Studies on Antioxidative Activities of Amino Compounds on Fats and Oils

Yamaguchi, Naohiko; Yokoo, Yoshio; Fujimaki, Masao

doi:10.3136/nskkk1962.18.313

Cited by 18 publications

(4 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…(Fan et al, 2012;Kawashima et al, 1979;Yamaguchi et al, 1975) Our results were similar to those of previous studies, Peptide C8 contained Tyr at the terminal position. Non-polar aliphatic that of component A3, because the components A3 and B3 were mixed peptides, and all of the two components contained the peptides C8 and C9.…”

Section: Discussionsupporting

confidence: 83%

Purification and Identification of Novel Antioxidant Peptides from Enzymatic Hydrolysate of Ginkgo biloba Seed Proteins

Shi

Fan

et al. 2013

FSTR

View full text Add to dashboard Cite

Ginkgo biloba seed proteins were hydrolyzed using alkali protease and pepsin to obtain antioxidant peptides. Ginkgo biloba antioxidant peptides (GKAPs) were separated by Sephadex G-25 and Sephadex G-10 gel filtration chromatography. The GKAP B3 exhibited highest antioxidant activity. B3 peptide was separated by reversed-phase high-performance liquid chromatography (RP-HPLC), and 2 peptides with good antioxidant activity, i.e., GKAPs C8 and C9, were obtained. The molecular weight and amino acid sequences of the peptides were identified by Liquid chromatography quadrupole time-of-flight mass spectrometry (LC-Q-TOF-MS). The results showed that the molecular mass of GKAP C8 was 452.21 Da and the amino acid sequence was YVGD (Tyr-Val-Gly-Asp), while the molecular mass of GKAP C9 was 988.49 Da and the amino acid sequence was LGNTDYAVH (Leu-Gly-Asn-Thr-Asp-Tyr-Ala-Val-His). GKAPs C8 and C9 exhibited good free radical-scavenging effect and inhibited the autoxidation of the linoleic acid system.Keywords: Ginkgo biloba seed protein, antioxidant peptide, radical scavenging activity, amino acid sequence *To whom correspondence should be addressed. E-mail: sxwucaie@163.com IntroductionIn China, Ginkgo biloba seeds are widely used in traditional medicines and foods. It is rich in vitamin C, riboflavin, carbohydrates, proteins, and many other nutrients (Son and Kim, 1998). The protein content of Ginkgo biloba seed is around 10% (dry mass). Ginkgo biloba seed protein is considered to be a high-quality protein and exhibits strong antioxidant properties (Huang et al., 2010;Zhou et al., 2012). The protein polypeptide chain contains various functional areas that are considered bioactive with respect to antioxidant property. When a protein polypeptide chain was hydrolyzed enzymatically, functional groups within the chain were exposed, and they can exhibit different biological activities (Meisel, 1997;Meisel and Bockelmann, 1999). In recent years, peptides generated from various species including animal and plant sources have been found to possess good antioxidant activity. For example, peptides ACGT and ATAGT from Tibpia frame protein (Fan et al., 2012), peptide LEELEEELEGCE from Bullfrog skin (Qian et al., 2008b), LPHSGY from Alaska Pollock protein hydrolysate (Je et al., 2005), NADFGLNGLEGLA from Giant squid, and LKQELEDLLEKQE from Oyster protein hydrolysate have been reported to possess antioxidant activity (Qian et al., 2008a;Rajapakse et al., 2005). In these studies, the antioxidant activity of peptides was evaluated by scavenging free radicals by in vitro assays using 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging, hydroxyl (•OH) radical, superoxide anion radical (•O 2 ), and determination of antioxidant capacity in linoleic acid system. However, there are few reports on antioxidant peptides from Ginkgo biloba seed peptides. In this research, Ginkgo biloba seed protein was hydrolyzed with alkaline protease 2709 and pepsin to obtain antioxidant peptides. The antioxidant activity of antioxidant peptides were evaluated b...

show abstract

Section: Discussionsupporting

confidence: 83%

Purification and Identification of Novel Antioxidant Peptides from Enzymatic Hydrolysate of Ginkgo biloba Seed Proteins

Shi

Fan

et al. 2013

FSTR

View full text Add to dashboard Cite

show abstract

“…However, cHb antioxidant properties might be associated with antioxidant amino acid residues present in its primary structures, such as Tyr, Met, His, Lys and Trp. The increasing degree of their hydrophobicity is related to their antioxidant properties [6,18,25,38,39,44,45]. Antioxidant activity of protein has been identified in several food proteins, such as soybean protein [6], capelin protein hydrolysates [2], porcine Hb [4], whey protein [34,41] and marine fish protein [39].…”

Section: Introductionmentioning

confidence: 99%

Complete Amino Acid Sequence of Globin Chains and Biological Activity of Fragmented Crocodile Hemoglobin (Crocodylus siamensis)

et al. 2012

View full text Add to dashboard Cite

Hemoglobin, α-chain, β-chain and fragmented hemoglobin of Crocodylus siamensis demonstrated both antibacterial and antioxidant activities. Antibacterial and antioxidant properties of the hemoglobin did not depend on the heme structure but could result from the compositions of amino acid residues and structures present in their primary structure. Furthermore, thirteen purified active peptides were obtained by RP-HPLC analyses, corresponding to fragments in the α-globin chain and the β-globin chain which are mostly located at the N-terminal and C-terminal parts. These active peptides operate on the bacterial cell membrane. The globin chains of Crocodylus siamensis showed similar amino acids to the sequences of Crocodylus niloticus. The novel amino acid substitutions of α-chain and β-chain are not associated with the heme binding site or the bicarbonate ion binding site, but could be important through their interactions with membranes of bacteria.

show abstract

“…A probable mechanism of the antioxidative reaction of protein is the interaction of lipid hydroperoxides with sulphur-containing amino acids, particularly with cystein and methionine [7]. Methionine is thus oxidized in methionine sulphoxide and methionine sulphone which possess an antioxidant activity as well [8]. Insoluble brown pigments are formed by these interactions [g].…”

Section: Resultsmentioning

confidence: 99%

Reaction of Oxidized Lipids with Protein. Part 10. Effect of Protein on the Autoxidation of Phospholipids

Pokorný

Šmidrkalovä

Zwain

et al. 1975

Nahrung

View full text Add to dashboard Cite

Phospholipids are oxidized a t 25 'C and a t 60 "C under the formation of brown pigments significantly more rapidly in mixtures with cellulose than in mixtures with casein of egg albumin. The extent of browning and the difference of reactivities are more pronounced in case of phosphatidylethanolamine, lysophosphatidylethanolamine and phosphatidylserine in mixtures with a low water content than in those containing a higher percentage of water. Oxidized phospholipids arc partially combined with protein in unextractable insoluble lipoprotein complexes.Phospholipids, particularly phosphatidylethanolamine and phosphatidylserine, are easily oxidized by air oxygen, even a t room temperature or in course of cold storage [I]. The reason is a high content of polyunsaturated fatty acids in the phosphatidyl- Hydroperoxides formed as primary oxidation products of phospholipids are rapidly decomposed to brown pigments [3]. Therefore, the determination of the extent of browning is more suitable as a criterion of autoxidation degree of phospholipids than the determination of peroxide value. The production of brown pigments is due to the reaction of secondary carbonylic oxidation products or their free radical precursors with the primary amino group of phosphatidylethanolamine or phosphati-Phospholipids are usually present in food materials in close contact with protein, frequently combined with protein in lipoproteins. Therefore the oxidation products of phospholipids could easily react with the &-amino group of lysine bound in protein instead of reacting with the primary amino group of phosphatidylethanolamine. The mechanism of interactions of oxidized phospholipids is the subject of this study. MaterialEgg yolk phospholipids were isolated after LEA et al. [5]. Phosphatidylethanolaniine and phosphatidylcholine were separated by column chromatography [I]. Lysophosphatidylethanolamine (prepared from egg yolk by enzymic hydrolysis) and phosphatidyl-L-serine (from bovinc brain) were products of Koch-Light Laboratories Ltd., Colnbrook, England. Casein after Hammarsten and microcrystalline cellulose (products of Lachema, n. p., Brno, CSSR) were used as non-lipidic mstriceq.Egg albumin (purity DAB, Erg. Bd. 6) was purified by chromatography on Sephadex G-75. ProcedureThe 10% solution of a phospholipid was mixed with cellulose or protein and the solvent (dicthyl ether or petroleum ether) was removed from the mixture in a vacuum rotating evaporator. The mixture was then stored a t constant temperature in dark and at free access of oxygen. The sample was extracted three times, each time by :shaking I g of the mixture for 20 min with 2 -5 nil of chloroform-methanol ( I : I v/v). The solvent was evaporated from the combined extracts under reduced pressure, the residue was dissolved in chloroform, dried with anhydrous sodium sulphatc, and the colour intensity of the filtrate was measured at 400-4480 nm (Spekol, V E B Carl ZeiB, Jena). I h e wcight of extract was deterinincd after having dried it a t 80 "C in a stream of nitrogen to a const...

show abstract

Studies on Antioxidative Activities of Amino Compounds on Fats and Oils

Cited by 18 publications

References 0 publications

Purification and Identification of Novel Antioxidant Peptides from Enzymatic Hydrolysate of Ginkgo biloba Seed Proteins

Purification and Identification of Novel Antioxidant Peptides from Enzymatic Hydrolysate of Ginkgo biloba Seed Proteins

Complete Amino Acid Sequence of Globin Chains and Biological Activity of Fragmented Crocodile Hemoglobin (Crocodylus siamensis)

Reaction of Oxidized Lipids with Protein. Part 10. Effect of Protein on the Autoxidation of Phospholipids

Contact Info

Product

Resources

About