour and texture qualities than T2 and T3 within 3 days. All fillets kept good quality based on the acceptable limit of sensory score, total volatile basic nitrogen and total aerobic count during storage time. According to the transportation and retail time, chilled storage is appropriate when it is within 3 days. If it extends for 5 days, freeze‐chilling treatment keeps better quality, but later chilled fillets should be retailed within 4 days.

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“…Raghavan and Kristinsson () reported alkali‐treated myosin from catfish exhibited increased surface hydrophobicity compared with control samples. In addition, Tadpitchayangkoon, Park, Mayer, and Yongsawatdigul () observed gradual increases in surface hydrophobicity in soluble sarcoplasmic proteins isolated from striped catfish as pH increased from 6 to 12. Therefore, the present study suggested that blending a higher concentration of FPI compared with surimi can demonstrate increased surface hydrophobicity (Figure ).…”

Section: Resultsmentioning

confidence: 99%

Optimal blending of differently refined fish proteins based on their functional properties

Kobayashi

Park

2017

J Food Process Preserv

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Two different mixtures (Alaska pollock surimi with grass carp fish protein isolate (FPI) and grass carp surimi with grass carp FPI) were investigated for their compatibility and functionalities. As the proportion of FPI increased, it was observed surface hydrophobicity and surface reactive sulfhydryl (SRSH) content increased significantly, indicating the degree of fish protein unfolding prior to gelation was much higher than surimi alone. Comparable results were shown as measured by storage modulus (G 0 ) in oscillatory dynamic rheology, demonstrating the gelling temperature was reduced when the proportion of FPI increased. Effects of mixing surimi and FPI on gel functionality (hardness, cohesiveness, and whiteness) exhibited a linear pattern when the proportion of surimi was larger than or equal to that of FPI. However, there were no linear relationships when the proportion of FPI exceeded that of surimi. Practical applicationsCommercial surimi has been successfully used in the Western world over 30 years. Unlike surimi which is a refined fish myofibrillar protein composite, fish protein isolate (FPI) is a refined composite of myofibrillar protein and sarcoplasmic protein. The former is made by avoiding any chemical/ physical denaturation, while the latter can be made by inducing chemical denaturation and renaturation with pH shift. Even though FPI is not currently available in a commercial scale, it has a great potential to replace all or a part of surimi for the manufacture of fish protein gel products. This study reveals how to optimally mixed these two differently refined fish proteins based on their functional properties. The results suggested that blending surimi and FPI may be feasible only when the proportion of FPI does not exceed 50%.

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Structural Changes and Dynamic Rheological Properties of Sarcoplasmic Proteins Subjected to pH-Shift Method

Cited by 56 publications

References 38 publications

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Effect of previous frozen storage on quality changes of grass carp (Ctenopharyngodon idellus) fillets during short‐term chilled storage

Optimal blending of differently refined fish proteins based on their functional properties

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