Rye secalin characterisation and use to improve zein‐based film performance

Abstract

Use of rye secalin for preparation of secalin/zein blend film.

Fabrication of κ‐carrageenan and whey protein isolate‐based films reinforced with nanocellulose: optimization via RSM

“…The elasticity of film samples including lower whey protein and glycerol contents was not significantly affected by N inclusion; however, the increase in N content resulted in higher E values for higher whey protein and glycerol amounts. Similarly, Qazanfarzadeh and Kadivar demonstrated that whey protein films including a high level of nanocellulose from oat husk (7.5 wt %) resulted in higher elongation at break values due to agglomeration of the fillers. On the other hand, film samples containing higher carrageenan presented higher elasticity when the G/S ratio was increased due to reduced tension of deformation and electrostatic charge.…”

Functional Properties of Rye Prolamin (Secalin) and Their Improvement by Protein Lipophilization through Capric Acid Covalent Binding

“…Tukey test was used to compare the mean at a 95% confidence level. Figure 1 shows that the extracted SCL exhibited the well-known protein electrophoretic profile containing four fractions (HMW, γ-75 KDa, ω, and γ-45 KDa) [4]. It is well known that all nucleophilic groups of protein amino acid residues, such as amino, hydroxyl, sulfhydryl, and phenol groups, can be acylated by fatty acid chlorides [25].…”

“…However, prolamin occurring in rye grains, and alcohol-soluble protein fraction called secalin (SCL), has not been so widely studied up to now, in relation to its functionality in food systems, as wheat prolamin has been. According to previous studies, the electrophoretic pattern of SCL shows four groups of polypeptides, indicated as high molecular weight (HMW, >100 KDa), γ-75 KDa, ω (50 KDa), and γ-40 KDa proteins, respectively [ 4 ]. Moreover, quantitative amino acid analysis evinced that glutamic acid and proline are the predominant components in SCL, followed by leucine, phenylalanine, and serine [ 4 ].…”

“…According to previous studies, the electrophoretic pattern of SCL shows four groups of polypeptides, indicated as high molecular weight (HMW, >100 KDa), γ-75 KDa, ω (50 KDa), and γ-40 KDa proteins, respectively [ 4 ]. Moreover, quantitative amino acid analysis evinced that glutamic acid and proline are the predominant components in SCL, followed by leucine, phenylalanine, and serine [ 4 ]. Because of the SCL amphiphilic behavior due to the presence of wide regions of protein β-sheets, ethanol (70% v / v ) is the most common solvent used for its extraction.…”

“…In addition, ethanol leads to the unfolding of the α-helical structures increasing the extent of the β sheets and, consequently, exposing a greater number of hydrophilic groups of the protein. It is worthy to note that the β-sheet structural feature could influence SCL functional properties, i.e., those conferred by the protein to a food product [ 2 , 3 , 4 , 5 , 6 ] as the protein hydrophobic behavior and hence its interactions with the aqueous phase are important factors for the protein functionality. Furthermore, it is well known that protein secondary and tertiary structure may change following a chemical modification able to cause alterations in the surface exposure of their amino acids [ 7 ].…”