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Tang X.,Northeast Agricultural University | Liu Q.,Northeast Agricultural University | Kong B.,Northeast Agricultural University | Han J.,National Soybean Engineering Technology Research Center
Journal of Chinese Institute of Food Science and Technology | Year: 2016

This study mainly investigated physicochemical properties and digestion kinetics of gelatinized, retrograded, resistant starch prepared from maize, high-amylose maize starch through autoclaving-cooling treatment. The results revealed that the gelatinized starch and retrograded starch samples prepared from maize starch have better solubility, swelling power and freeze-thaw stability than the others (P<0.05), The level of slowly digestible starch (SDS) in retrograded starch prepared from maize starch and high-amylose maize starch were significantly increased (P<0.05), Meanwhile, digestion kinetics analysis showed that equilibrium concentration, hydrolysis index, glycemic index decreased as the resistant starch (RS) content of starch samples increased. SDS could be slowly release the energy, however, not affect equilibrium concentrations. The results indicate that the autoclaving-cooling treatment can significantly change the physicochemical properties of starch, and the retrograded, RS could be widely used as fat mimetics. © 2016, Chinese Institute of Food Science and Technology. All right reserved. Source


Liu Q.,Northeast Agricultural University | Chen Q.,Northeast Agricultural University | Kong B.,Northeast Agricultural University | Han J.,Northeast Agricultural University | And 2 more authors.
LWT - Food Science and Technology | Year: 2014

The objective of the present study was to investigate the effects of superchilling combined with cryoprotectants (a mixture of sucrose and sorbitol, 1:1) on protein oxidation and structural changes in common carp (Cyprinus carpio) surimi. With increasing storage time, the carbonyl content of myofibrillar proteins increased from 31.4nmol/mg of protein (0 day) to 53.4, 46.3, and 39.7nmol/mg protein at 35 days (P<0.05) for-1°C superchilled,-3°C superchilled, and-3°C superchilled with cryoprotectants samples, respectively. The incorporation of cryoprotectants into common carp surimi was found to significantly inhibit the formation of carbonyls (P<0.05). The protein surface hydrophobicity increased in a similar direction, and the sulfhydryl content and Ca-ATPase stability decreased (P<0.05). Emulsifying activities, gel textural hardness, springiness, and water binding capacity were also decreased, but they exhibited significant improvements at-3°C when combined with cryoprotectants (P<0.05). These results suggest that superchilling treatments at-3°C combined with cryoprotectants offer an effective approach to reducing protein oxidation in carp surimi, thereby reducing protein structural changes known to impair the texture of surimi products. © 2014 Elsevier Ltd. Source


Liu Q.,Northeast Agricultural University | Kong B.,Northeast Agricultural University | Han J.,Northeast Agricultural University | Han J.,National Soybean Engineering Technology Research Center | And 2 more authors.
LWT - Food Science and Technology | Year: 2014

The objective of the present study was to investigate the effect of superchilling with cryoprotectants (a mixture of sucrose and sorbitol) on microbial growth, lipid oxidation, and proteolytic degradation in common carp (Cyprinus carpio) surimi. With increasing storage time, the microbial count of surimi increased from 4.4 log10CFU/g (0 days) to 7.2, 6.2, 5.9, and 5.5 log10CFU/g (35 days; P<0.05) in the samples superchilled at-1°C, superchilled at-3°C, superchilled at-3°C with cryoprotectants, and frozen at-18°C, respectively. The total volatile basic nitrogen and thiobarbituric acid-reactive substances exhibited an increasing trend (P<0.05) similar to that obtained with the microbial growth, whereas the whiteness and lightness stability decreased (P<0.05) with increasing storage time. The SDS-PAGE analysis revealed that the degree of protein degradation increased with increasing storage time. Compared with the sample frozen at-18°C, superchilling at-1°C and-3°C resulted in a marked reduction in the microstructure deterioration of the myofibrillar protein gels, and the addition of cryoprotectants further reduced this deterioration. These results suggest that superchilling with cryoprotectants offers an effective approach for reducing microbial growth and lipid oxidation and limiting proteolytic degradation in common carp surimi. © 2014 Elsevier Ltd. Source


Liu Q.,Northeast Agricultural University | Niu H.,Northeast Agricultural University | Zhao J.,Northeast Agricultural University | Han J.,Northeast Agricultural University | And 2 more authors.
International Journal of Food Properties | Year: 2016

The chemical characteristics and antioxidant properties of Maillard reaction products formed in the Maillard reaction in a model system at 95°C for different lengths of time (0-6 h) were investigated at three mass ratios (1:1, 1:2, and 1:3) of porcine plasma protein hydrolysate to galactose. The results revealed that the pH value and free amino group content decreased (p < 0.05), whereas the browning index, intermediate products, and browning intensity, as well as reducing power and 2,2-amino-di(2-ethyl-benzothiazoline sulfonic acid-6)ammonium salt radical scavenging activity of the Maillard reaction products increased as the reaction time increased (p < 0.05). Moreover, when the mass ratio of porcine plasma protein hydrolysate to galactose was 1:3, the Maillard reaction progressed easily, which rendered a higher degree of glycation and antioxidant activity (p < 0.05). These results indicated that the Maillard reaction can improve the antioxidant capacity of porcine plasma protein hydrolysate. © 2015 Taylor and Francis Group, LLC. Source


Lu Y.,Northeast Agricultural University | Liu Q.,Northeast Agricultural University | Geng R.,Northeast Agricultural University | Kong B.,Northeast Agricultural University | And 3 more authors.
Journal of Chinese Institute of Food Science and Technology | Year: 2015

This study mainly investigated the changes of structural properties induced by hydroxyl radical-stressed soybean protein isolate (SPI). SPI was exposed to a hydroxyl radical-generating system (HRGS) under different H2O2 concentrations (0.1-15 mmol/L) for 1 h. The results revealed that the total sulfhydryl and reactive sulfhydryl content decreased as the H2O2 concentration increased (P>0.05), while tryptophan fluorescent emission spectrum was observed blue-shift and UV-Vis spectra was observed blue-shift after the first red-shift. The SDS-PAGE patterns showed that protein oxidation caused protein aggregation by non-disulphides linkage between proteins. These results showed that structural characteristics of SPI were changed via protein oxidation. © 2015, Chinese Institute of Food Science and Technology. All right reserved. Source

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