scholarly journals Oil-in-Water Emulsions Stabilized by Ultrasonic Degraded Polysaccharide Complex

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1097 ◽  
Author(s):  
Yujie Li ◽  
Dong Xiang ◽  
Bo Wang ◽  
Xiaoyue Gong

The effects of ultrasound on the molecular weight distribution and emulsifying properties of both xanthan gum (XG) and propylene glycol alginate (PGA) were investigated. The results showed that ultrasonic treatment at different intensities decreased the apparent viscosity and narrowed the molecular weight distribution. Higher intensity increased the effectivity of the sonochemical effect. Ultrasound degradation did not change the primary structure of the PGA-XG complex, and SEM analysis showed that the morphology of the original polysaccharide differed from that of the degraded polysaccharide fractions. The ultrasonic intensities and treatment times had a substantial influence on the stability of the polysaccharide-stabilized oil-in-water (O/W) emulsions. The O/W emulsion stabilized by the polysaccharide treated with 270 W ultrasound waves for 7 min led to the smallest average particle size (detected via fluorescence microscopy) and showed stability against aggregation in O/W emulsions.

1982 ◽  
Vol 60 (5) ◽  
pp. 564-571 ◽  
Author(s):  
Dominique Ades ◽  
Michel Fontanille ◽  
Jacques Leonard

The anionic bulk polymerization of α-methylstyrene (αMS) has been carried out using tert-butyllithium (t-BuLi) as initiator with or without N,N,N′,N′-tetramethylethylenediamine (TMEDA). In absence of TMEDA, the "living ends" are rapidly deactivated at 62 °C whereas they are relatively more stable at 25 °C. The "living ends" are much more stable in presence of TMEDA; however, their stability is a function of the order in which t-BuLi and TMEDA are added to αMS. The stability of "living ends" is also a function of the ratio r = [TMEDA]/[t-BuLi] and best results are obtained with a one to one ratio. At high temperature, the formation of species with absorption bands at 390 and 424 nm and the broadening of the molecular weight distribution are observed. These results are explained in terms of a transfer reaction to the monomer or to the deactivated polymer.


Foods ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 686
Author(s):  
Hao Tian ◽  
Qizhu Zhao ◽  
Zhiyong He ◽  
Zhaojun Wang ◽  
Fang Qin ◽  
...  

The effects of molecular weight (MW) and degree of esterification (DE) of soluble soybean polysaccharide (SSPS) on the stability of casein under acidic conditions were investigated. The ability of SSPS to stabilize casein was characterized by the content of SSPS–casein complex, the LUMiSizer instability index, average particle size, zeta potential, and storage experiments. The long-term storage stability of the mixtures was related to their ability to combine casein and the stability of the complexes. At the same DE, SSPSs with medium MW formed more complexes with casein than SSPSs with high or low MW; and at the same MW, SSPSs with medium or low DE formed more complexes than SPSSs with high DE. In addition, SSPSs with higher MW had a better stabilizing behavior due to the large steric repulsion between complexes. SSPSs with high MW and low DE showed the best ability to stabilize casein under acid conditions.


2013 ◽  
Vol 10 (2) ◽  
pp. 29
Author(s):  
Normah Ismail ◽  
Nur' Ain Mohamad Kharoe

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage. 


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