scholarly journals Investigation on Structural Changes of Myofibrillar Proteins from Silver Carp (Hypophthalmichthys molitrix) during Frozen Storage

2013 ◽  
Vol 19 (6) ◽  
pp. 1051-1059 ◽  
Author(s):  
Ren LINA ◽  
Xu YANSHUN ◽  
Jiang QIXING ◽  
Xia WENSHUI ◽  
Qiu CHUNJIANG
Keyword(s):  
Structural Changes ◽  
Silver Carp ◽  
Frozen Storage ◽  
Myofibrillar Proteins ◽  
Hypophthalmichthys Molitrix

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.

Effect of Mild Ozone Oxidation on Structural Changes of Silver Carp (Hypophthalmichthys molitrix) Myosin

2016 ◽  
Vol 10 (2) ◽  
pp. 370-378 ◽  
Author(s):  
Wenxin Jiang ◽  
Yufan He ◽  
Shanbai Xiong ◽  
Youming Liu ◽  
Tao Yin ◽  
...  
Keyword(s):  
Structural Changes ◽  
Silver Carp ◽  
Hypophthalmichthys Molitrix ◽  
Ozone Oxidation

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 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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