Fig. 6 shows the values of tensile parameters (max, εmaxand Young’s Modulus) obtained for the reference systems and for probes containing 1.5 wt% LBG prepared at different pH. Ifonly polysaccharide-free bioplastics are compared, the presence of charges leads to apparent modifications of the tensile proper-ties of the system. At low pH, charges prevent formation of proteincross-linking by thermo-moulding, which leads to a microstruc-ture with higher mobility and ability to deform, due to presence of weak bonds (hydrogen bonds and van der Waals bonds), butshowing lower modulus Jansens et al. (2013). This microstructureis responsible for the low values of max, and Young’s Modulus andthe high material elongation (εmax) found at pH 3 (Fig. 6). At pH 6,the non-charged proteins are able to establish stronger bonds (ionicbonds and covalent bonds such as peptide and disulfide bonds) afterthermo-mechanical processing, which results in higher modulusvalues (max, and Young’s Modulus) and lower εmax, if compared to pH 3. Finally, at pH 9, the resultant microstructure is affected bythe negative charges and the formation of lysinoalanine, lanthion-ine and dehydroalanine-derived cross-links stimulated with alkaliat moulding temperatures exceeding 130◦C Jansens et al. (2013).Thus, the highest values of both max, Young’s Modulus are foundat pH 9. Furthermore, εmaxis higher than the value obtained at pH 6 but differences are not significant due to the data dispersion. Zhanget al. (2008) reported similar evolution of these tensile parameters as a function of acid or alkali content for compression-mouldedgluten bioplastics.As may be observed in Fig. 6, the same behaviour takes place when LBG is present such that the results found at pH 3 and pH 6 are similar to those of the polysaccharide-free specimens. However,the above mentioned enhancement of tensile properties reportedfor LBG-free samples at pH 9 is inhibited by the presence of LBG,which may be related to some crosslinking inhibition effects.Consistent with DMTA results, the thermodynamic incompat-ibility between WG proteins and LBG, due to the segregative separation phenomenon, seems to induce a decrease in the bio-plastic elongation at break (εmax), if compared to their reference systems.