INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Zhiyu Xiong,Xiangdai Wang,Ying Tian,Xin Wang,Li Yuan,Wengang Jin,Jianrong Li,Ruichang Gao
The effects of ethanol, 1,2-propanediol, and glycerol at concentrations from 10 % to 40 % on the thermal denaturation and aggregation of silver carp ( Hypophthalmichthys molitrix ) myosin were investigated. The results revealed that ethanol and 1,2-propanediol induced thermal denaturation of myosin more rapidly than glycerol, which minimally impacted the secondary structure. At 10 % concentration, 1,2-propanediol significantly influenced myosin's secondary structure more than ethanol. While at a concentration of 20 %, ethanol prompted faster thermal denaturation and aggregation, resulting in higher turbidity than 1,2-propanediol ( P < 0.05). Notably, higher concentrations of ethanol (30 % and 40 %) and 1,2-propanediol (40 %) induced the formation of non-disulfide covalent bonds, contributing to excessive myosin aggregation. Furthermore, hydrophobic interactions emerged as crucial within myosin aggregation in glycerol solutions during heating. Additionally, the effects of three alcohols at 1 %, 3 %, and 5 % on the gel properties were investigated. The results showed that an appropriate concentration of 1,2-propanediol (3 %) and glycerol (5 %) significantly enhanced the gel properties by inducing desirable unfolding and aggregation of myosin molecules. These findings offer a theoretical foundation for utilizing alcohol additives to enhance the gel quality of heat-induced surimi.
研究领域:
食品科学
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蛋白质化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY
·
2018
·Vol. 18
·期 8
·5542-5550
·
IF 1.354
Cai Chengxu,Wang Mingzhe,Wang Liming,Wang Bing,Feng Weiyue,Chen Chunying
Characterization of bio-nano interface is crucial for developing safer and more efficient nanoparticles in nanomedical application. PEGylation is commonly used in nanocarrier for drug delivery, as it confers nanoparticles good stability, stealth effect and better targeting specificity
compared with those without PEGylation. However, the protein binding state on PEGylated AuNP is still limited known. In present work, we prepared 13 nm AuNPs and then PEGylated them with thiol PEG methoxy. Lysozyme is selected as a model protein and to investigate the interactions on protein-PEGylated/AuNP
interface. The thermal unfolding processes of lysozyme in absence and presence of PEGylated AuNP were measured by synchrotron radiation based circular dichroism (SRCD), dynamic light scattering (DLS) and infrared spectroscopy (IR). The results suggest that in terms of secondary structural
changes, α helix content is decreased, while β sheet content is increased, and thus the adsorbed lysozyme may be present in PEG layer.
研究领域:
生物化学
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纳米医学
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材料科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF LUMINESCENCE
·
2022
·
IF 4.171
Shiyu Xiao,Shian Xie,Manbo Zhang,Shengmin Hu,Marc Adape,Jian Wang,Xinhui Zhang,Yongqin Wei,Wei Chen
Here we report two luminescent copper complexes with different structures and luminescent properties, the blue-green [CuI(dmpyHS) (PPh 3 ) 2 ]⸱CH 3 CN (CuPy-PPh 3 ) and the red [Cu 6 (dmpyS) 6 ]⸱H 2 O (CuPy). When the blue-green light (CuPy-PPh 3 ) is heated to above 147 °C, it loses the phosphine-containing ligand, PPh 3 , and turns into CuPy and instead emits red light. Many luminescent complexes show the change of luminescence properties when the temperature is lower than room temperature , while the luminescence change of CuPy-PPh 3 occurs during the heating process above room temperature. Even more interesting, the luminescence wavelength transition span is large, from blue-green light emission at 490 nm to red light at 676 nm. The luminescence of the two copper complexes covers the three primary colors of red, green and blue required for the formation of white light emitting diodes WLEDs, which has potential in the development of non-rare earth phosphor white color displays. The integration of CuPy-PPh 3 and CuPy on a 395 nm near-ultraviolet chip can assemble WLEDs with good white light properties, which provides a new way for the construction of rare earth-free phosphor WLEDs. The synthesis of the two luminescent copper complexes is simple and environmentally friendly. Even though the structures of two copper complexes have been reported, the synthesis methods are different from those in the related literature and the luminescence properties of these complexes have never been described previously. The red emission copper complex CuPy is obtained by the thermal conversion of the blue-green emission copper complex CuPy-PPh 3 , which is a new phenomenon discovered for the first time in this work.
研究领域:
材料科学
·
光学
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2014
·
IF 3.107
Nannan Chen,Lianzhu Lin,Weizheng Sun,Mouming Zhao
In this study, we examined the possibility of preparing stable soy protein nanogels by simply heating homogeneous soy protein dispersion. The protein nanogels formed were characterized by z-average hydrodynamic diameter, polydispersity index, turbidity, ζ-potential, morphology, and their stability to pH and ionic strength change. Soy protein dispersion (1% w/v) was homogeneous around pH 5.9 where it had the lowest polydispersity index (∼0.1). Stable and spherical nanogels were formed by heating soy protein dispersion at pH 5.9 under 95 °C. They sustained constantly low polydispersity index (∼0.1) in the investigated pH range of 6.06–7.0 and 2.6–3.0. The nanogels were pH-sensitive and would swell with pH change. They were stable at 0–200 mM NaCl concentration. Denaturation of soy glycinin was the prerequisite for the formation of stable nanogels. Soy protein nanogels had a core–shell structure with basic polypeptides and β subunits interacting together as the hydrophobic core; and acid polypeptides, α′, and α subunits locating outside the core as hydrophilic shell. The inner structure of soy protein nanogels was mainly stabilized by disulfide bonds cross-linked network and hydrophobic interaction. Soy protein nanogels made in this study would be useful as functional ingredients in biotechnological, pharmaceutical, and food industries.
研究领域:
食品科学
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生物材料学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF PHYSICAL CHEMISTRY B
·
2015
·
IF 3.302
Sha Wu,Yanwei Ding,Guangzhao Zhang
Folding and aggregation of proteins profoundly influence their functions. We have investigated the effects of thermal history, concentration and pH on the denaturation and refolding of lysozyme by using ultrasensitive differential scanning calorimetry (US-DSC) and sedimentation velocity (SV) via analytical ultracentrifugation (AUC). The former is sensitive to small energy change whereas the latter can differentiate the oligomers such as dimer and trimer from individual protein molecules. Our studies reveal that the degree of denaturation irreversibility increases as heating times increases. The denaturation temperature (Td) and enthalpy change (ΔH) are influenced by heating rate since the denaturation is not in equilibrium during the heating. We can obtain Td and ΔH in equilibrium by extrapolation of heating rate to zero. In a dilute solution, no aggregation but unfolding happens in the denaturation. However, when the concentration is above a critical value (∼15.0 mg/mL), lysozyme molecules readily form trimers or other oligomers. Lysozyme molecules unfold into stretched chains at pH > 6.0, which would further forms large aggregates. The formation of aggregates makes the refolding of lysozyme impossible.
研究领域:
生物化学
·
蛋白质科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2025
·
IF 6.2
Yue Liu,Kangyu Wang,Ke Bi,Lina Xu,Prince Chisoro,Fei Pan,Ping Yang,Chunhui Zhang,Imre Blank
This study investigated the mechanism of odor release in meat proteins, using stewed chicken as a model. The aim was to substantiate to which extent odor release rates (ORR) depend on structural features of odorants. 52 odor-active compounds were screened following the molecular sensory science approach. Machine learning methods were trained with 14 key molecular descriptors to find correlation between ORR and the molecular structure of odorants. Molecular dynamics simulations were used to investigate the interaction between 18 odorants having odor activity values (OAV) ≥ 1 and heat-denatured myosin (HDM). The ORR is determined by the binding between odor molecules and HDM, with hydrophobic interactions acting as the primary driving force. These findings were confirmed by headspace measurements and the use of bond-disrupting agents. For the first time, this study examines the release behavior and structure–activity relationship of odor compounds with food proteins from a molecular structure perspective.
研究领域:
食品科学
·
分子生物学
✓ 已验证
DOI
PubMed
高影响因子
CHEMICAL ENGINEERING JOURNAL
·
2025
·
IF 13.2
Jiawen Li,Qinbo Jiang,Meiyu Chen,Teng Li,Quancai Sun,Ye Peng,Yang Li,Yucheng Zou,Hui Zhang
This study aimed at improving the physical stability of the electrospinning fiber aerogel (EFA) templates and the templated oleogels (EFA-O), and study the effect of hydrophobic treatment on the properties of the templates and oleogels. The protein thermal denaturation and 12-hydroxystearic acid (12-HSA) loading were utilized to hydrophobically modify the electrospun fiber aerogel templates. Both of the two treatments increased the average fiber diameter, and 12-HSA loading made the EFA obtained a stable and lasting hydrophobicity (water contact angle was around 130°). Meanwhile, both hydrophobic treatments improved the stress feedback of EFA, and thermal denaturation could maintain the excellent resilient performance. The oil adsorption and holding capacity of EFA reached 48.77 g/g and 85.73 %, respectively, and the two low-degree hydrophobic methods were combined to prepare compositely treated EFA-O with excellent performances. The hydrophobic EFA framework supported the 3D structure of oleogels, where the fiber diameter could reach 464.01 nm. Thermal denaturation was beneficial to improve the rheological properties, and 12-HSA loading significantly strengthened the texture properties. Hydrophobic treatments could also effectively inhibit the release of free fatty acids (down to 23.84 %) or curcumin (down to 14.19 %) in EFA-O, which was promising for constructing stable controlled-release systems. The combination of the two treatments can achieve complementary modification effects and lead to better physical and chemical properties. This modification method was not only an effective way to strengthen the performances of EFA, but it met the edibility and safety requirements of oleogel preparation.
✓ 已验证
产品关联
DOI
高影响因子
LANGMUIR
·
2024
·
IF 3.7
Frank Peprah Addai,Jiacong Wu,Feng Lin,Xinnan Ma,Juan Han,Yuelin Liu,Yang Zhou,Yun Wang
In this work, a trimetallic (Ni/Co/Zn) organic framework (tMOF), synthesized by a solvothermal method, was calcinated at 400 and 600 °C and the final products were used as a support for lipase immobilization. The material annealed at 400 °C (Ni-Co-Zn@400) had an improved surface area (66.01 m2/g) and pore volume (0.194 cm3/g), which showed the highest enzyme loading capacity (301 mg/g) with a specific activity of 0.196 U/mg, and could protect the enzyme against thermal denaturation at 65 °C. The optimal pH and temperature for the lipase were 8.0 and 45 °C but could tolerate pH levels 7.0–8.0 and temperatures 40–60 °C. Moreover, the immobilized enzyme (Ni-Co-Zn@Lipase, Ni-Co-Zn@400@Lipase, or Ni-Co-Zn@600@Lipase) could be recovered and reused for over seven cycles maintaining 80, 90, and 11% of its original activity and maintained a residual activity >90% after 40 storage days. The remarkable thermostability and storage stability of the immobilized lipase suggest that the rigid structure of the support acted as a protective shield against denaturation, while the improved pH tolerance toward the alkaline range indicates a shift in the ionization state attributed to unequal partitioning of hydroxyl and hydrogen ions within the microenvironment of the active site, suggesting that acidic residues may have been involved in forming an enzyme–support bond. The high enzyme loading capacity, specific activity, encouraging stability, and high recoverability of the tMOF@Lipase indicate that a multimetallic MOF could be a better platform for efficient enzyme immobilization.
研究领域:
生物化学
·
材料科学
·
生物技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
·
2024
·
IF 11
Ya Li,Liwei Mao,Lifeng Wang,Wenfei Xiong
The effects of electrostatic repulsion (pH6.5) and attraction (pH4.6) between biopolymers on the physicochemical and foam properties of ovalbumin (OVA)/carboxymethylcellulose (CMC) mixtures subjected to mild heat treatment (60–75 °C) were comparatively investigated. It was found that electrostatic binding between OVA and CMC at pH 4.6 resulted in an increase in the peak temperature of thermal denaturation (T d ) of OVA from 71.3 °C to 74.4 °C, while no significant effect was observed at pH 6.5. Thus, 60 and 65 °C below T d were chosen to further investigate the effects of heating on the degree of thermal aggregation, protein conformation and foam properties of OVA/CMC mixtures. Confocal laser scanning microscopy observations and rheological results indicated that electrostatic binding between OVA and CMC at pH 4.6 significantly reduced the degree of protein thermal aggregation, while on the contrary, electrostatic repulsion between proteins and polysaccharides at pH 6.5 promoted OVA thermal aggregation. Raman spectroscopic characterisation indicated that mild heat treatment mainly led to a change in the microenvironment polarity of OVA tyrosine and tryptophan residues, as well as an increase in the content of random coil in the amide III band irrespective of pH. Moreover, after heating at 65 °C for 20 min, The foaming ability of the OVA/CMC mixtures at pH 6.5 and 4.6 increased by approximately 32% and 36% respectively compared to pure OVA. These findings have a positive value for enhancing the heat sterilisation strength of egg white proteins.
研究领域:
食品科学
·
物理化学
·
胶体科学
✓ 已验证
产品关联
DOI
高影响因子
ACS Sensors
·
2023
·
IF 8.9
Peng Yan,Xuewei Zheng,Shuang Liu,Yanhua Dong,Tao Fu,Zhongmin Tian,Yayan Wu
Rapid and efficient detection and identification of proteins hold great promise in medical diagnostics, treatment of different diseases, and proteomics. Here, we present a simple colorimetric sensor array for the differentiation of proteins in various osmolyte solutions. Osmolytes have different influences on the conformation of proteins, which have differential binding to silver nanoparticles, resulting in color changes. The sensor array shows unique color change patterns for each of the 19 proteins, allowing unambiguous identification. Very interestingly, the differentiation of 19 proteins is related to their molecular weight. Moreover, the sensor array can be used to identify protein mixtures, thermal denaturized proteins, and unknown protein samples. Finally, the sensor array can also analyze the plasma or liver samples of the four groups of salt-sensitive rats fed with different diets, indicating that it has the potential for the classification of metabolic profiles.
研究领域:
医学诊断
·
蛋白质组学
·
分析化学
·
生物化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
·
2020
·
IF 7.053
Lechuan Wang,Xun Liang,Yang Chen,Baomiao Ding,Weiqing Sun,Zhenshun Li,Yangchao Luo
Lysozyme (Ly) is an excellent natural preservative to prolong the storage and shelf life of food products . However, its bioactivity is often compromised when it coexists with negatively charged polysaccharides due to their unfavorable electrostatic interactions. In this study, we investigated the influence of carboxymethyl cellulose (CMC) on Ly structure and bioactivity under the different CMC and Ly mass ratios and thermal treatments. The CMC-Ly complexes were characterized by turbidity, protein intrinsic and extrinsic (isothiocyanate labeled) fluorescence, Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopies. The bioactivities of Ly were determined via enzymatic activity and inhibition zone methods. The results showed that their interactions could be modulated by the mass ratios of CMC to Ly. The strongest interactions were found at the mass ratio of 1:5, leading to the significant structural changes and thus the least heating stability of Ly. As a result, its enzymatic and antibacterial activities were restrained at the maximum level at this mass ratio owing to the strongest screening effects on the active sites, aggregation of Ly molecules, altering the spatial structure and neutralizing the surface charges. Notably, further increasing CMC concentration weakened their interactions and thus the complexes dissociated until at the mass ratio of 1:1, which, however, was helpful to recapture the bioactivities of Ly. When the CMC: Ly ratio was higher than 1:1, the bioactivities of Ly were diminished again, possibly due to the steric-hindrance effect of excessive CMC. Thermal denaturation further restrained the enzymatic activities of Ly in CMC-Ly complex. Whereas CMC remained the antibacterial activity of Ly at high temperature heating. In a nut shell, our findings from this work shed some light on the possible mechanistic explanation of negative effects from polysaccharides on the bioactivity of Ly during food processing.
研究领域:
食品科学
·
生物化学
·
生物物理学
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF MOLECULAR LIQUIDS
·
2017
·
IF 3.648
Yuqin Wu,Hongmei Zhang,Yanqing Wang
In the present study, we have investigated the thermal stability of bovine serum albumin (BSA) in the presence of TiO 2 nanoparticles (TiO 2 NPs). The effects of TiO 2 NPs on the transportation function of BSA were also studied by fluorescence spectral method . The circular dichroism (CD) study revealed that addition of TiO 2 NPs moderately decreased the α-Helix content of the protein with the abruptly changing its tertiary structure by hydrogen bonding , van der Waals or electrostatic forces . It has been found that TiO 2 NPs acted as a structure destabilizer for BSA during the thermal denaturation process. The fluorescence quenching and molecular modeling data indicated the existence of strong interaction between BSA and the TiO 2 NPs surface that changed the binding affinities of some ligands for BSA, implying that TiO 2 NPs in blood will affect the transporting ability of serum albumin.
研究领域:
生物物理学
·
纳米技术
·
蛋白质化学
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）