Haizhou Dong
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Haizhou Dong has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
- Fei Zhao
Shandong Facility Horticulture Bioengineering Research Center, Jia Sixie College of Agriculture, Weifang University of Science and Technology, Weifang 262700, China
2 shared publications - Wentao Wang
College of Food Science and Engineering, Engineering and Technology Center for Grain Processing of Shandong Province, Shandong Agricultural University, Tai'an, Shandong Province, 271018, China
2 shared publications - Xuemei Liu
Jinan Fruit Research Institute, All China Federation of Supply & Marketing Co-operatives, Jinan 250014, China
2 shared publications - Daofang Zhang
College of Food Science and Engineering, Shandong Agricultural University, Taian 271018, China
1 shared publication - Fei Zhao
Shandong Engineering Laboratory for Clean Utilization of Chemical Resources, Weifang University of Science and Technology, Weifang 262700, China
1 shared publication - Guoting Liang
College of Agronomy and Environment, Shandong Facility Horticulture Bioengineering Research Center, Weifang University of Science and Technology, Weifang 262700, China
1 shared publication
Latest Publications
- Open Access
Effects of High-Intensity Ultrasound Pretreatment on Structure, Properties, and Enzymolysis of Walnut Protein Isolate
The purpose of this paper was to investigate the effect of high-intensity ultrasonication (HIU) pretreatment before enzymolysis on structural conformations of walnut protein isolate (WPI) and antioxidant activity of its hydrolysates. Aqueous WPI suspensions were subjected to ultrasonic processing at different power levels (600–2000 W) and times (5–30 min), and then changes in the particle size, zeta (ζ) potential, and structure of WPI were investigated, and antioxidant activity of its hydrolysates was determined. The particle size of the particles of aqueous WPI suspensions was decreased after ultrasound, indicating that sonication destroyed protein aggregates. The ζ-potential values of a protein solution significantly changed after sonication, demonstrating that the original dense structure of the protein was destroyed. Fourier transform infrared spectroscopy indicated a change in the secondary structure of WPI after sonication, with a decrease in β-turn and an increase in α-helix, β-sheet, and random coil content. Two absorption peaks of WPI were generated, and the fluorescence emission intensity of the proteins decreased after ultrasonic treatment, indicating that the changes in protein tertiary structure occurred. Moreover, the degree of hydrolysis and the antioxidant activity of the WPI hydrolysates increased after sonication. These results suggest that HIU pretreatment is a potential tool for improving the functional properties of walnut proteins.
Open AccessEffects of High-Intensity Ultrasound Pretreatment on Structure, Properties, and Enzymolysis of Walnut Protein Isolate
The purpose of this paper was to investigate the effect of high-intensity ultrasonication (HIU) pretreatment before enzymolysis on structural conformations of walnut protein isolate (WPI) and antioxidant activity of its hydrolysates. Aqueous WPI suspensions were subjected to ultrasonic processing at different power levels (600–2000 W) and times (5–30 min), and then changes in the particle size, zeta (ζ) potential, and structure of WPI were investigated, and antioxidant activity of its hydrolysates was determined. The particle size of the particles of aqueous WPI suspensions was decreased after ultrasound, indicating that sonication destroyed protein aggregates. The ζ-potential values of a protein solution significantly changed after sonication, demonstrating that the original dense structure of the protein was destroyed. Fourier transform infrared spectroscopy indicated a change in the secondary structure of WPI after sonication, with a decrease in β-turn and an increase in α-helix, β-sheet, and random coil content. Two absorption peaks of WPI were generated, and the fluorescence emission intensity of the proteins decreased after ultrasonic treatment, indicating that the changes in protein tertiary structure occurred. Moreover, the degree of hydrolysis and the antioxidant activity of the WPI hydrolysates increased after sonication. These results suggest that HIU pretreatment is a potential tool for improving the functional properties of walnut proteins.
- Open Access
Effects of High-Intensity Ultrasound Pretreatment on Structure, Properties, and Enzymolysis of Soy Protein Isolate
The objective of this study was to investigate the effects of different high-intensity ultrasonication (HIU) pretreatment on the structure and properties of soybean protein isolate (SPI) as well as enzymatic hydrolysis of SPI by bromelain and antioxidant activity of hydrolysates. The HIU-treated SPI fractions showed a decrease in the proportion of α-helices and β-turns and an increase in the content of β-sheets and random coils based on Fourier-transform infrared spectroscopy. Near-infrared spectra and fluorescence spectra analyses provided support for the changes in secondary and tertiary structures of SPI after ultrasound treatment. The particle size of SPI decreased from 217.20 nm to 141.23 nm and the absolute zeta potential increased. Scanning electron microscopy showed that HIU treatment changed apparent morphology. Dynamic and static light scattering of ultrasonicated samples showed that SPI structure had changed from hard-sphere to hollow-sphere or polydisperse and monodisperse gaussian coils. HIU pretreatment significantly increased the hydroxyl-radical scavenging and the degree of hydrolysis of the SPI hydrolysates.
Open AccessEffects of High-Intensity Ultrasound Pretreatment on Structure, Properties, and Enzymolysis of Soy Protein Isolate
The objective of this study was to investigate the effects of different high-intensity ultrasonication (HIU) pretreatment on the structure and properties of soybean protein isolate (SPI) as well as enzymatic hydrolysis of SPI by bromelain and antioxidant activity of hydrolysates. The HIU-treated SPI fractions showed a decrease in the proportion of α-helices and β-turns and an increase in the content of β-sheets and random coils based on Fourier-transform infrared spectroscopy. Near-infrared spectra and fluorescence spectra analyses provided support for the changes in secondary and tertiary structures of SPI after ultrasound treatment. The particle size of SPI decreased from 217.20 nm to 141.23 nm and the absolute zeta potential increased. Scanning electron microscopy showed that HIU treatment changed apparent morphology. Dynamic and static light scattering of ultrasonicated samples showed that SPI structure had changed from hard-sphere to hollow-sphere or polydisperse and monodisperse gaussian coils. HIU pretreatment significantly increased the hydroxyl-radical scavenging and the degree of hydrolysis of the SPI hydrolysates.
- Open Access
High-Pressure Homogenization Pretreatment before Enzymolysis of Soy Protein Isolate: the Effect of Pressure Level on Aggregation and Structural Conformations of the Protein
The high-pressure homogenization (HPH) treatment of soybean protein isolate (SPI) before enzymatic hydrolysis using bromelain was investigated. Homogenization pressure and cycle effects were evaluated on the enzymatic degree of hydrolysis and the antioxidant activity of the hydrolysates generated. The antioxidant activity of SPI hydrolysates was analyzed by 1,1-dipheny-2-picrylhydrazyl (DPPH). The sizes and structures of the SPI-soluble aggregate after HPH treatment were analyzed using dynamic and static laser light scattering. The changes in the secondary structure, as measured by Fourier transform infrared spectroscopy (FTIR) and the macromorphology of SPI, were measured by scanning electron microscope (SEM). These results suggested that the HPH treatment (66.65%) could increase the antioxidant activities of the SPI hydrolysates compared with the control (54.18%). SPI hydrolysates treated at 20 MPa for four cycles obtained higher DPPH radical-scavenging activity than other samples. The control was predicted to be a hard sphere, and SPI treatment at 10 MPa was speculated to be Gaussian coil, polydisperse, and then the high-pressure treated SPI became a hollow sphere. Changes in the secondary structures showed protein aggregate formation and rearrangements. The image of SPI varied from a globular to a clump structure, as observed by the SEM. In conclusion, combining HPH treatment and enzymolysis could be an effective way to improve the antioxidant activity of the SPI.
Open AccessHigh-Pressure Homogenization Pretreatment before Enzymolysis of Soy Protein Isolate: the Effect of Pressure Level on Aggregation and Structural Conformations of the Protein
The high-pressure homogenization (HPH) treatment of soybean protein isolate (SPI) before enzymatic hydrolysis using bromelain was investigated. Homogenization pressure and cycle effects were evaluated on the enzymatic degree of hydrolysis and the antioxidant activity of the hydrolysates generated. The antioxidant activity of SPI hydrolysates was analyzed by 1,1-dipheny-2-picrylhydrazyl (DPPH). The sizes and structures of the SPI-soluble aggregate after HPH treatment were analyzed using dynamic and static laser light scattering. The changes in the secondary structure, as measured by Fourier transform infrared spectroscopy (FTIR) and the macromorphology of SPI, were measured by scanning electron microscope (SEM). These results suggested that the HPH treatment (66.65%) could increase the antioxidant activities of the SPI hydrolysates compared with the control (54.18%). SPI hydrolysates treated at 20 MPa for four cycles obtained higher DPPH radical-scavenging activity than other samples. The control was predicted to be a hard sphere, and SPI treatment at 10 MPa was speculated to be Gaussian coil, polydisperse, and then the high-pressure treated SPI became a hollow sphere. Changes in the secondary structures showed protein aggregate formation and rearrangements. The image of SPI varied from a globular to a clump structure, as observed by the SEM. In conclusion, combining HPH treatment and enzymolysis could be an effective way to improve the antioxidant activity of the SPI.