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      Determination Quantification of Molecular Interactions in Protein Films: A Review

      review-article
      1 , 1 , 2 , *
      Materials
      MDPI
      whey protein, soy protein, wheat gluten, cross-linking, SDS‑PAGE, NMR, CD, FTIR, protein solubility study

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          Abstract

          Protein based films are nowadays also prepared with the aim of replacing expensive, crude oil-based polymers as environmentally friendly and renewable alternatives. The protein structure determines the ability of protein chains to form intra- and intermolecular bonds, whereas the degree of cross-linking depends on the amino acid composition and molecular weight of the protein, besides the conditions used in film preparation and processing. The functionality varies significantly depending on the type of protein and affects the resulting film quality and properties. This paper reviews the methods used in examination of molecular interactions in protein films and discusses how these intermolecular interactions can be quantified. The qualitative determination methods can be distinguished by structural analysis of solutions (electrophoretic analysis, size exclusion chromatography) and analysis of solid films (spectroscopy techniques, X-ray scattering methods). To quantify molecular interactions involved, two methods were found to be the most suitable: protein film swelling and solubility. The importance of non-covalent and covalent interactions in protein films can be investigated using different solvents. The research was focused on whey protein, whereas soy protein and wheat gluten were included as further examples of proteins.

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          How to study proteins by circular dichroism.

          Circular dichroism (CD) is being increasingly recognised as a valuable technique for examining the structure of proteins in solution. However, the value of many studies using CD is compromised either by inappropriate experimental design or by lack of attention to key aspects of instrument calibration or sample characterisation. In this article, we summarise the basis of the CD approach and its application to the study of proteins, and then present clear guidelines on how reliable data can be obtained and analysed.
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            Functional properties of soy proteins

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              Stabilization of gelatin films by crosslinking with genipin.

              The possibility to stabilize gelatin films by crosslinking with genipin was investigated through a mechanical, chemical and thermal characterization of samples treated with genipin solutions at different concentrations. The extent of crosslinking, evaluated as difference between the number of free epsilon -amino groups before and after crosslinking, increases as a function of genipin concentration up to about 85%. Simultaneously, the deformability of the films decreases whereas the Young's modulus E, increases. Furthermore, crosslinking provokes a significant reduction of the swelling in physiological solution, and enhances the thermal stability of the samples, as indicated by the results of the d.s.c. investigation. The data obtained from the films treated with genipin at concentrations higher than 0.67% are quite similar, and indicative of a good stabilizing effect of genipin. In spite of the small gelatin release (2%) observed after 1 month of storage in buffer solution, the mechanical, thermal and swelling properties of the films are very close to those previously obtained for glutaraldehyde crosslinked gelatin, and suggest that genipin, which is by far less cytotoxic, can be considered a valid alternative for crosslinking gelatin biomaterials.
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                Author and article information

                Contributors
                Role: External Editor
                Journal
                Materials (Basel)
                Materials (Basel)
                materials
                Materials
                MDPI
                1996-1944
                10 December 2014
                December 2014
                : 7
                : 12
                : 7975-7996
                Affiliations
                [1 ]Fraunhofer-Institute for Process Engineering and Packaging IVV, Giggenhauser Strasse 35, Freising 85354, Germany; E-Mail: feeha@ 123456mytum.de
                [2 ]Chair of Food Packaging Technology, Technische Universität München, Weihenstephaner Steig 22, Freising 85354, Germany
                Author notes
                [* ] Author to whom correspondence should be addressed; E-Mail: markus.schmid@ 123456ivv.fraunhofer.de ; Tel.: +49-08161-491-526; Fax: +49-08161-491-555.
                Article
                materials-07-07975
                10.3390/ma7127975
                5456426
                483bf54c-7831-427e-b1d6-eccbf127fcaa
                © 2014 by the authors;

                licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 15 September 2014
                : 06 November 2014
                : 27 November 2014
                Categories
                Review

                whey protein,soy protein,wheat gluten,cross-linking,sds‑page,nmr,cd,ftir,protein solubility study

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