A review of protein-phenolic acid interaction: reaction mechanisms and applications.

Phenolic acids (PA) are types of phytochemicals with health benefits. The interaction between proteins and PAs can cause minor or extensive changes in the structure of proteins and subsequently affect various protein properties. This study investigates the protein/PA (PPA) interaction and its effects on the structural, physicochemical, and functional properties of the system. This work particularly focused on the ability of PAs as a subgroup of phenolic compounds (PC) on the modification of proteins. Different aspects including the influence of structure affinity relationship and molecular weight of PA on the protein interaction have been discussed in this review. The physicochemical properties of PPA change mainly due to the change of hydrophilic/hydrophobic parts and/or the formation of some covalent and non-covalent interactions. Furthermore, PPA interactions affecting functional properties were discussed in separate sections. Due to insufficient studies on the interaction of PPAs, understanding the mechanism and also the type of binding between protein and PA can help to develop a new generation of PPA. These systems seem to have good capabilities in the formulation of low-fat foods like high internal Phase Emulsions, drug delivery systems, hydrogel structures, multifunctional fibers or packaging films, and 3 D printing in the meat processing industry.

Pectin modification assisted by nitrogen glow discharge plasma.

This study is concerned with modification of high methoxy pectin (HMP) assisted by nitrogen AC glow discharge plasma. Intrinsic viscosity of plasma treated pectin (PTP) was measured as primary index for structural changes in pectin molecules at different plasma conditions. The intrinsic viscosity of pectin increased within 7 min of exposure to plasma treatment and then remained constant. According to Fourier Transform Infrared Spectrometry (FT-IR) analysis, the intensity of carboxylate peaks increased in PTP samples due to de-esterification of pectin. Moreover, by decreasing the degree of esterification (DE) in PTP samples, the results of FT-IR were confirmed. Based on high performance size-exclusion chromatography (HPSEC) analysis, the molecular weight of PTP reduced. PTP gel had higher storage and loss modulus and shorter linear viscoelastic region. Moreover, X-ray diffraction (XRD) studies indicated an increase of crystallinity in PTP due to the formation of hydrogen bonds. Results revealed that nitrogen AC glow discharge plasma had significant influence on physicochemical and functional properties of pectin. The result of this study showed AC glow discharge plasma has promising potential towards modification of pectin.

Acid-induced gelation behavior of casein/whey protein solutions assessed by oscillatory rheology.

Gelation process of acid-induced casein gels was studied using response surface method (RSM). Ratio of casein to whey proteins, incubation and heating temperatures were independent variables. Final storage modulus (G') measured 200 min after the addition of glucono-δ-lactone and the gelation time i.e. the time at which G' of gels became greater than 1 Pa were the parameters studied. Incubation temperature strongly affected both parameters. The higher the incubation temperature, the lower was the G' and the shorter the gelation time. Increased heating temperature however, increased the G' but again shortened the gelation time. Increase in G' was attributed to the formation of disulphide cross-linkages between denatured whey proteins and casein chains; whilst the latter was legitimized by considering the higher isoelectric pH of whey proteins. Maximum response (G' = 268.93 Pa) was obtained at 2.7 % w/w, 25 °C and 90 °C for casein content, incubation and heating temperatures, respectively.