Simultaneous nanoparticle formation and encapsulation driven by hydrophobic interaction of casein-graft-dextran and beta-carotene.
نویسندگان
چکیده
Casein-graft-dextran copolymer was produced using the Maillard reaction. The copolymer is molecularly soluble in neutral aqueous solution whereas beta-carotene is extremely insoluble. By the method of dialysis or evaporation then dispersing in water, the solubility of hydrophobic complex of casein and beta-carotene decreases whereas the solubility of dextran increases gradually, then nanoparticles formed with casein and beta-carotene core and dextran shell. The particles have spherical shape and are stable in aqueous solution against dilution, pH change, ionic strength change, FeCl3 oxidation and long time storage. The encapsulated beta-carotene can be released by pepsin or trypsin hydrolysis. To our knowledge, this is the first report of simultaneous nanoparticle formation and encapsulation induced by hydrophobic interaction. Casein-graft-dextran copolymer and the nanoparticle preparation is a green process in which only alkali and ethanol, no other chemicals, were used.
منابع مشابه
Exploring the Interaction Mechanism of Coumarin with Bovine β-Casein: Spectrofluorometric and Molecular Modeling Studies
This paper is designed to examine the binding behavior of Coumarin with bovine -casein (βCN) through fluorescence spectroscopy and molecular modeling techniques. The data analysis on fluorescence titration experiments at various temperatures represents the enthalpy driven nature for the formation of Coumarin–βCN complex and the prevailed role of hydrogen bonds and van der Waals interactions in...
متن کاملIn Vitro Cytotoxic Activity and Binding Properties of Curcumin in the Presence of β-Casein Micelle Nanoparticles
Curcumin (CUR) is the active curcuminoid with many physiological, biochemical, and pharmacological properties. Solubility and stability of CUR is the limiting factors for realizing its therapeutic potential. Bovine β-casein is an abundant milk protein that is highly amphiphilic and self-assembles into stable micellar nanoparticles in aqueous solution. β-Casein nanoparticle can solubilize CUR mo...
متن کاملInvestigation the protective ability of Pulicaria. undulata aqueous extract on aggregation of κ -casein
Protein aggregation is phenomenon wherein protein loses its native structure and aggregates due to the adaption of non-native conformation. Amyloid aggregation formed by the accumulation of various proteins causes many diseases in humans and other organisms. Antioxidants can prevent proteins aggregation. Pulicaria undulata extract along with phenolic compounds can increase protein stability an...
متن کاملThermodynamic investigation of the interaction between Mono-s-chloroTriazinyl MCT Reactive Dyes and cetylpyridinium chloride inaqueous solution
The interactions two synthetic triazinyl reactive dyes Mono-s-chloro Triazinyl reactive dyes DI and DII with the cationic surfactant N-hexadecyl pyridinium chloride CPC were studied using a conductometric method in 25, 30, 35, 40 and 45ºC. The equilibrium constants and other thermodynamic parameters for the ion pair formation were calculated on the basis of a theoretical model using the data ob...
متن کاملSpectroscopic, Docking and Molecular Dynamics Simulation Studies on the Interaction of Etofylline and Human Serum Albumin
The purpose of this study is to investigate the interaction of Etofylline as an established drug for asthma remedy, with the major transport protein in human blood circulation, the human serum albumin (HSA). In this respect, the fluorescence and circular dichroism (CD) spectroscopy techniques, along with the molecular docking and molecular dynamics simulation methods were employed. Analysis of ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of colloid and interface science
دوره 315 2 شماره
صفحات -
تاریخ انتشار 2007