Novatein is a biopolymer produced from blood meal and can be foamed for use as a packaging material. The effect of foaming on protein ordered structures such as a-helices and b-sheets was investigated using synchrotron Fourier transform infrared (FTIR). Foaming caused a reduction in ordered structures due to an increase in random coils. FTIR also revealed a higher proportion of plasticizer (triethylene glycol, TEG) and b-sheets toward the surface of enclosed bubbles. Increased TEG will assist foaming with greater plasticization aiding nucleation, while b-sheets contribute to bubble stabilization. These structural changes occur as foaming takes place close to the degradation temperature of Novatein, and coincide with melting of a-helices and/or b-sheets. A more amorphous polymer is therefore produced which is subsequently easier to foam due to its increased elasticity. V C 2017 Wiley Periodicals, Inc. J.Appl. Polym. Sci. 2018, 135, 46005.Normal limits as defined in literature were redefined due to the shape of the second derivative.
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