Amino Acid Composition, Antioxidant and Antihypertensive Activity in Extracts from Mexican Añejo Cheese.

Research Background: Authentic Mexican cheeses have potential health benefits, although there are few studies on their bioactive components. In this study, we analysed soluble extracts from añejo cheese from Zacazonapan (Mexico), obtained from two dairies (A and B) that used milk from cows of different breeds and differed in processing.

Experimental Approach: The soluble extracts of Zacazonapan añejo cheese during ripening (0, 30, 95 and 180 days) were used to determine proximate composition, amino acid composition, peptide profile, molecular mass profile, antioxidant and antihypertensive activities.

Purification, Characterization, and Antiproliferative Activity of a Single-Chain Lectin from Vicia palaestina (Fabaceae) Seeds.

Vicia palaestina Boiss. is an annual herb that grows in dry areas of eastern Mediterranean countries. It belongs to section Cracca subgenus Vicilla, which is characterized by having a high content in the non-protein amino acid canavanine.

Physicochemical characteristics and antiproliferative and antioxidant activities of Moroccan Zantaz honey rich in methyl syringate.

Zantaz honey is a monofloral variety produced from the melliferous plant Bupleurum spinosum (Apiaceae), a shrub that grows mainly in the Atlas Moroccan Mountains. Determination of the polyphenol composition revealed that methyl syringate accounts for more than 50% of total polyphenols, which represents a very useful parameter for the characterization of this monofloral honey. Epicatechin, syringic acid and catechin are also abundant.

Characterization of Vicia ervilia (bitter vetch) seed proteins, free amino acids, and polyphenols.

Vicia ervilia is an ancient crop from the Mediterranean Region. It may represent a useful source of proteins for food and animal feed, as well as bioactive components. Seed samples from 39 populations of V.

Pectin-rich extracts from olives inhibit proliferation of Caco-2 and THP-1 cells.

Three olive modified pectin extracts have been produced by heat and acid treatment of the major by-product of olive oil production. Their effect on proliferation of the colon carcinoma Caco-2 and the leukemia monocytic THP-1 cell lines has been studied in order to determine possible anti-tumor properties. All extracts inhibited proliferation at some of the concentrations ranging from 1 to 10 mg ml.

Purification of free arginine from chickpea (Cicer arietinum) seeds.

Chickpea is a grain legume widely consumed in the Mediterranean region and other parts of the world. Chickpea seeds are rich in proteins but they also contain a substantial amount of free amino acids, especially arginine. Hence chickpea may represent a useful source of free amino acids for nutritional or pharmaceutical purposes.

Influence of peptides-phenolics interaction on the antioxidant profile of protein hydrolysates from Brassica napus.

The role of the peptides-phenolic compounds (PC) interaction on the antioxidant capacity profile (ACP) of protein hydrolysates from rapeseed (Brassica napus) was studied in 36 hydrolysates obtained from a PC-rich and PC-reduced protein substrate. The latent profile analysis (LPA), with data of seven in vitro methods and one assay for cellular antioxidant activity (CAA), allowed identifying five distinctive groups of hydrolysates, each one with distinctive ACP. The interaction of peptides with naturally present PC diminished in vitro antioxidant activity in comparison with their PC-reduced counterparts.

Determination of β -Cyano-L-alanine, γ -Glutamyl- β -cyano-L-alanine, and Common Free Amino Acids in Vicia sativa (Fabaceae) Seeds by Reversed-Phase High-Performance Liquid Chromatography.

A method for determination of β-cyano-L-alanine, γ-glutamyl-β-cyano-L-alanine and other free amino acids in Vicia sativa is presented. Seed extracts were derivatized by reaction with diethyl ethoxymethylenemalonate and analyzed by reverse-phase high-performance liquid chromatography. Calibration curves showed very good linearity of the response.

Determination of L-canavanine and other free amino acids in Vicia disperma (Fabaceae) seeds by precolumn derivatization using diethyl ethoxymethylenemalonate and reversed-phase high-performance liquid chromatography.

A method for determination of the non-protein amino acid l-α-amino-γ-(guanidinooxy)-n-butyric acid (L-canavanine) and other free amino acids in Vicia disperma is presented. Seed extracts were derivatized by reaction with diethyl ethoxymethylenemalonate and analyzed by reverse-phase high-performance liquid chromatography. Calibration curves showed very good linearity of the response.

Antioxidant and metal chelating activities of peptide fractions from phaseolin and bean protein hydrolysates.

Bean protein isolate and phaseolin were hydrolysed using pepsin and pancreatin, and the resulting hydrolysates were filtered through a 1kDa cut-off membrane and fractionated by size exclusion chromatography. Three fractions corresponding to MW 0.7-1.

Nutritional quality of protein in the leaves of eleven Asphodeline species (Liliaceae) from Turkey.

The nutritional quality of the protein in the leaves of 11 Asphodeline (Liliaceae) species was investigated by the determination of the amino acid composition and calculation of several nutritional parameters. The average protein content was 4.7% and ranged from 2.

Angiotensin-converting enzyme-inhibitory activity in protein hydrolysates from normal and anthracnose disease-damaged Phaseolus vulgaris seeds.

Background: Bean seeds are an inexpensive source of protein. Anthracnose disease caused by the fungus Colletotrichum lindemuthianum results in serious losses in common bean (Phaseolus vulgaris L.) crops worldwide, affecting any above-ground plant part, and protein dysfunction, inducing the synthesis of proteins that allow plants to improve their stress tolerance.

Nutritional and functional properties of Vicia faba protein isolates and related fractions.

The goal of this research was the characterisation of Vicia faba (broadbean) protein isolates and related fractions in order to determine whether this grain legume could be used for production of high quality protein products and other fractions rich in functional components. Alkaline extraction of the defatted seed flour, followed by precipitation at the isoelectric pH, yielded a 92% protein isolate with a high oil absorption capacity. The contents of the favism-inducing glycosides, vicine and convicine, in the isolate were reduced by more than 99% as compared to the original flour, although the amino acid composition was similar to that of the flour.

Hemagglutinating activity of polyphenols extracts from six grain legumes.

The erythrocyte agglutinating activity of polyphenol extracts from six grain legumes was investigated. Polyphenols are amphipathic molecules that can bind to proteins and lipids through hydrophobic and polar interactions, leading to agglutination of liposomes and bacteria. The extracts from four of the six legumes that were studied caused erythrocyte agglutination at concentrations in the μM range.

Antioxidant and chelating activity of Jatropha curcas L. protein hydrolysates.

Background: Antioxidant and chelating activities were determined in protein hydrolysates that were produced by treating a protein isolate of a non-toxic genotype of Jatropha curcas with the protease preparation alcalase.

Results: 50 min protein hydrolysate with a degree of hydrolysis of 31.7% showed highest antioxidant and chelating activity.

Sunflower protein hydrolysates reduce cholesterol micellar solubility.

Plant protein hydrolysates are a source of bioactive peptides. There are peptides that decrease the micellar cholesterol solubility from bile acids and therefore may reduce in vivo cholesterol absorption. The presence of these peptides in sunflower protein hydrolysates has been studied.

Chickpea protein hydrolysate as a substitute for serum in cell culture.

The growth of mammalian cells in vitro requires the use of rich culture media that are prepared by combining serum with specific nutrient formulations. Serum, the most expensive component of culture media, provides a complex mixture of growth factors and nutrients. Protein hydrolysates that can support in vitro cell growth and eliminate or reduce the need to use serum have been obtained from different sources.

Affinity purification of copper-chelating peptides from sunflower protein hydrolysates.

Copper-chelating peptides were purified from sunflower protein hydrolysates by affinity chromatography using immobilized copper. A variety of protein hydrolysates were obtained by incubation with the proteases Alcalase and Flavourzyme for different periods of time. Chelating activity was indirectly determined by measuring the inhibitory effect of hydrolysates on the oxidation of beta-carotene by copper.

Partial purification and immobilization/stabilization on highly activated glyoxyl-agarose supports of different proteases from flavourzyme.

The fractioning of some components and their immobilization of Flavourzyme, a commercial protease/aminopeptidase preparation, has been investigated to improve its specificity and stability. Adsorption of Flavourzyme on two ionic exchangers yielded two fractions with endoprotease activity and one fraction containing aminopeptidase activity. The use of an amine agarose gel has made it possible to purify a 43 kDa protein with only endoprotease activity.

Affinity purification of copper chelating peptides from chickpea protein hydrolysates.

Chickpea protein hydrolysates obtained with alcalase and flavourzyme were used for purification of copper chelating peptides by affinity chromatography using copper immobilized on solid supports. The chelating activity of purified peptides was indirectly measured by the inhibition of beta-carotene oxidation in the presence of copper. Two protein hydrolysates, obtained after 10 and 100 min of hydrolysis, were the most inhibitory of beta-carotene oxidation.

Production of Brassica carinata protein hydrolyzates with a high Fischer's ratio using immobilized proteases.

Brassica carinata protein isolates were hydrolyzed using the digestive enzymes trypsin, chymotrypsin, and carboxypeptidase A in order to obtain hydrolyzates with a high Fischer's ratio. The proteases were immobilized using two glyoxyl-agarose supports of different porosity, 4 and 10% agarose gels, in order to evaluate the effect of substrate diffusion into the support containing the enzyme on the hydrolytic process. Reaction time, substrate concentration, and the enzyme to substrate ratio were optimized in an attempt to increase the Fischer's ratio in the resulting hydrolyzates.

Affinity purification of angiotensin converting enzyme inhibitory peptides using immobilized ACE.

A lung extract rich in angiotensin converting enzyme (ACE) and pure ACE were immobilized by reaction with the activated support 4 BCL glyoxyl-agarose. These immobilized ACE derivatives were used for purification of ACE inhibitory peptides by affinity chromatography. The immobilized lung extract was used to purify inhibitory peptides from sunflower and rapeseed protein hydrolysates that had been obtained by treatment of protein isolates with alcalase.

Immobilization of angiotensin-converting enzyme on glyoxyl-agarose.

The assay of angiotensin-converting enzyme (ACE) inhibition by food-derived peptides is usually carried out by using soluble ACE in a batch process. The purification of this enzyme from tissues is not an easy task, and the resulting preparation loses activity very fast. In addition, ACE commercial preparations are very expensive.

Effect of chickpea aqueous extracts, organic extracts, and protein concentrates on cell proliferation.

Pulses should be part of a healthy diet, and it is also becoming clear that they have health-promoting effects. Nevertheless, most studies on the bioactive or health-promoting properties of pulses have been carried out using soybeans. We have studied cell growth-regulating properties, which may be responsible for anti-cancer properties, in chickpea seeds.

Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates.

Sunflower protein isolates and the proteases pepsin and pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Hydrolysates obtained after 3 h of incubation with pepsin and 3 h with pancreatin were studied. An ACE inhibitory peptide with the sequence Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser was obtained by G-50 gel filtration chromatography and high-performance liquid chromatography C18 reverse phase chromatography.