scholarly journals Effects of Ozone Treatments on the Physicochemical Changes of Myofibrillar Proteins from Silver Carp (Hypophthalmichthys molitrix) during Frozen Storage

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Rongrong Zhang ◽  
Shanbai Xiong ◽  
Juan You ◽  
Yang Hu ◽  
Ru Liu ◽  
...  
Keyword(s):  
Silver Carp ◽  
Frozen Storage ◽  
Surface Hydrophobicity ◽  
Myofibrillar Proteins ◽  
Breaking Force ◽  
Hypophthalmichthys Molitrix ◽  
Oxidation Treatment ◽  
Gel Texture ◽  
Physicochemical Changes ◽  
Ozone Treatments

Physicochemical changes of myofibrillar proteins from silver carp surimi during frozen storage as affected by two manners of ozone treatments were investigated. For preparation of surimi treated with ozone, ozone water (8 mg/L) was used in either the first (To1) or the second (To2) cycle of rinsing. As compared with control samples (Tc) (rinsing two cycles with water), myofibrillar proteins from To1 surimi showed slightly lower free sulfhydryl contents and higher surface hydrophobicity throughout frozen storage and lower Ca2+-ATPase activities after 30 d. To2 did not significantly (P>0.05) affect these physicochemical properties, indicating that myofibrillar proteins structure was well maintained. Consequently, To1 significantly (P>0.05) decreased breaking force of surimi gels while To2 did not significantly (P>0.05) affect gel breaking force. In addition, the whiteness of surimi gels was increased more obviously by To2 than by To1. The results indicate that To2 could be used as a mild oxidation treatment for improving white color of silver carp surimi without negatively affecting gel texture.

Effects of vacuum chopping on physicochemical and gelation properties of myofibrillar proteins from silver carp (Hypophthalmichthys molitrix)

2018 ◽  
Vol 245 ◽  
pp. 557-563 ◽  
Author(s):  
Yaolan Ma ◽  
Shanbai Xiong ◽  
Juan You ◽  
Yang Hu ◽  
Qilin Huang ◽  
...  
Keyword(s):  
Silver Carp ◽  
Myofibrillar Proteins ◽  
Hypophthalmichthys Molitrix

scholarly journals Chemical changes in silver carp (Hypophthalmichthys molitrix) minced muscle during frozen storage: Effect of a previous washing process

2009 ◽  
Vol 61 (1) ◽  
pp. 95-101 ◽  
Author(s):  
Santiago P. Aubourg ◽  
Afsaneh Asgharzadeh ◽  
Bahareh Shabanpour ◽  
Hedayat Hosseini
Keyword(s):  
Silver Carp ◽  
Frozen Storage ◽  
Storage Effect ◽  
Hypophthalmichthys Molitrix ◽  
Chemical Changes ◽  
Washing Process ◽  
Minced Muscle

scholarly journals Cryoprotective Effects of Protein Hydrolysates Prepared from By-Products of Silver Carp (Hypophthalmichthys Molitrix) on Freeze-Thawed Surimi

2019 ◽  
Vol 9 (3) ◽  
pp. 563
Author(s):  
Wen-Juan Zhou ◽  
Fa-Xiang Wang ◽  
Jian Yu ◽  
Xiang-Hong Li ◽  
Yong-Le Liu
Keyword(s):  
Atpase Activity ◽  
Silver Carp ◽  
Textural Properties ◽  
Surface Hydrophobicity ◽  
Protein Hydrolysates ◽  
Control Group ◽  
Hypophthalmichthys Molitrix ◽  
Freeze Thaw ◽  
And Control ◽  
By Products

The cryoprotective effects of different amounts of protein hydrolysates prepared from by-products of silver carp using Protamex and Alcalase on surimi that were subjected to six freeze-thaw cycles were investigated. Commercial cryoprotectant (8% w/w 1:1 sucrose-sorbitol blend, SuSo) and control (without cryoprotectant) groups were used for comparison. After six freeze-thaw cycles, the lowest actomyosin extractability, Ca2+-ATPase activity and total sulfhydryl content, along with the highest surface hydrophobicity of actomyosin, were observed in the control group (P < 0.05). On the contrary, the group with addition of 2 g of hydrolysate prepared by Protamex hydrolysis (PH-2) displayed the highest actomyosin extractability, Ca2+-ATPase activity and correspondingly, lowest surface hydrophobicity of actomyosin (P < 0.05). Total sulfhydryl content of actomyosin and textural properties of heat-set surimi gels were similar between samples with PH-2 and those with SuSo (P > 0.05). Differences in molecular weight distribution, total and free amino acid compositions between the hydrolysates prepared by Protamex and Alcalase hydrolysis were possible reasons attributing to their variable cryoprotective effects on freeze-thawed surimi. Results from this study clearly support that hydrolysate prepared by Protamex hydrolysis at an appropriate amount could serve as an effective cryoprotectant without increasing the sweetness of surimi products. Furthermore, our findings suggest that the hydrolysates follow a different cryoprotection mechanism compared to SuSo (sucrose-sorbitol blend).

scholarly journals Ovalbumin and Kappa-Carrageenan Mixture Suppresses the Oxidative and Structural Changes in the Myofibrillar Proteins of Grass Carp (Ctenopharyngodon idella) during Frozen Storage

Antioxidants ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1186
Author(s):  
Noman Walayat ◽  
Xiukang Wang ◽  
Asad Nawaz ◽  
Zhongli Zhang ◽  
Abdullah Abdullah ◽  
...  
Keyword(s):  
Grass Carp ◽  
Structural Changes ◽  
Protein Denaturation ◽  
Frozen Storage ◽  
Surface Hydrophobicity ◽  
Ctenopharyngodon Idella ◽  
Myofibrillar Proteins ◽  
Grass Carp Ctenopharyngodon Idella ◽  
Α Helix ◽  
Kappa Carrageenan

This study was done to analyze the cryoprotective influence of ovalbumin (OVA) with kappa-carrageenan (KC) in grass carp myofibrillar proteins during frozen storage. Ca2+-ATPase activity of MP was significantly reduced due to protein denaturation and showed a direct association with decreased sulphydryl (SH) contents and tertiary structural properties. Besides that, an increase in carbonyl, surface hydrophobicity, and dityrosine contents was observed. The addition of OVA-KC significantly restricted the decline in Ca2+-ATPase and SH groups, which were further confirmed by the retarded increase in carbonyls. Furthermore, the addition of OVA-KC increased the stability of α-helix contents. Moreover, MP treated with 6% OVA-KC also improved intermolecular interaction forces linked with gelling and water holding properties of MP. Therefore, it can be concluded that OVA-KC could be used as an effective cryoprotectant in fish and related products for preservation and commercialization.

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