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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Physicochemical characterization of collagen fibers and collagen powder for self-composite film production

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Author(s):
Wolf, K. L. [1] ; Sobral, P. J. A. [2] ; Telis, V. R. N. [1]
Total Authors: 3
Affiliation:
[1] UNESP, Dept Engn & Tecnol Alimentos, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[2] USP, Dept Engn Alimentos, BR-13635900 Pirassununga, SP - Brazil
Total Affiliations: 2
Document type: Journal article
Source: FOOD HYDROCOLLOIDS; v. 23, n. 7, p. 1886-1894, OCT 2009.
Web of Science Citations: 20
Abstract

The purpose of this work was to determine some physicochemical characteristics of collagen fibers and collagen powder obtained from bovine hides as potential raw materials for production of films with improved mechanical properties. These materials are collagen in its crude form, without the hydrolysis reaction that leads to gelatin production. The following analyses were carried out: proximate composition, amino acid composition, solubility in water, differential scanning calorimetry (DSC). Fourier transform infrared spectroscopy (FTIR), size distribution and moisture sorption isotherms. The collagen fibers and collagen powder showed practically the same protein content, and the only differences between them, apart from the particle shape and size, were in their solubility in water, which was probably partly due to differences in particle size. Due to their similar composition but different physical properties, collagen fibers and collagen powder were shown to be suitable for the production of biocomposite films where the powder is the basis of the film matrix and the fibers act as filler, exerting a reinforcement effect. Films with the protein content supplied by 50% collagen powder and 50% collagen fibers could be produced with the film thickness fixed at 180 pm and subjective evaluations suggested that the fibers remained completely involved in the filmogenic matrix. (C) 2009 Elsevier Ltd. All rights reserved. (AU)