Conformational Changes and Some Functional Characteristics of Gelatin Esterified with Fatty Acid

Abstract

This study investigated the effects of attachment of fatty acid chains to gelatin molecules on their conformation and some functional properties in order to determine the effectiveness of this procedure for improving the emulsifying properties of gelatin. The esterification conferred upon the gelatin molecules a folded configuration resulting in a lambda(max) of fluorescence emission shift to lower wavelengths and decreases in solubility, intrinsic viscosity, and gelling ability. In contrast, surface hydrophobicity increased with extent of esterification, and the esterified derivatives exhibited higher emulsion stabilities. These results indicated that the oligomeric structure and functional attributes of the gelatin were altered with the modification.

Characterization of soy protein-based films prepared with acids and oils by compression

“…This behaviour indicates that surfaces of the films differed depending on the type of additive. In the case of oils, some authors (Djagny et al, 2001;Quiroga et al, 2010) stated that, depending on the size of the molecule, large contents of oils led to partial changes of the protein configuration, reducing hydrophilic groups on the surface, so thus increasing the hydrophobic character. This fact could explain the behaviour of the smaller molecule of OO related to ESO.…”

Physical, mechanical and water barrier properties of yuba films incorporated with various types of additives

“…For BW, the lowered contact angle might be explained by esterification reaction of BW. Its hydrophobic groups aggregate toward interior of the polymer, resulting in a decreased value of contact angle . Blending S with SP decreased the contact angle to 64.8° in SPS, whereas blending G with CMC increased the contact angle to 66.9° in CMCG ( P < 0.05).…”

Application Potential of Food Protein Modification

“…Increased exposed hydrophobicity of proteins has for example been related to an improved capacity to form and stabilize emulsions and foams which is the result of improved potential to interact with hydrophobic surfaces, both the air-water and oil-water interface, and including (model)membranes (Nakai, 1983;Wierenga et al, 2003;reviewed in Wilde, 2000;Wilde et al, 2004). Various saturated and unsaturated fatty acids have been employed to induce lipophilization of proteins including caproic acid (Liu et al, 2000), capric acid (Aewsiri et al, 2010;Liu et al, 2000), lauric acid (Aewsiri et al, 2010), myristic acid (Aewsiri et al, 2010;Ibrahim et al, 1993;Liu et al, 2000), palmitic acid (Haque et al, 1982;Haque & Kito, 1983a, 1983bIbrahim et al, 1991), stearic acid (Djagny et al, 2001;Ibrahim et al, 1993), and oxidized forms of linoleic acid (Aewsiri et al, 2011a(Aewsiri et al, , 2011b, and the efficiency of the lipophilization reaction was found to be inversely proportional to the length of the lipid chains used (Liu et al, 2000). Reaction of 28% of the available free amino groups of ovalbumin with activated capric acid was shown to result in retained secondary structure while inducing oligomerization and destabilization of the protein structure as a result of lowering the enthalpy for unfolding .…”