Effects of three treatments on protein structure and gel properties of Perccottus glenii myofibrillar protein

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Guochuan Jiang ◽  
Lili Tian ◽  
Ruifeng Hu ◽  
Hongrui Sun ◽  
Yuan Fu ◽  
...  
Keyword(s):  
Protein Structure ◽  
Hydrophobic Interactions ◽  
Sulfhydryl Group ◽  
Myofibrillar Protein ◽  
Control Group ◽  
Perccottus Glenii ◽  
Scanning Calorimetry ◽  
Gel Properties ◽  
Protein Gels ◽  
Group Protein

Abstract In order to improve Perccottus glenii myofibrillar protein (MP) gel properties, three treatments were evaluated: ultrasonic, transglutaminase (TGase) and combined ultrasonic-transglutaminase treatments. Combined ultrasonic-transglutaminase treatment altered protein structure and gel properties most dramatically. As compared with untreated control group protein, treated protein gels possessed decreased sulfhydryl group content and increases in water holding capacity, whiteness value and hydrophobic interactions that increased gel strength value by up to 3.79 times that of untreated protein gel. Protein structural and Differential scanning calorimetry (DSC) analyses revealed that combined ultrasonic-TGase treatment increased both protein thermal denaturation temperature and UV absorbance (as compared to control and other treatment groups) that supported formation of MP gels with desirable characteristics. These results provide a theoretical basis for development of superior MP gels to promote greater utilization of this fish protein resource by the food industry.

Myofibrillar Protein Structure and Gel Properties of Trichiurus Haumela Surimi Subjected to High Pressure or High Pressure Synergistic Heat

2020 ◽  
Vol 13 (4) ◽  
pp. 589-598 ◽  
Author(s):  
Yanting Chen ◽  
Anqi Xu ◽  
Rong Yang ◽  
Ru Jia ◽  
Jinjie Zhang ◽  
...  
Keyword(s):  
High Pressure ◽  
Protein Structure ◽  
Myofibrillar Protein ◽  
Gel Properties

scholarly journals Emulsion Surimi Gel with Tunable Gel Properties and Improved Thermal Stability by Modulating Oil Types and Emulsification Degree

Foods ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 179
Author(s):  
Shichen Zhu ◽  
Xiaocao Chen ◽  
Jiani Zheng ◽  
Wenlong Fan ◽  
Yuting Ding ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Soybean Oil ◽  
Seed Oil ◽  
Hydrophobic Interactions ◽  
Control Group ◽  
Gel Properties ◽  
Oil Emulsion ◽  
Surimi Gel ◽  
Thermal Stability Of ◽  
Perilla Seed

High resistance to heating treatments is a prerequisite for ready-to-eat (RTE) surimi products. In this study, emulsion-formulated surimi gels were prepared, and the effects of oil types and emulsification degrees on the thermal stability of surimi gel were investigated. The results showed the gel properties of surimi gels were modulated by oil types and emulsification degrees. In detail, the rising pre-emulsification ratio caused the increase of the emulsifying activity index (EAI) and decrease of emulsifying stability index (ESI) for both emulsions. The larger droplet sizes of perilla seed oil than soybean oil may be responsible for their emulsifying stability difference. The gel strength, water retention, dynamic modulus and texture properties of both kinds of surimi gels displayed a firstly increased and then decreased tendency with the rising pre-emulsification ratios. The peak values were obtained as perilla seed oil emulsion with emulsification ratio of 20% group (P1) and soybean oil emulsion with emulsification ratio of 40% group (S2), respectively. Anyway, all emulsion gels showed higher thermal stability than the control group regardless of oil types. Similar curves were also obtained for the changes of hydrogen bond, ionic bond and hydrophobic interactions. Overall, perilla seed oil emulsion with emulsification ratio of 20% (P1 group) contributed to the improved thermal stability of surimi gels.

Antioxidant Mechanism of Yam Saponin, Hesperidin, Ginger Extract on Oxidative Chicken Myofibrillar Protein

2021 ◽  
Vol 15 (3) ◽  
pp. 428-434
Author(s):  
Yingying Cao ◽  
Ping Zhao ◽  
Wenguang Fan ◽  
Yuhui Liu
Keyword(s):  
Plant Extracts ◽  
Sulfhydryl Group ◽  
Surface Hydrophobicity ◽  
Water Holding Capacity ◽  
Control Group ◽  
Myofibrillar Proteins ◽  
Ginger Extract ◽  
Antioxidant Mechanism ◽  
Protein Gels ◽  
Water Holding

The antioxidant mechanism of three plant extracts on the oxidative myofibrillar proteins oxidized by Fe3+/H2O2 at 0 °C for 12 h was analyzed. These plant extracts were added to myofibrillar proteins with the concentrations of 0.5 and 1 mg/mL Besides, the group without added extracts was adopted as controls. Total sulfhydryl content, carbonyls, surface hydrophobicity, and protein cross-linking, protein gel properties were analyzed. In the meantime, the oxidized suspensions were processed as protein gels. Then, the water-holding capacity and the hardness of gels were analyzed. The resulted showed that the suspensions of three plant extracts and the oxidized myofibrillar proteins led to a significant decrease in surface hydrophobicity, carbonyls and gel hardness of the sulfhydryl group, while three plant extracts promoted aggregation of the myofibrillar proteins and increased water-holding capacity of gels compared with that of the control. The scanning electron microscope showed that the gels structure of the three extracts were obviously better than that of the control group, and the ginger group was the best.Yam saponin exhibited the best antioxidant effect, followed by ginger extract and hesperidin.

scholarly journals Nitrogen balance and myofibrillar protein turnover in double muscled Belgian Blue bulls in relation to compensatory growth after different periods of restricted feeding

1998 ◽  
Vol 78 (4) ◽  
pp. 549-559 ◽  
Author(s):  
C. Van Eenaeme ◽  
M. Evrard ◽  
J. L. Hornick ◽  
P. Baldwin ◽  
M. Diez ◽  
...  
Keyword(s):  
Nitrogen Balance ◽  
Compensatory Growth ◽  
Muscle Protein ◽  
Growth Period ◽  
Myofibrillar Protein ◽  
Control Group ◽  
Protein Breakdown ◽  
Low Protein ◽  
Fattening Period ◽  
Synthesis And Degradation

Nitrogen balance and myofibrillar protein breakdown were studied in 16 double-muscled Belgian Blue bulls during a low growth period (0.5 kg d−1) (LGP) of 4 mo (L4), 8 mo (L8), or 14 mo (L14) and the subsequent fattening period (rapid growth period, RGP). The control group (CG) was given a conventional fattening diet; the others received a low-energy, low-protein diet during LGP, and the same diet as the CG during RGP. Measurements were made halfway through the LGP, l mo after the beginning of the fattening period, and 1 mo before slaughter. Nitrogen balance was about half of CG (P < 0.001) during LGP, e.g., 50.8, 21.3, 25.8, and 23.8 g d−1, for CG, L4, L8, and L14, respectively. Between LGP and RGP, N balance increased by about 18 g N d−1 above the control in the compensating groups L4, L8 and L14. This was due to the higher digestibility and the higher metabolizability of the nitrogen in the fattening diet. Lower muscle protein accretion during the LGP resulted from decreased synthesis (P < 0.001) and degradation (P < 0.05) compared with the GC. When changing to RGP different evolution patterns were observed in the three formerly restricted groups, e.g. after a short restriction (L4) both synthesis and degradation rose during the RGP but declined towards the end. After a longer restriction (L8 and L14), synthesis and degradation increased and remained high. The magnitude of these increases was inversely proportional to the length of the restriction period. Key words: Belgian Blue bulls, compensatory growth, nitrogen balance, muscle, muscle protein breakdown

scholarly journals RESVERATROL INCLUSION COMPLEX WITH β-CYCLODEXTRIN (RCD): CHARACTERIZATION AND EVALUATION OF TOXICITY IN WISTAR RATS

2016 ◽  
Vol 9 (1) ◽  
pp. 27 ◽  
Author(s):  
V. S. K. Nishihira ◽  
N. J. Mezzomo ◽  
M. D. Baldissera ◽  
R. A. Vaucher ◽  
C. G. Pinto ◽  
...  
Keyword(s):  
Inclusion Complex ◽  
Oral Administration ◽  
Biochemical Parameters ◽  
Wistar Rats ◽  
Metabolic Diseases ◽  
Hematological Parameters ◽  
Density Lipoprotein ◽  
Blood Parameters ◽  
Control Group ◽  
Scanning Calorimetry

<p class="RSCB01ARTAbstract"><strong>Objective</strong>:<strong> </strong>The aim of this study was to characterise the resveratrol inclusion complex with β-cyclodextrin (RCD) and evaluate their toxicity in wistar rats.</p><p class="RSCB01ARTAbstract"><strong>Methods: </strong>The RCD were prepared in ultra-turrax. For characterization of the RCD were used: Fourier transform infra-red Spectroscopy, Nuclear Magnetic Resonance (NMR), Differential Scanning Calorimetry (DSC) and X-ray powder diffraction. The RCD and others 4 treatments were performed by the chronic oral administration in 35 rats during 60 ds. After the treatments they were euthanized and the serum blood were collected to analyzed some hemogram and biochemical parameters including aspartyl aminotransferase (AST); alanine aminotransferase (AST); phosphatase alkaline (ALP); total bilirubin (TB); direct bilirubin (DB); total protein (TP); total cholesterol (TC), triacylglycerol (TAG), very low-density lipoprotein (VLDL), high-density lipoprotein (HDL), calcium, iron and phosphate using fully automated biochemistry analyzer.</p><p class="RSCB01ARTAbstract"><strong>Results: </strong>The characterization results indicated a successful formation of the RCD. All hematological parameters analysed were within the normal values in all the groups. Furthermore, the hemogram and biochemical parameters were significantly (P&gt;0.05) similar to the control group.</p><p class="RSCB01ARTAbstract"><strong>Conclusion: </strong>The daily oral administration during 60 d of RCD are not harmful on blood parameters of Wistar rats. Thus, RCD can be used safely for treatment of some metabolic diseases.</p>

scholarly journals The Influence of Particle Size and Protein Content in Particle-Filled Myofibrillar Protein Gels

2017 ◽  
Vol 1 (1) ◽  
pp. 109 ◽  
Author(s):  
Andrew J. Gravelle ◽  
Alejandro G. Marangoni ◽  
Shai Barbut
Keyword(s):  
Particle Size ◽  
Protein Content ◽  
Myofibrillar Protein ◽  
Protein Gels

scholarly journals Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review

Foods ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1872
Author(s):  
Huipeng Liu ◽  
Yiyuan Xu ◽  
Shuyu Zu ◽  
Xuee Wu ◽  
Aimin Shi ◽  
...  
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Tertiary Structure ◽  
Quaternary Structure ◽  
Meat Products ◽  
Myofibrillar Protein ◽  
Conformational Structure ◽  
Gel Properties ◽  
The Relationship

In meat processing, changes in the myofibrillar protein (MP) structure can affect the quality of meat products. High hydrostatic pressure (HHP) has been widely utilized to change the conformational structure (secondary, tertiary and quaternary structure) of MP so as to improve the quality of meat products. However, a systematic summary of the relationship between the conformational structure (secondary and tertiary structure) changes in MP, gel properties and product quality under HHP is lacking. Hence, this review provides a comprehensive summary of the changes in the conformational structure and gel properties of MP under HHP and discusses the mechanism based on previous studies and recent progress. The relationship between the spatial structure of MP and meat texture under HHP is also explored. Finally, we discuss considerations regarding ways to make HHP an effective strategy in future meat manufacturing.

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