Protein adsorption at solid-liquid interfaces: Part II--Adsorption from binary protein mixture.

Simple item page
dc.contributor.authorHajra, Sen_US
dc.contributor.authorChattoraj, D Ken_US
dc.date.accessioned1991-04-01en_US
dc.date.accessioned2009-05-27T09:43:11Z
dc.date.available1991-04-01en_US
dc.date.available2009-05-27T09:43:11Z
dc.date.issued1991-04-01en_US
dc.description.abstractExtent of adsorption of proteins at alumina-water interface from solutions containing binary mixture of beta-lactoglobulin and bovine serum albumin (BSA), beta-lactoglobulin and gelatin, and gelatin and bovine serum albumin has been estimated as functions of protein concentrations at varying pH, ionic strength, temperature and weight fraction ratios of protein mixture. The extent of adsorption (gamma lacw) of lactoglobulin in the presence of BSA increases with increase of protein concentration (Clac) until it reaches a maximum but a fixed value gamma lacw(m). Extent of adsorption gamma serw also initially increases with increase of protein concentrations until it reaches maximum value gamma serw(m). Beyond these protein concentrations, adsorbed BSA is gradually desorbed due to the preferential adsorption of lactoglobulin from the protein mixture. In many systems, gamma serw at high protein concentrations even becomes negative due to the strong competition of BSA and water for binding to the surface sites in the presence of lactoglobulin. For lactoglobulin-gelatin mixtures, adsorption of both proteins is enhanced as protein concentration is increased until limiting values for adsorption are reached. Beyond the limiting value, lactoglobulin is further accumulated at the interface without limit when protein concentration is high. For gelatin-albumin mixtures, extent of gelatin adsorption increases with increase in the adsorption of BSA. The limit for saturation of adsorption for gelatin is not reached for many systems. At acid pH, adsorbed BSA appears to be desorbed from the surface in the presence of gelatin. From the results thus obtained the role of electrostatic and hydrophobic effects in controlling the adsorption process has been analysed.en_US
dc.description.affiliationDepartment of Food Technology & Biochemical Engineering, Jadavpur University, Calcutta.en_US
dc.identifier.citationHajra S, Chattoraj DK. Protein adsorption at solid-liquid interfaces: Part II--Adsorption from binary protein mixture. Indian Journal of Biochemistry & Biophysics. 1991 Apr; 28(2): 124-32en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/28356
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAdsorptionen_US
dc.subject.meshAluminum Oxideen_US
dc.subject.meshGelatin --chemistryen_US
dc.subject.meshLactoglobulins --chemistryen_US
dc.subject.meshProteins --chemistryen_US
dc.subject.meshSerum Albumin, Bovine --chemistryen_US
dc.titleProtein adsorption at solid-liquid interfaces: Part II--Adsorption from binary protein mixture.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
Files
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
1.79 KB
Format:
Plain Text
Description:
Download
Collections
Indian Journal of Biochemistry & Biophysics