Role of hydrophobic and electrostatic interactions for initial enteric virus retention by MF membranes

نویسندگان

  • E. M. van Voorthuizen
  • N. J. Ashbolt
  • A. I. Schäfer
چکیده

Membranes are of increasing interest for the removal of human enteric viruses from wastewater, especially when the goal of treatment is reuse. Limited work has been undertaken on fundamental issues such as aggregation and the role of electrostatic and hydrophobic interactions, as opposed to the sieving of viruses by membranes. One apparently critical factor would be the iso-electric point (pI) of a virus. As an example of a worst-case model virus, the retention of bacteriophage MS-2 was investigated using hydrophobic (GVHP) and hydrophilic (GVWP) 0.22 μm MF membranes at different pH levels and with different salts. High retention levels were measured at the iso-electric point of MS-2, pH 3.9 (5 log retention) and pH 7 (4.3 log retention) in the presence of salts and with a hydrophobic membrane. When retention was compared on a hydrophilic membrane, it was clear that hydrophobic interactions dominated virus retention, and this was improved by salt, presumably causing reduction of the Gouy double-layer when MS-2 was charged (pH 7). This paper shows that knowledge of the adsorption characteristics of viruses and the suspending conditions are important to predict removal of viruses by hydrophobic MF membranes, and discusses some of the practical implications of these important hydrophobic interactions.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Thermodynamic Analysis for Cationic Surfactants Binding to Bovine Serum Albumin

In the present study, the binding isotherms for interaction of a homologous series of n-alkyltrimethyl ammonium bromides with bovine serum albumin (BSA) have been analyzed on basis of intrinsic thermodynamic quantities. In this regards, the intrinsic Gibbs free energy of binding, AGb(i,)„ has been estimated at various surfactant concentrations and its trend of variation for both binding sets ha...

متن کامل

Electrostatic and hydrophobic interactions differentially tune membrane binding kinetics of the C2 domain of protein kinase Cα.

The cellular activation of conventional protein kinase C (PKC) isozymes is initiated by the binding of their C2 domains to membranes in response to elevations in intracellular Ca(2+). Following this C2 domain-mediated membrane recruitment, the C1 domain binds its membrane-embedded ligand diacylglycerol, resulting in activation of PKC. Here we explore the molecular mechanisms by which the C2 dom...

متن کامل

Novel consensus quantitative structure-retention relationship method in prediction of pesticides retention time in nano-LC

In this study, quantitative structure-retention relationship (QSRR) methodology employed for modeling of the retention times of 16 banned pesticides in nano-liquid chromatography (nano-LC) column. Genetic algorithm-multiple linear regression (GA-MLR) method employed for developing global and consensus QSRR models. The best global GA-MLR model was established by adjusting GA parameters. Three de...

متن کامل

Coductometric studies of the interaction of acid green 25 with cationic alkyltrimethylammonium bromid surfactants

The interactions between an anionic dye, Acid Green 25 AG and the two cationic surfactants tetradecyltrimethylammonium bromide TTAB, and hexadecyltrimethylammonium bromide CTAB in aqueous solutions far below the CMC are studied using the conductometric method at different temperature. The equilibrium constants and other thermodynamic functions for the process of dye-surfactant ion pair formatio...

متن کامل

Thermodynamic 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 کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2010