NDLI: Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels

Please wait, while we are loading the content...

Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels

Content Provider	Springer Nature Link
Author	Kerstens, Sven Mugnier, Cindy Murray, Brent S. Dickinson, Eric
Copyright Year	2006
Abstract	Using confocal microscopy, we studied the effect of heating (up to 85°C) on the microstructure of β-lactoglobulin-stabilized emulsions (20 vol% oil, pH 6.8) containing excess protein (total protein content 13.2%). Two different fluorescent dyes were used to separately visualize the oil droplets and the protein. In overlay micrographs, their location with respect to each other could then be determined. In the presence of a low salt concentration, flocculation of the emulsion without surfactant was inhibited, by a mechanism analogous to the “salting-in” of aqueous protein solutions. Addition of the anionic surfactant sodium dodecyl sulfate (SDS) caused weak flocculation, probably as a result of the formation of protein−SDS complexes. The final heat-set emulsion contained distinct pores for a surfactant/protein ratio of R = 1, but no pores for R = 2. Addition of the cationic surfactant cetyl trimethyl ammonium bromide (CTAB) caused strong aggregation, as indicated by microscopic observation of the concentrated emulsion and light scattering of the diluted emulsion. For R = 1 with CTAB, there were aggregates consisting of oil droplets and excess protein. At R = 2, almost all the excess protein was aggregated into separate protein flakes. In the final emulsion gels containing CTAB, the protein was more spread out. Differing structural behavior with anionic and cationic surfactants has been interpreted in terms of different protein−surfactant interactions in aqueous solution and at the oil−water interface, both before and after protein denaturation.
Starting Page	133
Ending Page	143
Page Count	11
File Format	PDF
ISSN	15571858
Journal	Food Biophysics
Volume Number	1
Issue Number	3
e-ISSN	15571866
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2006-08-02
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Confocal laser scanning microscopy Protein−surfactant interactions Competitive displacement Emulsion gel β-Lactoglobulin SDS CTAB
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Biophysics Bioengineering Food Science Applied Microbiology and Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Texture and Microstructure of Gelatin/Corn Starch-Based Gummy Confections

Influence of Environmental Stresses on O/W Emulsions Stabilized by β-Lactoglobulin–Pectin and β-Lactoglobulin–Pectin–Chitosan Membranes Produced by the Electrostatic Layer-by-Layer Deposition Technique

The Observation of the Displacement of Emulsifiers by Confocal Scanning Laser Microscopy

Influence of Emulsifier on the Competitive Adsorption of Whey Proteins in Emulsions

Influence of Emulsifier on the Competitive Adsorption of Whey Proteins in Emulsions

Formation of Multilayers at the Interface of Oil-in-Water Emulsion via Interactions between Lactoferrin and β-Lactoglobulin

Influence of Levan on the Thermally Induced Gel Formation of β-Lactoglobulin

Influence of a Non-Ionic Surfactant in the Microstructure and Rheology of a Pickering Emulsion Stabilized by Cellulose Nanofibrils

The Effect of pH and Heat Pre-Treatments on the Physicochemical and Emulsifying Properties of β-lactoglobulin

Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels

Similar Documents

Texture and Microstructure of Gelatin/Corn Starch-Based Gummy Confections

Influence of Environmental Stresses on O/W Emulsions Stabilized by β-Lactoglobulin–Pectin and β-Lactoglobulin–Pectin–Chitosan Membranes Produced by the Electrostatic Layer-by-Layer Deposition Technique

The Observation of the Displacement of Emulsifiers by Confocal Scanning Laser Microscopy

Influence of Emulsifier on the Competitive Adsorption of Whey Proteins in Emulsions

Influence of Emulsifier on the Competitive Adsorption of Whey Proteins in Emulsions

Formation of Multilayers at the Interface of Oil-in-Water Emulsion via Interactions between Lactoferrin and β-Lactoglobulin

Influence of Levan on the Thermally Induced Gel Formation of β-Lactoglobulin

Influence of a Non-Ionic Surfactant in the Microstructure and Rheology of a Pickering Emulsion Stabilized by Cellulose Nanofibrils

The Effect of pH and Heat Pre-Treatments on the Physicochemical and Emulsifying Properties of β-lactoglobulin

Influence of Ionic Surfactants on the Microstructure of Heat-Set β-Lactoglobulin-Stabilized Emulsion Gels