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.     

Application of high density steam flash-explosion in protein extraction of soybean meal

The high density steam flash-explosion (HDSFE) was used to extract protein from soybean meal. Soybean meal samples were treated at 1.3 MPa and 1.8 MPa for 60 s, 120 s and 180 s, respectively. After HDSFE treatment at 1.8 MPa for 180 s, the extraction yield of protein was increased from 50.50% to 65.66% compared with untreated soybean meal. The emulsification properties and fat-binding capacity of soy protein isolate (SPI) extracted from soybean meal treated by HDSFE were all improved compared with SPI extracted from untreated soybean meal and white flakes. Molecular weight distribution analysis of SPI showed that after HDSFE treatment the peak with molecular weight about 504 kDa and 43.3 kDa disappeared and the peak with molecular weight about 669 kDa increased indicating protein aggregation. Gel electrophoresis showed that high molecular weight aggregates of protein have been formed by covalent bond.     

Physicochemical and structural characterisation of protein isolate,globulin and albumin from soapnut seeds (Sapindus mukorossi Gaertn.)

The amino acid (AA) composition and physicochemical and conformational properties of protein isolate (SNPI), globulin (SNG) and albumin (SNA) fractions from soapnut seeds were evaluated. The essential AA of SNG, SNA and SNPI (except sulfur-containing AA) are sufficient for the FAO/WHO suggested requirements for 2–5 year old infants. SNG and SNPI showed similar electrophoresis patterns and AA compositions, the subunit of those proteins consisted of two polypeptides linked by disulfide bonds. In contrast, SNA showed a different AA compositions and SDS–PAGE pattern. Both SNG and SNPI presented a typical U-shape protein solubility (PS)–pH profile, SNA showed a completely different PS–pH profile, especially at pH 2.0–4.0. The near-UV circular dichroism (CD), differential scanning calorimetry (DSC) and tryptophan fluorescence spectra analyses indicated that the flexibility in tertiary conformations decreased in the order: SNA > SNPI > SNG, while soapnut proteins had a similar secondary conformation, with a highly ordered structure (the β-types), as evidenced by far-UV CD spectra.