LWT-FOOD SCIENCE AND TECHNOLOGY
·
2021
·
IF 4.952
Kefei Chang,Jingbo Liu,Wei Jiang,Yong Fan,Bo Nan,Sitong Ma,Yan Zhang,Boqun Liu,Ting Zhang
In this study, we investigated the effects of different caffeic acid (CA) concentrations on the ovalbumin structure and foaming properties. When the concentration of CA was 0.18 mg/mL, the surface hydrophobicity of ovalbumin decreased from 705.37 to 542.79, the sulfhydryl content decreased from 4.15 μmol/g to 2.26 μmol/g, and the foaming ability and stability increased by 72% and 71%, respectively. We observed that hydrophobic interactions represented the main binding force between CA and ovalbumin. Using circular dichroism spectroscopy (α-Helix increased from 7.2% to 13.9%) and endogenous fluorescence spectra (Reduction of fluorescence intensity and redshift), it showed that CA affected the secondary and tertiary ovalbumin structure, thus increasing the flexible structure. The increase in particle size Increased from 10.26 nm to 65.97 nm indicated that CA acted as a crosslinking agent between the ovalbumin molecules and increased the viscosity of the system through hydrophobic interactions. Although the increase in ovalbumin aggregation and the decrease in hydrophobicity were not conducive to the foaming properties of ovalbumin solutions, the increase in solubility, absolute potential, and flexible molecular structure contributed to the improvement of the foaming properties. All results showed that CA could improve the foaming properties of ovalbumin, a potential food-grade foaming agent.
研究领域:
食品科学
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生物化学
·
胶体科学
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产品关联
DOI
高影响因子
Food and Bioprocess Technology
·
2016
·Vol. 10
·期 2
·370-378
·
IF 2.574
Jiang Wenxin,He Yufan,Xiong Shanbai,Liu Youming,Yin Tao,Hu Yang,You Juan
To produce high-quality surimi, we investigated the effect of ozone-induced mild oxidation on structural changes of silver carp myosin by analyzing circular dichroism (CD), intrinsic fluorescence, the sulfhydryl group, surface hydrophobicity, SDS-PAGE, and dynamic light scattering (DLS) of myosin. Mild ozone oxidation of myosin was performed by applying gaseous ozone for a short time. Results showed that the content of sulfhydryl group decreased, and carbonyl content and surface hydrophobicity increased with an increase in ozone treatment time. A red shift in the maximum wavelength of intrinsic fluorescence indicated the unfolding of oxidized myosin. Further conformational change of myosin was illustrated by CD; α-helical content decreased significantly and β-turn, β-sheet, and random coil content increased with increased ozone treatment time, which demonstrated the rearrangement of β-structure in myosin. The results from DLS and SDS-PAGE indicated that soluble oligomers or aggregates were formed by disulfide bonds under mild ozone treatment. Therefore, ozone-induced mild oxidation did not strongly alter myosin structure but promoted myosin partial unfolding, which might result in exposing more cross-linking sites for the formation of surimi gel.
研究领域:
食品科学
·
生物化学
·
蛋白质化学
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DOI
高影响因子
Food Science & Nutrition
·
2018
·Vol. 6
·期 4
·1053-1064
·
IF 1.521
Shuang Ma,Xu Yang,Changhui Zhao,Mingruo Guo
Effect of ultrasound treatment on the physicochemical properties and structure of β-lactoglobulin were investigated. β-Lactoglobulin was treated with ultrasound at different amplitudes, temperatures, and durations. The surface hydrophobicity and free sulfhydryl group of β-lactoglobulin were significantly increased after ultrasound treatment ( p < .05). The maximal surface hydrophobicity and free sulfhydryl group were 5,812.08 and 5.97 μmol/g, respectively. Ultrasound treatment changed the physicochemical properties of β-lactoglobulin including particle size (from 1.21 ± 0.05 nm to 1.66 ± 0.03 nm), absolute zeta potential (from 15.47 ± 1.60 mV to 27.63 ± 3.30 mV), and solubility (from 84.66% to 95.17%). Ultrasound treatment increased α-helix and β-sheet structures of β-lactoglobulin. Intrinsic fluorescence intensity of ultrasound-treated β-lactoglobulin was increased with shift of λ max from 334 to 329 nm. UV absorption of β-lactoglobulin was decreased with shift of λ max from 288 to 285 nm after ultrasound treatment. There were no significant changes in high-performance liquid chromatography and protein electrophoretic patterns. These findings indicated that ultrasound treatment had high potential in modifying the physiochemical and structural properties of β-lactoglobulin for industrial applications.
研究领域:
食品科学
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蛋白质化学
·
生物物理学
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产品关联
DOI
PubMed
高影响因子
Food Bioscience
·
2024
·
IF 4.8
Yingyan Li,Lijie Zhu,Yingjie Zhou,He Li,Xinqi Liu,Lei Chen,Guozhen Wang,Qian Shen,Xiuying Liu,Wenping Ding
The bitterness of soyasaponins (Ssa) is one of the main causes of undesirable flavors in soy products. In this study, a Ssa-soybean protein isolate (SPI) binary system was constructed to simulate the adsorption behavior of soybean products at the oral-salivary interface and the mechanism of bitter taste development was investigated. The concentration of Ssa with was determined to be the minimum bitterness value approximately 0.5 mg/mL by sensory evaluation and electronic tongue determination. The nonspecific interactions were confirmed by isothermal titration calorimetry (ITC) and endogenous fluorescence measurements. Ssa formed aggregates with SPI that desorbed from the interface into the bulk phase, resulting in a subsequent increase in particle size and turbidity. This study demonstrated the ability of SPI with Ssa at specific concentrations to attenuate the bitter flavor of Ssa, thus providing important implications for increasing the acceptability of soy products.
研究领域:
食品科学
·
化学感官科学
·
胶体化学
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产品关联
DOI
高影响因子
FOOD HYDROCOLLOIDS
·
2024
·
IF 11
Chang Liu,Ning Wang,Lin Li,Dandan Wu,Liqi Wang,Na Zhang,Dianyu Yu
To investigate the effects of microwave plasma treatment on rice bran protein (RBP), various power levels (150, 160, 170, 180, and 190 W) and processing times (1, 3, 5, 7, and 9 min) were examined for their impact on the conformation, physicochemical properties, and functional properties. The results showed that high-energy active particles generated by microwave plasma could oxidize modify the spatial structure of RBP, thus affecting its functional characteristics. The primary structure of RBP, as revealed by SDS-PAGE, remained unchanged. While the content of β -sheet structures initially decreased and then increased, the random coil content first increased and then decreased, the spatial structure first unfolded and then folded again. The intrinsic fluorescence spectrum showed that hydrophobic amino acids buried within the protein's interior were initially exposed but later reburied. The disulfide bond was first broken to sulfhydryl group and then reformed due to excessive oxidation, which promoted the intermolecular aggregation of RBP. Compared with its natural counterpart, the average particle size decreased from 519.6 nm to 186.7 nm at a power of 160 W and a treatment time of 5 min. Consequently, the emulsification activity index and the stability index increased by factors of 2.18 and 1.40, respectively. The foaming capacity index and foam stability index reached maximum values of 73.07% and 43.34%, respectively. These results provide theoretical evidence for the application of microwave plasma technology to modify plant proteins.
研究领域:
食品科学
·
蛋白质化学
·
生物技术
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产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2023
·
IF 8.2
Xinghui Wu,Lina Yang,Mingjie Xia,Kejin Yu,Wenqi Cai,Taiyuan Shi,Mengxi Xie,He Liu
The stable energy barrier of mucin and soy hull polysaccharide (SHP) is established at the air/water interface in the intestinal fluid and is conducive to the absorption and transportation of nutrients. This study aimed to investigate the effect of different concentrations (0.5 % and 1.5 %) of Na + and K + on the energy barrier through the digestive system model in vitro . The interaction between ions and microwave-assisted ammonium oxalate-extracted SP (MASP)/mucus was characterized by particle size, zeta potential, interfacial tension, surface hydrophobicity, Fourier transform infrared spectroscopy, endogenous fluorescence spectroscopy, microstructure, and shear rheology. The results showed that the interactions between ions and MASP/mucus included electrostatic interaction, hydrophobic interaction, and hydrogen bond. The MASP/mucus miscible system was destabilized after 12 h, and the ions could improve the system stability to some extent. MASP aggregated continuously with the increase in the ion concentration, and large MASP aggregates were trapped above the mucus layer. Furthermore, the adsorption of MASP/mucus at the interface increased and then decreased. These findings provided a theoretical basis for an in-depth understanding of the mechanism of action of MASP in the intestine.
研究领域:
食品科学
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营养学
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生物物理学
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产品关联
DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2022
·
IF 8.025
Linlin Wang,Lilong Wang,Chengrong Wen,Nan Wang,Chunhong Yan,Caihong Shen,Shuang Song
Chitosan (CTS)/chitosan oligosaccharide (COS) and whey protein isolate (WPI) have been frequently used as food supplements, but notably, the interaction between the carbohydrate and the protein may affect the digestibility of protein. Thus, the present study focused on effects of the interaction between CTS/COS and WPI on the protein digestibility. A series of chemical and spectroscopic techniques including gel electrophoresis, gel permeation chromatography, Fourier transform-infrared (FT-IR) spectroscopy, intrinsic fluorescence (IF) spectroscopy, and circular dichroism (CD) spectroscopy were applied. According to the findings, both CTS and COS dramatically reduced intestinal digestibility of WPI, resulting in a decrease of DH by 43.33 % and 52.31 %, respectively. The substitution degree of WPI on CTS was 0.87 g WPI/g CTS, and the electrostatic interaction between amine groups of CTS and carboxyl groups of WPI caused changes in WPI's stability, microstructure, and fluorescence intensity. Notably, CTS affected the digestibility of WPI by precipitating protein and enzyme, whereas COS altered WPI's digestibility by decreasing or inactivating enzyme activity. The present study offered a solid scientific foundation for the rational formulations of carbohydrates and proteins in food industry.
研究领域:
食品科学
·
营养学
·
生物物理学
·
化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Innovative Food Science & Emerging Technologies
·
2025
·
IF 6.8
Xiaopeng Wei,Ziyan Zhou,Xiaoyuan Wang,Megan Povey,Guo Liu,Shanshan Zhang,Ping Geng,Lihua Zhang,Zhenzhen Ge
To break through the limitation of technological functionalities of chickpea protein isolate (CPI) in food processing conditions (e. g. high temperature and pH variations) and broaden CPI application, glycosylation modification was used to improve the structural and functional properties of CPI. Herein, ozone treatment was utilized to unfold CPI structure for promoting the Maillard reaction between CPI and arabinose (Ara). Then the influence of glycosylation modification on the structural and functional properties of CPI was investigated, and the stability of oil-in-water (O/W) emulsions loaded with β-carotene prepared with glycosylated products was evaluated. Compared to CPI, CPI pretreatment with ozone (CPI/O 3 ) conjugated with Ara efficiently, with a (CPI/O 3 )/Ara mass ratio of 1:2, the degree of graft reached 25.3 %, suggesting the successful covalent binding of Ara to the protein. Fourier transform infrared spectroscopy (FTIR), intrinsic fluorescence spectroscopy and surface hydrophobicity analyses demonstrated that glycosylation could alter secondary and tertiary structure of CPI. Notably, the glycosylation significantly improved solubility, oil holding capacity, emulsifying properties and interfacial characteristics. Moreover, emulsions prepared with CPI/O 3 -Ara conjugates, especially CPI/O 3 -Ara 1:2 conjugate, showed a higher encapsulation efficiency for β-carotene, smaller droplet size, stronger ζ-potential and lower turbiscan stability index compared to emulsions made with CPI, displaying excellent stability under heating treatment and pH variation. Collectively, the results revealed that the ozone-assisted glycosylation is an efficient approach for the improvement of the functional and interfacial properties of CPI.
研究领域:
食品科学与技术
·
蛋白质化学
·
胶体与界面科学
·
功能食品
·
纳米载体递送系统
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产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2021
·
IF 6.953
Yiming Zhou,Qingyi Jiang,Sijia Ma,Xiaoli Zhou
Tartary buckwheat is one of the few pseudocereals with abundant flavonoids and starch. However, there are different views on the digestibility of Tartary buckwheat starch (TBS) because of its particle size and structure. In this study, fluorescence spectrum methods and enzymatic kinetics were used to investigate the interaction between TBS /two glycosidase (α-amylase and α-glucosidase) and quercetin to explore its digestive properties and provide a perspective regarding the application of TBS in functional starch products. The results showed that the interaction between TBS and quercetin was probably weak hydrophobic force and hydrogen bonding. The inhibitory effect of quercetin on α-amylase was better than that on α-glucosidase. The half inhibitory concentrations (IC 50 ) of quercetin to α-amylase and α- glucosidase was (270 ± 3.31) and (544 ± 9.01) μg/mL, respectively. The intrinsic fluorescence of two enzymes was statically quenched by forming a complex with quercetin. Quercetin also increased the microenvironment hydrophilicity of tryptophan residues in glycosidase. In vitro digestion experiment demonstrated that quercetin and TBS co-gelatinized together was more effective to inhibit TBS hydrolysis than quercetin itself alone. In the first-order kinetic and LOS model, quercetin-starch gel structure and quercetin inhibitory activity against enzymes had synergistic effects of the TBS digestion.
研究领域:
食品科学
·
营养学
·
生物化学
·
药理学
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产品关联
DOI
PubMed
高影响因子
JOURNAL OF CEREAL SCIENCE
·
2021
·
IF 3.616
Lanlan Wu,Jianhua Li,Weijing Wu,Libo Wang,Fei Qin,Wen Xie
The tartary buckwheat protein isolates (TBPIs) were extracted by different pH combined with isoelectric precipitation. The impacts of extraction pH on Osborne-type protein fractions, functional properties, structural properties, and in vitro gastrointestinal digestion were investigated. The result showed that alkaline extraction was effective to increase yield of TBPI. With increase of extraction pH, the content of albumin in TBPI gradually decreased, while content of glutenin was increased. The solubility of TBPIs extracted by pH above 12 were significantly decreased while emulsion stability was significantly increased, which was related to significant increase of surface hydrophobicity. The digestive rate of TBPIs of pH 7 and 8 were high. With increase of pH from 8 to 10, digestive rate of TBPIs decreased. It was related to the compact structure of TBPIs, which had higher α-helix content, higher disulfide bonds , and lower intrinsic fluorescence intensity. Continuous increase of pH increased digestive rate of TBPIs. It was associated with unfolded and denatured structure of TBPIs (pH ≥ 12), as evidenced by breakdown of disulfide bonds, lower α-helix structure, red-shift in intrinsic fluorescence, and dissociation of subunits. Overall, extraction pH during protein extraction has great impacts on TPBIs.
研究领域:
食品科学
·
蛋白质化学
·
营养学
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2020
·
IF 4.192
Jianhua Yi,Manyan Qiu,Ning Liu,Li Tian,Xinpeng Zhu,Eric Andrew Decker,David Julian McClements
The food industry is exploring the natural environment to identify botanical extracts that can be used as functional ingredients that can replace synthetic ingredients in foods. In the present study, the ability of black rice anthocyanins as natural antioxidants to inhibit both lipid and protein oxidation in protein-stabilized oil-in-water emulsions was examined. Whey-protein-stabilized emulsions were prepared containing 0, 0.02, 0.04, and 0.06% (w/v) anthocyanins, and then the impact of this plant-based extract on their physical and chemical stabilities was evaluated. The addition of the anthocyanins improved the physical stability of the emulsions in a dose-dependent manner by inhibiting droplet aggregation during storage (35 °C for 5 days). The anthocyanins also exhibited good antioxidant activity in a dose-dependent manner, as seen by their capacity for inhibiting both lipid oxidation (reduced lipid hydroperoxides and malondialdehyde) and protein oxidation (reduced carbonyl and Schiff base formation, intrinsic fluorescence loss, and molecular weight changes). Black rice anthocyanins may therefore be an effective botanical extract for improving the stability of protein-stabilized food emulsions by inhibiting oxidative reactions.
研究领域:
食品科学
·
营养学
·
化学
·
生物技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2018
·
IF 4.946
Minjie Cao,Ailing Cao,Jing Wang,Luyun Cai,Joe Regenstein,Yunjie Ruan,Xiuxia Li
In order to evaluate the effects of magnetic nanoparticles plus microwave (MNPMT) or far-infrared (MNPFT) thawing on protein conformation changes and moisture migration of red seabream ( Pagrus major ) fillets, cold storage thawing, microwave thawing, MNPMT, far-infrared thawing and MNPFT were subjected to red seabream fillets. DSC and dynamic rheology were conducted to analyze physicochemical changes. Raman spectra before and after isotope H/D exchange, intrinsic fluorescence and UV second derivative spectra were carried out to explore myofibrillar protein structural changes. Low-field NMR was used to test water migration. SEM was performed to observe fiber microstructure. Results indicated that MNPMT and MNPFT both had a desirable thermal stability and gelation property. Besides, both showed stable protein secondary and tertiary structure. Immobilized water in them also had no significant changes compared with fresh sample. This research provided some novel thawing technologies for application in food industry.
研究领域:
食品科学
·
生物物理学
·
化学工程
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）