Gliadin, an abundant wheat storage protein, is fractionated from wheat gluten with aqueous ethanol. New functionalities may arise from the unique and valuable ability to form foams of these proteins. The development of gliadin-based foams is catering for a range of novel applications in food systems. Although, disadvantages as, brittleness of gliadin foams is limiting its utilization. Transglutaminases (TG) are enzymes that catalyse the formation of cross-links in proteins, thereby improving breadmaking performance. TGs can be a way to improve the structure of gliadin foams, due to the fact that polymers formed by the gliadins are important for foam properties. In this study, we focused on understanding whether the use of a newly TG type can improve the protein network and structure of gliadin foams. We studied the gliadin polymerization caused by the treatment with TG from a newly isolated Streptomyces sp. CBMAI 1617 (SB6) and compared to a control. The effect of TG enzyme concentration and an impact of lipid containing additives were studied. The resulting foams were analyzed from the nano to micro-structure by small angle x-ray scattering (SAXS) and scanning electron microscopy (SEM). The cell structure and cell size distribution were evaluated by x-ray tomography. Gliadin protein polymerization was monitored by SE-HPLC. The results showed that the gliadin foams, which were treated with newly produced TG, presented more homogeneous cell size distribution and larger sectional area than foams not treated with TG. The cross-links formed in gliadins by the catalysis of TG, decreased the extractability of proteins and induced polymerization. The results support the use of SB6 as a potential new catalyst to improve functionality to gliadin based products.