Chemical lipophilization of soy protein isolates and wheat gluten

Preparation and Thermoplastic Processing of Modified Plant Proteins

“…The decrease in water uptake of proteins, and thereby the dependence of properties on the water content, is an important aspect of research on technical applications of proteins. Different ways of binding hydrophobic groups or modifying protein hydrophobicity are described in literature, for instance acylation by fatty acid derivatives and N ‐hydroxysuccinimide esters,24–27 reductive alkylation28 and reactions inserting hydrophobic amino acids or alcohols 29,30. Obviously, the nature and chain length of the hydrophobic groups bound to proteins are directly linked to the final structural and functional properties of so modified proteins.…”

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

“…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 ].…”

“…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 ]. Therefore, an induced increase in protein hydrophobicity can enable its integration into lipid systems and, consequently, trigger new, as well as ameliorated or impaired, functional properties [ 6 , 8 ].…”

“…Protein lipophilization reaction is defined as a chemical or enzymatic structural change of a polypeptide chain by the addition of lipid components, carried out with several different methods and resulting in biomacromolecules with an increased affinity towards non-polar compounds of low or high molecular mass. Acylation by N-hydroxysuccinimide ester, acetic, succinic, or citraconic anhydrides [ 9 , 10 , 11 , 12 , 13 ], fatty acid chlorides [ 6 ] or reductive alkylation [ 14 ], as well as by attaching hydrophobic amino acids or alcohols [ 15 , 16 , 17 , 18 ], are the most frequently used experimental procedures to obtain protein lipophilization. In particular, the chemical acylation of a protein is a quite considerable structural modification that can dramatically influence the ability of the protein to interact with other molecules and, consequently, modify its activity.…”

Effect of Lipophilization on the Antioxidant Activity of Carvacrol, Quercetin and Vanillin With Conjugated Linoleic Acid

“…Lipophilization is the modification of a substrate via esterification with a lipophilic moiety, resulting in a new molecule with greater affinity to non-polar compounds and with a modified HLB (Figueroa-Espinoza and Villeneuve, 2005). This reaction can be carried out by different methods, including N-hydroxysuccinamide esters (Haque et al, 1982), succinic or acetic anhydrides (Messinger et al, 1987) or fatty acid chlorides (Roussel-Philippe et al, 2000). However, there are unproven reactions, such as Fischer esterification, which is a type of simple esterification involving the formation of a hydroxyl group ester and a carboxyl in the presence of an acid catalyst (Offenhauer, 1964).…”