scholarly journals Analysis of Stability of Silica Nano-Particle-Laden Microbubble Dispersion

Author(s):  
Rashi Gupta ◽  
Roshan Saini ◽  
Rajeev Parmar

Abstract Microbubbles are small gas filled bubbles which has wide application in various industries. Stability of microbubble dispersion is of primary concern for the application of microbubbles in these fields. In this research, the stability of microbubble dispersion generated using CTAB surfactant is analysed by drainage mechanism. The stability is studied on the basis of half-life of microbubble dispersion. Microbubble dispersion gas fraction and rise velocity of microbubble is also calculated and the size of microbubble is estimated from the rise velocity of microbubble. Further, Silica nanoparticles are added in the surfactants to study their effect on the stability of microbubble dispersion. The observed results clearly indicates that the stability of microbubble dispersion is significantly affected by the surfactant concentration and the weight of silica nanoparticle in the liquid. Similar results were observed for rise velocity and bubble size. The present work may be beneficial for the application of microbubble in various chemical and biochemical industries and scientific community.

1977 ◽  
Vol 16 (04) ◽  
pp. 157-162 ◽  
Author(s):  
C. Schümichen ◽  
B. Mackenbrock ◽  
G. Hoffmann

SummaryThe bone-seeking 99mTc-Sn-pyrophosphate compound (compound A) was diluted both in vitro and in vivo and proved to be unstable both in vitro and in vivo. However, stability was much better in vivo than in vitro and thus the in vitro stability of compound A after dilution in various mediums could be followed up by a consecutive evaluation of the in vivo distribution in the rat. After dilution in neutral normal saline compound A is metastable and after a short half-life it is transformed into the other 99mTc-Sn-pyrophosphate compound A is metastable and after a short half-life in bone but in the kidneys. After dilution in normal saline of low pH and in buffering solutions the stability of compound A is increased. In human plasma compound A is relatively stable but not in plasma water. When compound B is formed in a buffering solution, uptake in the kidneys and excretion in urine is lowered and blood concentration increased.It is assumed that the association of protons to compound A will increase its stability at low concentrations while that to compound B will lead to a strong protein bond in plasma. It is concluded that compound A will not be stable in vivo because of a lack of stability in the extravascular space, and that the protein bond in plasma will be a measure of its in vivo stability.


Genetics ◽  
2003 ◽  
Vol 163 (1) ◽  
pp. 91-101 ◽  
Author(s):  
Erin N Asleson ◽  
Dennis M Livingston

Abstract We investigated the stability of the Saccharomyces cerevisiae Rad52 protein to learn how a cell controls its quantity and longevity. We measured the cellular levels of wild-type and mutant forms of Rad52p when expressed from the RAD52 promoter and the half-lives of the various forms of Rad52p when expressed from the GAL1 promoter. The wild-type protein has a half-life of 15 min. rad52 mutations variably affect the cellular levels of the protein products, and these levels correlate with the measured half-lives. While missense mutations in the N terminus of the protein drastically reduce the cellular levels of the mutant proteins, two mutations—one a deletion of amino acids 210-327 and the other a missense mutation of residue 235—increase the cellular level and half-life more than twofold. These results suggest that Rad52p is subject to post-translational regulation. Proteasomal mutations have no effect on Rad52p half-life but increase the amount of RAD52 message. In contrast to Rad52p, the half-life of Rad51p is >2 hr, and RAD51 expression is unaffected by proteasomal mutations. These differences between Rad52p and Rad51p suggest differential regulation of two proteins that interact in recombinational repair.


1988 ◽  
Vol 43 (11-12) ◽  
pp. 871-876 ◽  
Author(s):  
Imre Vass ◽  
Narendranath Mohanty ◽  
Sándor Demeter

Abstract The effect of photoinhibition on the primary (QA) and secondary (QB) quinone acceptors of photosystem I I was investigated in isolated spinach thylakoids by the methods of thermoluminescence and delayed luminescence. The amplitudes of the Q (at about 2 °C) and B (at about 30 °C) thermoluminescence bands which are associated with the recombination of the S2QA- and S2QB charge pairs, respectively, exhibited parallel decay courses during photoinhibitory treatment. Similarly, the amplitudes of the flash-induced delayed luminescence components ascribed to the recombination of S20A and S2OB charge pairs and having half life-times of about 3 s and 30 s, respectively, declined in parallel with the amplitudes of the corresponding Q and B thermoluminescence bands. The course of inhibition of thermoluminescence and delayed luminescence intensity was parallel with that of the rate of oxygen evolution. The peak positions of the B and Q thermoluminescence bands as well as the half life-times of the corresponding delayed luminescence components were not affected by photoinhibition. These results indicate that in isolated thylakoids neither the amount nor the stability of the reduced OB acceptor is preferentially decreased by photoinhibition. We conclude that either the primary target of photodamage is located before the O b binding site in the reaction center of photosystem II or QA and OB undergo simultaneous damage.


2010 ◽  
Vol 192 (22) ◽  
pp. 6064-6076 ◽  
Author(s):  
John W. Little ◽  
Christine B. Michalowski

ABSTRACT Complex gene regulatory circuits exhibit emergent properties that are difficult to predict from the behavior of the components. One such property is the stability of regulatory states. Here we analyze the stability of the lysogenic state of phage λ. In this state, the virus maintains a stable association with the host, and the lytic functions of the virus are repressed by the viral CI repressor. This state readily switches to the lytic pathway when the host SOS system is induced. A low level of SOS-dependent switching occurs without an overt stimulus. We found that the intrinsic rate of switching to the lytic pathway, measured in a host lacking the SOS response, was almost undetectably low, probably less than 10−8/generation. We surmise that this low rate has not been selected directly during evolution but results from optimizing the rate of switching in a wild-type host over the natural range of SOS-inducing conditions. We also analyzed a mutant, λprm240, in which the promoter controlling CI expression was weakened, rendering lysogens unstable. Strikingly, the intrinsic stability of λprm240 lysogens depended markedly on the growth conditions; lysogens grown in minimal medium were nearly stable but switched at high rates when grown in rich medium. These effects on stability likely reflect corresponding effects on the strength of the prm240 promoter, measured in an uncoupled assay system. Several derivatives of λprm240 with altered stabilities were characterized. This mutant and its derivatives afford a model system for further analysis of stability.


Foods ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2261
Author(s):  
Oscar López-Balladares ◽  
Patricio J. Espinoza-Montero ◽  
Ramiro Acosta-Sandoval

The physicochemical properties of pastry and confectionery products greatly influence the aesthetic design of a cake topping, since they can be susceptible to physicochemical changes in a very short time, so maintaining a good appearance and texture of the topping becomes a challenge. Generally, cake creams deteriorate over time. The evaluation of the physicochemical properties of natural gums (arabic gum, tara gum, carrageenan, and pectin) is proposed in this work as a way to improve the physicochemical stability of butter-based cake creams (coverage creams) to maintain the initial appearance of the cream and to lengthen the separation time of their phases. For this purpose, some parameters related to the physicochemical stability of the cream, such as viscosity, density, bubble size, syneresis, volume and rheological behavior were measured. The result of the ANOVA and Tukey’s tests displayed significant differences for the measured parameters, which shows that natural gums substantially improve the stability of butter cream. The best natural gum found was the tara gum (TG) which improved viscosity 5.6 times with respect to that of the cream without gums (η¯ without gums = 15.49 Pa·s, η¯ with TG = 87.09 Pa·s), while the bubble size remained small, 1.6 times smaller compared to that of the cream without gum (BS¯) without gums = 57 μm, (BS¯) with TG = 35 μm), and the volume loss decreased two times when compared to that of the cream without gums ((ΔV¯) without gums = 1.57 cm3, (ΔV¯) with TG = 0.80 cm3). The cream with TG showed better rheology compared to that of the cream without gums (the cream without gums exhibited a plastic and thixotropic behavior, with permanent elastic deformation, while cream with TG exhibited thixotropic behavior without permanent elastic deformation). Finally, it was found that the cream with TG acquired a higher thixotropic index (TI) compared to that of the cream without gums (TI max. without gums = 17.40 y 71.78 q.u., TI max. with TG = 74.67 and 1559.90 q.u., at 4 °C and 25 °C, respectively) which demonstrates the effective contribution of cream with TG in 66.67% of the measured parameters.


Catalysts ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 983
Author(s):  
Wahhida Latip ◽  
Victor Feizal Knight ◽  
Ong Keat Khim ◽  
Noor Azilah Mohd Kasim ◽  
Wan Md Zin Wan Yunus ◽  
...  

Immobilization is a method for making an enzyme more robust in the environment, especially in terms of its stability and reusability. A mutant phosphotriesterase (YT PTE) isolated from Pseudomonas dimunita has been reported to have high proficiency in hydrolyzing the Sp and Rp-enantiomers of organophosphate chromophoric analogs and therefore has great potential as a decontamination agent and biosensor. This work aims to investigate the feasibility of using Fuller’s earth (FE) as a YT PTE immobilization support and characterize its biochemical features after immobilization. The immobilized YT PTE was found to show improvement in thermal stability with a half-life of 24 h compared to that of the free enzyme, which was only 8 h. The stability of the immobilized YT PTE allowed storage for up to 4 months and reuse for up to 6 times. The immobilized YT PTE showed high tolerance against all tested metal ions, Tween 40 and 80 surfactants and inorganic solvents. These findings showed that the immobilized YT PTE became more robust for use especially with regards to its stability and reusability. These features would enhance the future applicability of this enzyme as a decontamination agent and its use in other suitable industrial applications.


The design of open-cut slopes and embankments, foundations, levees, and earth-dam cross-sections is based primarily on stability considerations. There are many causes and types of earth instability. There are also many ways of analyzing the stability of slopes. The chapter considers the limit equilibrium approach, which aims essentially to determine a factor of safety, F, that would ensure a slope does not fail. The chapter considers the analysis of stability of infinite slopes based on translational type of failure and the analysis of finite slopes using the Swedish Method, Method of Slices, Bishop Simplified Method, Friction Circle Method, and the Translational Method. The solution of equations developed for the analysis of stability of slopes can be tedious and time consuming. A way of reducing the amount of calculation required in slope stability studies is by use of charts based on geometric similarity. The chapter discusses how Taylor (1948) and Janbu (1964) charts are used in stability analysis of slopes. Finally, the chapter discusses ways to reduce the risk of instability in slopes.


1989 ◽  
Vol 35 (8) ◽  
pp. 1774-1776 ◽  
Author(s):  
D A Smith ◽  
G C Moses ◽  
A R Henderson

Abstract We examined the stability of human lactate dehydrogenase (EC 1.1.1.27) isoenzyme 5--purified to a specific activity of about 400 kU/g--when lyophilized in a buffered, stabilized matrix of bovine albumin. This isoenzyme was prepared with a final activity of about 500 U/L and stored at -20, 4, 20, 37, and 56 degrees C for as long as six months. This isoenzyme decayed with approximate first-order kinetics, with an estimated half-life at -20 degrees C of about 475 years. Stability of reconstituted samples stored at 20 or 4 degrees C was poor, suggesting that the reconstituted material should be used without delay; material stored at -20 degrees C showed excellent stability for 15 days. We propose that such preparations might be further investigated as standards for use in electrophoresis of lactate dehydrogenase isoenzymes.


2011 ◽  
Vol 189-193 ◽  
pp. 3153-3157
Author(s):  
Yan Zhen Zhang ◽  
Yong Hong Liu ◽  
Ren Jie Ji ◽  
Bao Ping Cai

In this paper, the EDM performance of water-in-oil (W/O) emulsions dielectric with different surfactant concentration is investigated by correlated to its physical properties, such as viscosity and droplets size, which is predominantly determined by the surfactant concentration. Experimental results show that the stability of the W/O emulsions increases with increasing surfactant concentration, whereas the EDM performance deteriorates with increasing surfactant concentration. So, taking a comprehensively consideration of the emulsion stability and EDM performance, the concentration of surfactant must be appropriately selected.


Sign in / Sign up

Export Citation Format

Share Document