National anch Center for Conventional Freshwater Fish Processing Wuhan

Wuhan, China

National anch Center for Conventional Freshwater Fish Processing Wuhan

Wuhan, China
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Wang W.,Huazhong Agricultural University | Zhou H.,Huazhong Agricultural University | Yang H.,Huazhong Agricultural University | Yang H.,Collaborative Innovation Center for Efficient and Health Production of Fisheries in Hunan | And 5 more authors.
Food Chemistry | Year: 2017

The objective of this study was to evaluate the effects of salts on the gelatinization and retrogradation of maize and waxy maize starch. Experimental results showed that the salting-out or structure-making ions, such as F− and SO4 2−, decreased the swelling power, solubility and transparency of both starches, but increased the gelatinization temperature, enthalpy, and syneresis, due to the tendency of these ions to protect the hydrogen bond links among starch molecules. On the other hand, the salting-in or structure-breaking ions, such as I− and SCN−, exhibited the opposite effects. Microscopic observations confirmed such effects of salts on both starches. Furthermore, the effects of salts were more significant on waxy maize and on normal maize starch. Generally, salts could significantly influence on the gelatinization and retrogradation of maize and waxy maize starch, following the order of the Hofmeister series. © 2016 Elsevier Ltd


Wang W.,Huazhong Agricultural University | Zhou H.,Huazhong Agricultural University | Yang H.,Huazhong Agricultural University | Yang H.,Collaborative Innovation Center for Efficient and Health Production of Fisheries in Hunan | And 2 more authors.
Journal of Food Science and Technology | Year: 2016

The objective of this study was to evaluate the effects of different salts (NaF, NaCl, NaBr, NaI, K2SO4, KCl, KNO3, KSCN, LiCl) on freeze–thaw stability, gel strength and rheological properties of potato starch. Addition of the structure-making (salting-out) ions, such as F− and SO4 2−, decreased freeze–thaw stability and increased gel strength, maximal storage modulus (G′) and maximal loss modulus (G″) of potato starch, due to a stronger three-dimensional network by promoting the starch retrogradation and inhibiting starch gelatinization. Shear stress versus shear rate of all samples at 25 °C was well fitted to the simple power-law model with high determination coefficients (R2 = 0.9863–0.9990). Flow behavior index (n), consistency index (K) and apparent viscosities increased with adding salting-out ions. However, the structure-breaking (salting-in) ions had reverse effects on freeze–thaw stability, gel strength and rheological characteristics of potato starch. The addition of structure-breaking ions, such as Br−, NO3 −, I−, SCN−, Na+ and Li+, decreased gel strength, G′ and G″ values and increased freeze–thaw stability. Salts could significantly influence on the retrogradation of potato starch, generally following the ion order: F− > SO4 2− > Cl− > Br− > NO3 − > I− > SCN− for anions and K+ > Na+ > Li+ for cations, consistent with the Hofmeister series. © 2016 Association of Food Scientists & Technologists (India)


Cao L.,Huazhong Agricultural University | Cao L.,National anch Center for Conventional Freshwater Fish Processing Wuhan | Su S.,Huazhong Agricultural University | Regenstein J.M.,Cornell University | And 7 more authors.
Food Biophysics | Year: 2015

The role of Ca2+ in gelation of myosin extracted from silver carp (Hypophthalmichthys molitrix) was investigated. Compared with the control, myosin with CaCl2 showed higher turbidity and larger particle size, indicating that CaCl2 contributed to myosin aggregation. Addition of CaCl2 decreased the myosin thermostability and promoted the unfolding of myosin α-helical structure during heating. Moreover, CaCl2 could increase surface hydrophobicity at low temperatures (20–40 °C) and promoted hydrophobic interactions. Meanwhile, it decreased the temperature of disulfide bond formation by about 10 °C. Addition of 10–40 mM CaCl2 favored activation of the Ca2+-ATPase activity at 20 to 30 °C, but not obvious with elevated temperatures. Ca2+-ATPase activity of myosin was undetectable when heated above 60 °C because of severe structural damage of myosin heads. G’ at both the first and second peaks increased with increasing CaCl2 concentration. Therefore, CaCl2 was beneficial for gelation of myosin by inducing the unfolding of myosin and enhancing disulfide bonds along with hydrophobic interactions between neighboring myosin molecules. © 2015 Springer Science+Business Media New York


PubMed | Huazhong Agricultural University, Cornell University and National anch Center for Conventional Freshwater Fish Processing Wuhan
Type: Journal Article | Journal: Journal of food science | Year: 2016

The gel properties of silver carp/pork mince mixtures were investigated as well as the protein structural changes and interactions during gelling using rheology, SEM, and FT-Raman spectroscopy. The breaking force values for gels containing 0% to 40% pork was significantly lower (P < 0.05) compared with gels containing 50% to 100% pork. Gels containing 70% to 100% pork had significantly higher (P < 0.05) breaking force values compared with gels containing 50% to 60% pork. Deformation values were more mixed. Dynamic rheological data suggested that mixing fish and pork at 3:7 could strengthen the gel network. The addition of 40% pork or above, significantly decreased (P < 0.05) the water retention of the gels compared with the 100% fish gels. The dimensional ordering of gels was also reduced by addition of pork. The reduced ordering was one of the reasons for the low water retention for fish/pork mixed gels. Raman spectral analysis confirmed that mixing fish and pork in 7:3 and 3:7 ratios could promote hydrophobic interactions such as bringing tyrosine residues into the intermolecular interface. The interactions in the 3:7 fish/pork mixed gels were favorable for forming a stronger gel. However, the interactions in the 7:3 fish/pork mixed gels were adverse. The water retention of gels was related to both molecular interactions and secondary structures of protein as well as the microstructure of the gels.

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