Amino acid composition and antioxidant properties of the enzymatic hydrolysate of calabash nutmeg (
Monodora myristica
) and its membrane ultrafiltration peptide fractions
Abstract:The aim of this work was to determine amino acid composition and in vitro antioxidant activities of Monodora myristica protein hydrolysate and its membrane ultrafiltration peptide fractions. The Alcalase hydrolysate was fractionated using ultrafiltration membranes to produce peptide sizes of <1, 1-3, 3-5, and 5-10 kDa. The results showed that sequential fractionation resulted in higher glycine and glutamic acid and glutamine contents. Analysis of in vitro antioxidant properties showed that fractionation of the… Show more
“…The amino acid composition of protein hydrolysates and peptides has been closely correlated with their antioxidant activity ( 51 ). It is reported that protein hydrolysates and/or peptides containing amino acid residues such as valine (Val), alanine (Ala), leucine (Leu), phenylalanine (Phe), tryptophan (Trp), methionine (Met), aspartic acid (Asp), proline (Pro), and histidine (His) show higher antioxidant ability ( 52 ).…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, it shows activity in the OH radical scavenging experiment in this paper. Moreover, according to Piu et al ( 53 ) and Akinyede et al ( 51 ), acidic or basic amino acids, like Asp, Glu, Arg, and the presence of His residue containing imidazole ring, which was responsible for metal chelation through enhancing electrostatic and ionic interactions with iron. In summary, the presence of these amino acids makes A-BRPH could, to some extent, exert different antioxidant properties in different oxidative systems.…”
Excessive reactive oxygen species (ROS) is an important cause of aging, and supplementing antioxidants through diet is one of the important ways to delay aging. Some studies have confirmed that rice protease hydrolysate has antioxidant activity, but was rarely been investigated on cells. Thus, commercial enzymes, alkaline enzyme, neutral enzyme, pepsin, chymotrypsin, and trypsin were selected to hydrolyze broken rice protein (BRP) to obtain the corresponding hydrolysates, which were A-broken rice protein hydrolysate (BRPH), N-BRPH, P-BRPH, C-BRPH, and T-BRPH, respectively. Then the antioxidant properties of BRPHs were evaluated by different chemical and cellular antioxidation. Molecular weight, peptide length distribution, and amino acid sequence were detected to insight into the antioxidant properties. Among BRPHs, the A-BRPH displayed the strongest hydroxyl radical scavenging activity (IC50 = 1.159 mg/ml) and metal ion-chelating activities (IC50 = 0.391 mg/ml). Furthermore, cellular antioxidation confirmed that A-BRPH significantly increased cell viability and inhibited the intracellular ROS release in both aging cells and cell-aging processes. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results revealed that peptides with molecular weight <14.5 KDa were produced by enzymatic hydrolysis. Additionally, A-BRPH rich in low molecular weight (<3 kDa) and short-length peptides with some specific amino acids, such as aromatic and hydrophobic amino acids, contributes to the antioxidant properties. This study provided theoretical to the utilization of broken rice and confirmed that A-BRPH could be used in new anti-aging food and health products for human consumption.
“…The amino acid composition of protein hydrolysates and peptides has been closely correlated with their antioxidant activity ( 51 ). It is reported that protein hydrolysates and/or peptides containing amino acid residues such as valine (Val), alanine (Ala), leucine (Leu), phenylalanine (Phe), tryptophan (Trp), methionine (Met), aspartic acid (Asp), proline (Pro), and histidine (His) show higher antioxidant ability ( 52 ).…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, it shows activity in the OH radical scavenging experiment in this paper. Moreover, according to Piu et al ( 53 ) and Akinyede et al ( 51 ), acidic or basic amino acids, like Asp, Glu, Arg, and the presence of His residue containing imidazole ring, which was responsible for metal chelation through enhancing electrostatic and ionic interactions with iron. In summary, the presence of these amino acids makes A-BRPH could, to some extent, exert different antioxidant properties in different oxidative systems.…”
Excessive reactive oxygen species (ROS) is an important cause of aging, and supplementing antioxidants through diet is one of the important ways to delay aging. Some studies have confirmed that rice protease hydrolysate has antioxidant activity, but was rarely been investigated on cells. Thus, commercial enzymes, alkaline enzyme, neutral enzyme, pepsin, chymotrypsin, and trypsin were selected to hydrolyze broken rice protein (BRP) to obtain the corresponding hydrolysates, which were A-broken rice protein hydrolysate (BRPH), N-BRPH, P-BRPH, C-BRPH, and T-BRPH, respectively. Then the antioxidant properties of BRPHs were evaluated by different chemical and cellular antioxidation. Molecular weight, peptide length distribution, and amino acid sequence were detected to insight into the antioxidant properties. Among BRPHs, the A-BRPH displayed the strongest hydroxyl radical scavenging activity (IC50 = 1.159 mg/ml) and metal ion-chelating activities (IC50 = 0.391 mg/ml). Furthermore, cellular antioxidation confirmed that A-BRPH significantly increased cell viability and inhibited the intracellular ROS release in both aging cells and cell-aging processes. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results revealed that peptides with molecular weight <14.5 KDa were produced by enzymatic hydrolysis. Additionally, A-BRPH rich in low molecular weight (<3 kDa) and short-length peptides with some specific amino acids, such as aromatic and hydrophobic amino acids, contributes to the antioxidant properties. This study provided theoretical to the utilization of broken rice and confirmed that A-BRPH could be used in new anti-aging food and health products for human consumption.
“…Cit has the characteristics of a hydroxyl radical scavenger [ 51 ]. Glutamic acid and histidine decreased the generation of the hydroxyl radicals [ 52 ]. Hwang et al demonstrated a strong antioxidant activity of methionine and lysine [ 53 ].…”
Rosa roxburghii Tratt. is a specific fruit with high nutritional value and antioxidative activities. However, the key metabolites and their biosynthesis are still unknown. Herein, a main cultivated variety, ‘Guinong 5’ (Rr5), was chosen to analyze the metabolomics of the three developmental stages of R. roxburghii fruit by liquid chromatography–tandem mass spectrometry (LC-MS/MS). A total of 533 metabolites were identified, of which 339 were significantly altered. Total phenols, flavonoids, and amino acids were significantly correlated to at least one in vitro antioxidant activity. The conjoint Kyoto Encyclopedia of Genes and Genomes (KEGG) co-enrichment analysis of metabolome and transcriptome was focused on amino acid, phenylpropanoid, and flavonoid biosynthesis pathways. The amino acid, phenolic acid, and flavonol biosynthesis networks were constructed with 32 structural genes, 48 RrMYBs, and 23 metabolites. Of these, six RrMYBs correlated to 9–15 metabolites in the network were selected to detect the gene expression in six different R. roxburghii genotypes fruits. Subsequently, 21 key metabolites were identified in the in vitro antioxidant activities in the fruits at various developmental stages or in fruits of different R. roxburghii genotypes. We found that four key RrMYBs were related to the significantly varied amino acids, phenolic acids, and flavonol derivatives in the network during fruit development and the key metabolites in the in vitro antioxidative activities in the fruits of six R. roxburghii genotypes. This finding provided novel insights into the flavonoid, polyphenol, and amino acid synthesis in R. roxburghii.
“…Among them, SHP2 was significantly stronger than SHP4 and SHP5 at the same concentration, but lower than GSH. In biological systems, antioxidants inhibit the continuous oxidation reactions as reducing reagents, and the capacity is positively related to their antioxidant activity [48]. The result showed that SHP2 can be used to reduce the oxidation intermediates in the lipid peroxidation reaction of organisms as reducing reagents.…”
Section: Reducing Powermentioning
confidence: 99%
“…Furthermore, the component and sequences of amino acids were also important factors that could affect antioxidant activity. Some hydrophobic amino acids, such as methionine (Met), tryptophan (Trp), valine (Val), proline (Pro), alanine (Ala), leucine (Leu) or phenylalanine (Phe), can play a significant role in antioxidant peptides [48,54], through increasing the solubility of peptides in lipids and enhancing the interaction with oxidant substances. Ketnawa et al [55] believed that if the peptides contain high proportions of aromatic amino acids (His, Trp) or Leu, Ala and Pro, they could directly transfer electrons, and hence they are always linked to strong antioxidant activity.…”
Section: The Relationship Between Structure and Activitymentioning
In this study, an alkaline protease BaApr1 from the Bacillus altitudinis W3 was chosen to hydrolysis grass carp (Ctenopharyngodon idella) scales. The hydrolysate of alkaline protease BaApr1 exhibited the best antioxidant activity compared to other protease hydrolysates. The optimal hydrolysis conditions for BaApr1 were an enzyme dosage of 1250 U/g, a hydrolysis time of 7 h, a pH of 9.5 and a temperature of 50 °C. Three novel peptides were purified using ultrafiltration, anion exchange chromatography, gel filtration chromatography and ultra-performance liquid chromatography, and their sequences were identified
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