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      The Role of Extrusion Conditions on the Mechanical Properties of Thermoplastic Protein

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          Abstract

          Mechanical properties of Novatein thermoplastic protein compounded at different extrusion temperatures and processing water contents have been examined in a factorial experiment. Thermoplastic proteins are moisture sensitive and can be prone to thermal degradation during processing. Processing water was varied between 30 and 45 parts per hundred parts bloodmeal while the extrusion temperature was varied between 120 and 150 °C to identify a processing window suitable for process scale up. To resolve any effects processing water had on protein-protein interactions from its plasticising effect, injection molded specimens were mechanically tested both as molded and after conditioning at controlled temperature and humidity. Despite all conditioned samples having approximately the same moisture content, mechanical properties were different. Tensile strength and modulus decreased with increasing processing water at the same equilibrium moisture content. DMA and WAXS suggested this was due to changes in chain mobility within the amorphous phase of the material, rather than conformational change towards a more ordered state. Properties of unconditioned specimens were mostly dependent on the plasticising effect of different amounts of processing water remaining in the material after injection molding. Extrusion temperature had very little effect on mechanical properties, suggesting that Novatein is robust enough to handle some temperature variations during processes such as injection molding.

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          Most cited references 29

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          Thermoplastic processing of proteins for film formation--a review.

          Increasing interest in high-quality food products with increased shelf life and reduced environmental impact has encouraged the study and development of edible and/or biodegradable polymer films and coatings. Edible films provide the opportunity to effectively control mass transfer among different components in a food or between the food and its surrounding environment. The diversity of proteins that results from an almost limitless number of side-chain amino-acid sequential arrangements allows for a wide range of interactions and chemical reactions to take place as proteins denature and cross-link during heat processing. Proteins such as wheat gluten, corn zein, soy protein, myofibrillar proteins, and whey proteins have been successfully formed into films using thermoplastic processes such as compression molding and extrusion. Thermoplastic processing can result in a highly efficient manufacturing method with commercial potential for large-scale production of edible films due to the low moisture levels, high temperatures, and short times used. Addition of water, glycerol, sorbitol, sucrose, and other plasticizers allows the proteins to undergo the glass transition and facilitates deformation and processability without thermal degradation. Target film variables, important in predicting biopackage performance under various conditions, include mechanical, thermal, barrier, and microstructural properties. Comparisons of film properties should be made with care since results depend on parameters such as film-forming materials, film formulation, fabrication method, operating conditions, testing equipment, and testing conditions. Film applications include their use as wraps, pouches, bags, casings, and sachets to protect foods, reduce waste, and improve package recyclability.
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            Extrusion Processing and Properties of Protein-Based Thermoplastics

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              Mechanical and thermal properties of extruded soy protein sheets

               P Mungara,  J. Jane,  J ZHANG (2001)
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                Author and article information

                Journal
                ipp
                International Polymer Processing
                Carl Hanser Verlag
                0930-777X
                2195-8602
                27 May 2018
                : 33
                : 2
                : 180-190
                Affiliations
                1 Department of Engineering, School of Science and Engineering, University of Waikato, Hamilton, New Zealand
                2 Aduro Bioploymers LP, Hamilton, New Zealand
                Author notes
                [* ] Correspondence address, Mail address: Casparus Johannes Reinhard Verbeek, Department of Engineering, School of Science and Engineering, University of Waikato, Private Bag 3105, Hamilton 3240, New Zealand, E-mail: jverbeek@ 123456waikato.ac.nz
                Article
                IPP3391
                10.3139/217.3391
                © 2018, Carl Hanser Verlag, Munich
                Page count
                References: 33, Pages: 11
                Product
                Self URI (journal page): http://www.hanser-elibrary.com/loi/ipp
                Categories
                Regular Contributed Articles

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