Formation of secondary structures in protein foams as detected by synchrotron FT-IR

Abstract FT-IR analysis was used to study the effect of temperature on foaming Novatein, a semi-crystalline thermoplastic biopolymer based on blood meal. Foaming was caused by rapid expansion of steam, ammonia and CO 2 from urea hydrolysis, leading to expansion ratios between 3.8 and 5.6. Plasticisers were more concentrated near the bubble surface, suggesting some tri-ethylene glycol accumulation. The β-sheet fraction in Novatein was not influenced by foaming or thermal treatment, but their distribution was influenced by bubble growth. β-sheets agglomerated near the bubble surface and was more pronounced at higher temperatures.