Characterization of Myosin Subfragment‐1 of Summer and Winter Silver Carp (<i>Hypophthalmichthys molitrix</i>) Muscle

Zheng, Liang; Yu, Kefeng; Yuan, Chunhong; Wang, Xichang; Chen, Shunsheng; Kimura, Ikuo; Konno, Kunihiko

doi:10.1111/j.1750-3841.2012.02835.x

Cited by 15 publications

(8 citation statements)

References 32 publications

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“…To further study it, structural changes of the myosin molecules were also determined by using chymotryptic digestion technique (Konno, 1988, Figure 1). Myosin in a filament form at low salinity could be cleaved at the S1/rod junction by chymotrypsin in the presence of EDTA (Zheng et al, 2012), and the decreased production of S‐1 and rods via the chymotryptic digestion hence would provide an indicator of the denaturation at these two regions (Abe, Kinoshita, & Konno, 2012). The chymotryptic digestion profile of the homogenate was shown in Figure 1a.…”

Section: Resultsmentioning

confidence: 99%

Effects of microbial transglutaminase on textural, water distribution, and microstructure of frozen‐stored longtail southern cod (Patagonotothen ramsayi) fish mince gel

Zhang

Yang

et al. 2022

Journal of Texture Studies

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Frozen-stored fish mince tend to have poor gelling ability due to significant myosin denaturation caused by freezing. In this study, microbial transglutaminase (MTGase) was used to improve the quality of fish mince gel products made from frozen-stored longtail southern cod (LSC). The gel strength of the gel product increased with the addition of MTGase and reached a plateau value of ~19 N mm beyond 300 U/kg of MTGase, at the same condition, T 22 was reduced from 57.22 to 49.77 ms, T 23 was reduced from 1,273.88 to 1,072.27 ms. As the MTGase addition increased from 0 to 400 U/kg, the hardness of the fish surimi gel increased from 14.52 to 21.36 N, and the microstructure changed from loose to dense, respectively. This study showed that MTGase could promote gelation to improve the quality of frozen-stored LSC fish mince gel, especially at 300 U/kg, which potentially can be utilized to produce good surimi gel products out of frozen-stored fish.

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Section: Resultsmentioning

confidence: 99%

Effects of microbial transglutaminase on textural, water distribution, and microstructure of frozen‐stored longtail southern cod (Patagonotothen ramsayi) fish mince gel

Zhang

Yang

et al. 2022

Journal of Texture Studies

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“…Small portions of the minced meat are packed into PET bags and stored at −20 °C for future use. For protein extraction from the porcine heart, a portion of the frozen meat powder is repeatedly homogenized and washed with a solution containing 0.1 mol L –1 of KCl and 20 mmol L –1 of Tris-HCl at pH 7.5 . The myofibril suspension is then filtered through two layers of cotton gauze, and the filtrate is collected for the ensuing study of protein adsorption by the V 12 O 32 -DNA@SVM composite.…”

Section: Methodsmentioning

confidence: 99%

Selective Isolation of Myosin Subfragment-1 with a DNA-Polyoxovanadate Bioconjugate

Chen

Zhang

et al. 2017

Bioconjugate Chem.

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The bioconjugation of a polyoxometalate (POMs), i.e., dodecavanadate (VO), to DNA strands produces a functional labeled DNA primer, VO-DNA. The grafting of DNA primer onto streptavidin-coated magnetic nanoparticles (SVM) produces a novel composite, VO-DNA@SVM. The high binding-affinity of VO with the ATP binding site in myosin subfragment-1 (S1) facilitates favorable adsorption of myosin, with an efficiency of 99.4% when processing 0.1 mL myosin solution (100 μg mL) using 0.1 mg composite. Myosin adsorption fits the Langmuir model, corresponding to a theoretical adsorption capacity of 613.5 mg g. The retained myosin is readily recovered by 1% SDS (m/m), giving rise to a recovery of 58.7%. No conformational change is observed for myosin after eliminating SDS by ultrafiltration. For practical use, high-purity myosin S1 is obtained by separation of myosin from the rough protein extract from porcine left ventricle, followed by digestion with α-chymotryptic and further isolation of S1 subfragment. The purified myosin S1 is identified with matrix-assisted laser desorption/ionization time-of-flight/mass spectrometry, giving rise to a sequence coverage of 38%.

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“…Protein pattern Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed using 12% polyacrylamide gels containing 1 mg mL −1 SDS to determine the protein pattern of shrimp meat after preheating. 22 The shrimp muscle was dissolved in SDS-UM solution which contains 2.0 mg mL −1 SDS, 0.5 mg mL −1 urea, 5.0 mg mL −1 2-mercaptoethanol, and Tris-HCl buffer (containing 2.42 mg mL −1 , pH 7.5). Then the concentration of protein solution was adjusted to 1.2 mg mL −1 , and 10 μL of protein solution was loaded into the gel.…”

Section: Weight Lossmentioning

confidence: 99%

Effect of two‐stage heating treatment on physicochemical properties of shrimp (Penaeus vannamei) meat

et al. 2022

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BACKGROUND Changes in the physicochemical properties of shrimp meat treated with two‐stage heating were investigated. Currently, shrimp products in the processing process are susceptible to uneven dehydration, shrimp meat shrinkage, which results in rough and hard texture, poor chewiness, and seriously affects the edible quality as well as economic benefits. Improving the utilization value of shrimp resources, expanding its market shares, optimizing the tenderness of shrimp is the key to developing new types of fresh and ready‐to‐eat shrimp products. RESULTS The results indicated that preheating at 30 °C could not affect the quality of shrimp meat significantly (P > 0.05). As the preheating temperature increased from 40 °C to 50 °C, the hardness and shear force of shrimp meat decreased due to the exposure of protein hydrophobic groups, protein aggregation and degradation, muscle fraction broken, and weight loss increase. Further increase in preheating temperature would lead to further aggregation and gelation of proteins, causing hardness and shear force increase. Besides, the results of microstructure showed that preheating at 40 °C and 50 °C could cause the shrimp muscles to become loose. CONCLUSION This study showed that the preheating temperature ranging from 40 °C to 50 °C could effectively improve the tenderness of shrimp meat. This study might be useful for developing tenderized shrimp products in the future. © 2022 Society of Chemical Industry.

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Characterization of Myosin Subfragment‐1 of Summer and Winter Silver Carp (Hypophthalmichthys molitrix) Muscle

Cited by 15 publications

References 32 publications

Effects of microbial transglutaminase on textural, water distribution, and microstructure of frozen‐stored longtail southern cod (Patagonotothen ramsayi) fish mince gel

Effects of microbial transglutaminase on textural, water distribution, and microstructure of frozen‐stored longtail southern cod (Patagonotothen ramsayi) fish mince gel

Selective Isolation of Myosin Subfragment-1 with a DNA-Polyoxovanadate Bioconjugate

Effect of two‐stage heating treatment on physicochemical properties of shrimp (Penaeus vannamei) meat

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