Inhibition of angiotensin I-converting enzyme by wheat gliadin hydrolysates

A tryptic gliadin hydrolysate was fractionated into peptide fractions, which were assigned to either the central domain (CD) or terminal domains (TD) of gliadins. The domains were expected to contain amino acid (AA) sequences which, when released from the parent protein, inhibit the angiotensin I-converting enzyme (ACE), which plays a key role in regulating blood pressure. A proline (Pro) poor TD related fraction, containing the smallest peptides, showed the highest ACE inhibitory activity (IC₅₀ = 0.33 mg/ml). Additional peptidases were selected based on their in silico predicted ability to release ACE inhibitory peptides. Further hydrolysis of the tryptic hydrolysate fractions with thermolysin, Clarex, Alcalase and Esperase increased ACE inhibitory activities. Immobilised Ni²⁺-ion affinity chromatography (IMAC) purification of a TD related peptide fraction obtained by sequential hydrolysis with trypsin and thermolysin yielded a fraction with an IC₅₀ value of 0.02 mg/ml. This IMAC fraction was enriched in histidine and hydrophobic AA (Pro, Val, Ile, Leu and Phe).     

Foaming properties of tryptic gliadin hydrolysate peptide fractions

A tryptic gliadin hydrolysate was separated into central domain (CD) or terminal domain (TD) related peptide fractions. Whereas the initial foam volume (FV) of CD peptide fractions remained constant as a function of pH, FV of TD peptide fractions increased from acidic to alkaline pH. Foam stability (FS) of CD peptide fractions was maximal near neutral pH. For TD peptide fractions, one fraction showed maximal FS at strongly alkaline pH, while the other showed no clear maximal FS. CD related peptide foams contained higher levels of hydrophobic peptides than the respective solutions, while small differences were observed for TD peptide fractions. Peptide compositions of foams did not vary with pH, indicating that the foaming properties of gliadin peptides are mainly dictated by charges. As the pH dependent foaming properties of TD related peptides resemble best those of gliadin, it was concluded that the pH dependent foaming properties of gliadins are mainly determined by their TDs.     

The breakage susceptibility of raw and parboiled rice: A review

Rice (Oryza sativa L.) is one of the most important cereals in the world. Before it is consumed, it is common to remove the hull, bran and germ from the rough rice kernel which is either parboiled or not. During such processing, rice kernels are subjected to mechanical stresses which cause some rice grains to break. A main challenge of the rice industry is to minimize the quantities of broken rice. We here review the factors impacting the breakage susceptibility of rice kernels. Their tendency to break is primarily determined by fissures, chalkiness, immaturity and rice kernel dimensions, properties which are both cultivar and rice grain history dependent. The intensity of processing of any given rice feedstock determines the actual level of broken rice kernels. If performed properly, parboiling, a three-step hydrothermal treatment consisting of soaking, heating and drying of rough rice, substantially reduces the level of broken kernels.     

Barriers impairing mineral bioaccessibility and bioavailability in plant-based foods and the perspectives for food processing

Abstract

Plant-based foods gain more importance since they play a key role in sustainable, low-meat and healthy diets. In developing countries, these food products, especially legumes and cereals, are important staple foods. Nevertheless, the question arises on how efficient they are to deliver minerals and if it is useful to encourage their consumption to reduce the prevalence of mineral deficiencies? This review paper focuses on the discrepancy between the mineral content and the amount of minerals that can be released and absorbed from plant-based foods during human digestion which can be attributed to several inherent factors such as the presence of mineral antinutrients (phytic acid, polyphenols and dietary fiber) and physical barriers (surrounding macronutrients and cell wall). Further, this review paper summarizes the effects of different processing techniques (milling, soaking, dehulling, fermentation, germination and thermal processing) on mineral bioaccessibility and bioavailability of plant-based foods. The positive impact of these techniques mostly relies on the fact that antinutrients levels are reduced due to removal of fractions rich in antinutrients and/or due to their leaching into the processing liquid. Although processing can have a positive effect, it also can induce leaching out of minerals and a reduced mineral bioaccessibility and bioavailability.     

Extractability and Chromatographic Characterization of Wheat (Triticum aestivum L.) Bran Protein

About 70% of the protein for human consumption is derived from plants, with cereals as the most important source. Wheat bran protein has a more balanced amino acid profile than that of flour. We here for the first time report the amino acid, size exclusion, and SDS‐PAGE profiles of bran Osborne protein fractions (OPFs). Moreover, we also investigated how OPFs are affected when physical barriers which entrap proteins in bran tissues are removed. Albumin/globulin is the most abundant OPF. It is richer in lysine and asparagine/aspartic acid than other OPF. Most bran albumin/globulin proteins have a molecular weight (MW) lower than 30 k and their chromatographic profiles differ from those of flour. The prolamin has high levels of proline and glutamine/glutamic acid. It is rich in proteins with a MW of 30 to 45 k and about 66 k reflecting contamination with gliadin from endosperm. The glutelin has high levels of glycine, proline, and glutamine/glutamic acid. Its protein is of intermediate and high MW with little protein with MW lower than 30 k. The high (MWs from 80 to 120 k) and low (MW around 45 k) MW glutenin subunits of flour are also present in bran. The glutelin of wheat endosperm is named glutenin. Ball milling releases albumin/globulin and glutelin but not prolamin. Not all glutelin was endosperm glutenin as a substantial part was entrapped in the aleurone cells.