English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/17757
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Structural and functional properties of soy protein isolate and cod gelatin blend films

AuthorsPérez-Mateos, Miriam ; Denavi, Gabriela A.; Añón, María Cristina; Montero García, Pilar ; Mauri, Adriana N.; Gómez Guillén, M. C.
KeywordsEdible films
Soy proteins
Cod gelatine
Structural properties
Mechanical properties
Water vapor permeability
FTIR
Issue DateDec-2009
PublisherElsevier
CitationFood Hydrocolloids 23(8): 2094-2101 (2009)
AbstractThe structure-function relationship of composite films obtained from soybean-protein isolate (SPI) and cod gelatin was studied. Films with different ratios of SPI:gelatin (0, 25, 50, 75, 100% [w/w]) and plasticized by a mixture of glycerol and sorbitol were prepared by casting. Regardless of the soybean-protein concentration, the thickness and water-vapor permeability of the composite films diminished significantly as compared to pure-gelatin films. The formulation containing 25% SPI: 75% cod-skin gelatin had the maximum force at the breaking point, which was 1.8-fold and 2.8-fold greater than those of 100% gelatin and 100% SPI films, respectively. Moreover, this formulation offered high percent-deformation values lower than those of gelatin but higher than all other films containing SPI-, and the same relatively low water-vapor permeability as the 100% SPI film. While all the films exhibited high water solubility, a slight reduction in film solubility and soluble protein was observed with increasing SPI concentration. Differential-scanning calorimetry analyses revealed that gelatin was completely denatured in all films, while soy proteins largely maintained their native conformation. Analysis by fourier-transform–infrared spectroscopy revealed that the presence of 25% SPI produced gelatin conformational changes, self-aggregation of gelatin chains, and intermolecular associations via CO bonds between gelatin and SPI proteins. All films were translucent in appearance, but the yellowish color increased with increasing proportions of the soybean proteins.
Description8 pages, 6 figures, 3 tables
Publisher version (URL)http://dx.doi.org/10.1016/j.foodhyd.2009.03.007
URIhttp://hdl.handle.net/10261/17757
DOI10.1016/j.foodhyd.2009.03.007
ISSN0268-005X
Appears in Collections:(IF) Artículos
Files in This Item:
File Description SizeFormat 
structfilm.pdf164,29 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.