Redox agents and N-ethylmaleimide affect the extractability of gluten proteins during fresh pasta processing

The gluten protein network is of great importance for pasta cooking quality. Redox agents were used as a tool to impact the protein network formation during laboratory scale fresh pasta making (mixing and sheet rolling) and cooking. SE- and RP-HPLC data showed that disulphide bonds are formed in the pre-existing gluten protein network during cooking of fresh pasta and that, in the process, glutenin polymerisation occurs faster than gliadin–glutenin copolymerisation. The thiol blocking agent N-ethylmaleimide (245 ppm, expressed on semolina, dry basis) and, to a lesser extent, the oxidising agent potassium iodate (70 ppm), hindered glutenin polymerisation and gliadin–glutenin copolymerisation during cooking. However, the introduction of reactive thiol groups, by addition of the reducing agent glutathione (100 ppm), resulted in faster gliadin–glutenin copolymerisation during cooking.     

The molecular weight,solubility and viscosity of oat beta-glucan affect human glycemic response by modifying starch digestibility

The interaction between oat β-glucan and other food components has the potential to influence starch digestibility and consequently affect its bioactivity in reducing glycemic responses. Blood glucose concentrations were measured before and after ingesting wheat and oat granolas, with 0.6 and 6.2 g of β-glucan, respectively, and two starch doses (40 and 60 g). As the in vitro extract viscosity of β-glucan increased, the in vitro starch digestibility was reduced and the glucose responses were lowered. The peak blood glucose response (PBGR) and the incremental area under the curve (iAUC) were lower in the 40 g than in the 60 g starch formulation. β-Glucan was significantly more active in reducing PBGR and iAUC when the β-glucan/starch ratio was 1.6:10 rather than 1.1:10. This information is valuable for new product development and for quality assessment of bioactive foods containing oat β-glucan.     

Glycosylation,amino acid analysis and kinetic properties of a major Kunitz-type trypsin inhibitor from Acacia victoriae Bentham seeds

An Acacia victoriae trypsin inhibitor (AvTI) was purified from the seeds of prickly wattle (A. victoriae Bentham) by salt precipitation, ion-exchange and gel filtration chromatography, and its degree of glycosylation, amino acid composition, and kinetic properties were determined. Gel electrophoresis revealed at least four glycoprotein bands in the crude extract, salt-precipitated and ion-exchange protein fractions, while the purified AvTI showed only one band and a degree of glycosylation of 2.06%. Glutamate (13.3%), aspartate (10.3%), leucine (7.62%) and lysine (7.01%) were the major amino acids in AvTI while the contents of sulphur-containing amino acids, cysteine (1.38%) and methionine (0.75%), as well as of tryptophan (1.17%) were low. Its dissociation constant (K_i) for the inhibition of bovine trypsin was found to be 1.06 × 10⁻⁸ M, indicating a high affinity between AvTI and this enzyme, and its role as a competitive inhibitor was confirmed by a double reciprocal plot. These results complement our earlier studies which indicated the presence of three isoforms of this Kunitz-type trypsin inhibitor in prickly wattle seed.