Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters











Database
Publication year range
1.
Int J Biol Macromol ; 253(Pt 4): 127029, 2023 Dec 31.
Article in English | MEDLINE | ID: mdl-37742903

ABSTRACT

Effective separation of lignin macromolecules from the xylose pre-hydrolysates (XPH) during the xylose production, thus optimizing the separation and purification process of xylose, is of great significance for reducing the production costs, achieving the high value-added utilization of lignin and increasing the industrial revenue. In this study, a simple and robust method (pH adjustment) for the separation of lignin from XPH was proposed and systematically compared with the conventional acid-promoted lignin precipitation method. The results showed that the lignin removal ratio (up to 60.34 %) of this simple method was higher than that of the conventional method, and the proposed method eliminated the necessity of heating and specialized equipment, which greatly reduced the separation cost. Meanwhile, this simple method does not destroy the components in XPH (especially xylose), ensuring the yield of the target product. On the other hand, the obtained lignin was nano-scale with less condensed structures, which also possessed small molecular weights with narrow distribution, excellent antioxidant activity (8-14 times higher than commercial antioxidants) and UV protection properties. In conclusion, the proposed simple separation method could effectively separate lignin from XPH at low cost, and the obtained lignin had potential commercial applications, which would further enhance the overall profitability of industrial production.


Subject(s)
Lignin , Xylose , Lignin/chemistry , Xylose/chemistry , Hydrolysis , Alcoholic Beverages
2.
Chem Biol Interact ; 240: 134-44, 2015 Oct 05.
Article in English | MEDLINE | ID: mdl-26282491

ABSTRACT

Ganoderic acids (GAs) produced by Ganoderma lucidum possess anticancer activities with the generation of reactive oxygen species (ROS). However, the role of oxidative stress in apoptotic process induced by GAs is still undefined. In this study, the effects of four structurally related GAs, i.e. GA-T, GA-Mk, and two deacetylated derivatives of GA-T (GA-T1 and GA-T2) on the antioxidant defense system and induced apoptosis in cervical cancer cells HeLa were investigated in vitro. Our results indicated that the tested GAs (5-40 µM) induced apoptotic cell death through mitochondrial membrane potential decrease and activation of caspase-9 and caspase-3. Furthermore, GAs increased the generation of intracellular ROS and attenuated antioxidant defense system by decreasing glutathione (GSH) level, superoxide dismutase (SOD) and glutathione peroxidase (GPX) activities. The above effects were remarkably blocked by the exogenous antioxidants, i.e. N-acetylcysteine, catalase and diphenyleneiodonium chloride. The potency of the four GAs toward induced apoptosis, generation of ROS and suppression of antioxidant defense system was in the order of: GA-T > GA-Mk ≈ GA-T1 > GA-T2 in HeLa cells. These findings suggest that GAs induced mitochondria-dependent cell apoptosis in HeLa cells are mediated via enhancing oxidative stress and depressing antioxidant defense. Additionally, the acetylation of hydroxyl groups in GAs may contribute to their pro-oxidant activities and cytotoxicity, which is helpful to the development of novel chemotherapy agents.


Subject(s)
Apoptosis/drug effects , Oxidative Stress/drug effects , Triterpenes/pharmacology , Antioxidants/chemistry , Antioxidants/metabolism , Female , HeLa Cells , Humans , Molecular Structure , Reactive Oxygen Species , Triterpenes/chemistry , Triterpenes/classification , Uterine Cervical Neoplasms/drug therapy
3.
Langmuir ; 23(6): 3075-83, 2007 Mar 13.
Article in English | MEDLINE | ID: mdl-17269812

ABSTRACT

An aqueous micellar solution of a PEO-PPO-PEO triblock copolymer, pluronic F88 (EO103PO39EO103), in the presence of salt (KCl) has been investigated by 1H NMR spectroscopy. The hydrogen-bonding structure in water is directly changed by the strong polarization effect of added salt, which indirectly weakens the interaction of polymer molecules with water. Both EO and PO blocks are dehydrated by the addition of salt in a similar way, whereas the solubility of the PO blocks may be affected in a more pronounced way, which results in the decrease of the critical micellization temperature (CMT). It is found that the addition of salt favors a more compact micellar core, where the water content is decreased and an effective PO-PO interaction is increased. Increasing the salt concentration would result in a decrease in the number of gauche conformers in the PPO chain, which may be the deeper reason for the decreasing solubility of PPO segments in aqueous salt solution. The temperature region over which the micellization occurs is broad, indicating that micelles and unimers coexist over an extended temperature range, whereas this transition region is significantly narrowed by the addition of salt. The addition of salt offers a good substitute way of changing the temperature to induce micellization. The critical micellization salt concentration (CMSC) is determined to be 1.0 mol l-1 for KCl in 2.5% aqueous pluronic F88 solution at 25 degrees C, and the transition region in which both free and associated copolymer molecules coexist is defined to range from 1 to 2 mol L-1.


Subject(s)
Magnetic Resonance Spectroscopy/methods , Polymers/chemistry , Salts/pharmacology , Chemistry, Physical/methods , Deuterium Oxide , Hydrogen Bonding , Micelles , Molecular Conformation , Potassium Chloride/chemistry , Protons , Solubility , Temperature , Time Factors , Water/chemistry
4.
Langmuir ; 22(23): 9704-11, 2006 Nov 07.
Article in English | MEDLINE | ID: mdl-17073500

ABSTRACT

In this paper we present the effect of poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide) block copolymer micelles and their hydrophobicity on the stabilization of gold nanoparticles. Gold nanoparticles were prepared by a method developed by Sakai et al. (Sakai, T.; Alexandridis, P. Langmuir 2004, 20, 8426). An absorption centered at 300-400 nm in time-dependent UV spectra provided evidence that the very first step of the synthesis was to form primary gold clusters. Then the gold clusters grew in size and were stabilized by block copolymer micelles. The stabilization capacities of the micelles were modulated by tuning the block copolymer concentration and composition and by adding salts. With good stabilization, gold particles were spherical and uniform in size with a diameter of 5-10 nm. Otherwise they were aggregates with irregular shapes such as triangular, hexagonal, and rodlike. The presence of a small amount of NaF significantly increased the stabilization capacity of the micelles and consequently modified the quality of the gold particles. Using FTIR and 1H NMR spectroscopy, micellization of the block copolymers and hydrophobicity of the micelles were proven very important for the stabilization. A higher hydrophobicity of the micelle cores was expected to favor the entrapment of primary gold clusters and the stabilization of gold nanoparticles.


Subject(s)
Gold/chemistry , Hydrophobic and Hydrophilic Interactions , Metal Nanoparticles/chemistry , Metal Nanoparticles/ultrastructure , Micelles , Polyethylene Glycols/chemistry , Propylene Glycols/chemistry , Colloids , Color , Microscopy, Electron, Transmission , Solutions , Spectrophotometry , Temperature
5.
Guang Pu Xue Yu Guang Pu Fen Xi ; 26(9): 1598-600, 2006 Sep.
Article in Chinese | MEDLINE | ID: mdl-17112025

ABSTRACT

FTIR spectroscopy was applied to investigate the interaction of anionic surfactant Sodium Dodecyl Sulfate (SDS) and Bovine Serum Albumin (BSA). Amide band I of BSA was analyzed to obtain the change in secondary structure of BSA when different concentration of SDS was added and during different interaction period. In short interaction period and at low concentration of SDS, the alpha-helixes increased and the random coil decreased. In long interaction period or at high concentration of SDS, SDS unfolded the protein by decreasing the alpha-helix structure and increasing the random coil.


Subject(s)
Serum Albumin, Bovine/chemistry , Sodium Dodecyl Sulfate/chemistry , Spectroscopy, Fourier Transform Infrared , Animals , Anions , Cattle , Hydrogen-Ion Concentration , Protein Binding , Protein Folding , Protein Structure, Secondary , Serum Albumin, Bovine/metabolism , Sodium Dodecyl Sulfate/metabolism , Surface-Active Agents/chemistry , Surface-Active Agents/metabolism , Time Factors
SELECTION OF CITATIONS
SEARCH DETAIL