scholarly journals Purification and Characterization of Antioxidant Peptides Derived from Protein Hydrolysate of the Marine Bivalve Mollusk Tergillarca granosa

Marine Drugs ◽  
2019 ◽  
Vol 17 (5) ◽  
pp. 251 ◽  
Author(s):  
Xiu-Rong Yang ◽  
Yi-Ting Qiu ◽  
Yu-Qin Zhao ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Protein Hydrolysate ◽  
Cation Radical ◽  
Amino Acid Sequences ◽  
Marine Bivalve ◽  
Antioxidant Peptides ◽  
Food Ingredient ◽  
Molecular Weights ◽  
Ph Conditions ◽  
Blood Cockle

In this report, protein hydrolysate (TGH) of blood cockle (Tegillarca granosa) was prepared using a two-enzyme system (Alcalase treatment for 1.5 h following Neutrase treatment for 1.5 h). Subsequently, six antioxidant peptides were isolated from TGH using ultrafiltration and chromatography methods, and their amino acid sequences were identified as EPLSD, WLDPDG, MDLFTE, WPPD, EPVV, and CYIE with molecular weights of 559.55, 701.69, 754.81, 513.50, 442.48, and 526.57 Da, respectively. In which, MDLFTE and WPPD exhibited strong scavenging activities on DPPH radical (EC50 values of 0.53 ± 0.02 and 0.36 ± 0.02 mg/mL, respectively), hydroxy radical (EC50 values of 0.47 ± 0.03 and 0.38 ± 0.04 mg/mL, respectively), superoxide anion radical (EC50 values of 0.75 ± 0.04 and 0.46 ± 0.05 mg/mL, respectively), and ABTS cation radical (EC50 values of 0.96 ± 0.08 and 0.54 ± 0.03 mg/mL, respectively). Moreover, MDLFTE and WPPD showed high inhibiting ability on lipid peroxidation. However, MDLFTE and WPPD were unstable and could not retain strong antioxidant activity at high temperatures (>80 °C for 0.5 h), basic pH conditions (pH > 9 for 2.5 h), or during simulated GI digestion. In addition, the effect of simulated gastrointestinal digestion on TGP4 was significantly weaker than that on MDLFTE. Therefore, MDLFTE and WPPD may be more suitable for serving as nutraceutical candidates in isolated forms than as food ingredient candidates in functional foods and products.

scholarly journals Four Antioxidant Peptides from Protein Hydrolysate of Red Stingray (Dasyatis akajei) Cartilages: Isolation, Identification, and In Vitro Activity Evaluation

Marine Drugs ◽  
2019 ◽  
Vol 17 (5) ◽  
pp. 263 ◽  
Author(s):  
Xiao-Yang Pan ◽  
Yu-Mei Wang ◽  
Li Li ◽  
Chang-Feng Chi ◽  
Bin Wang
Keyword(s):  
Protein Hydrolysate ◽  
Guanidine Hydrochloride ◽  
Cation Radical ◽  
Reducing Power ◽  
Amino Acid Sequences ◽  
Water Soluble ◽  
Antioxidant Peptides ◽  
Antioxidant Additive ◽  
Dasyatis Akajei ◽  
Red Stingray

In the work, water-soluble proteins of red stingray (Dasyatis akajei) cartilages were extracted by guanidine hydrochloride and hydrolyzed using trypsin. Subsequently, four antioxidant peptides (RSHP-A, RSHP-B, RSHP-C, and RSHP-D) were isolated from the water-soluble protein hydrolysate while using ultrafiltration and chromatographic techniques, and the amino acid sequences of RSHP-A, RSHP-B, RSHP-C, and RSHP-D were identified as Val-Pro-Arg (VPR), Ile-Glu-Pro-His (IEPH), Leu-Glu-Glu--Glu-Glu (LEEEE), and Ile-Glu-Glu-Glu-Gln (IEEEQ), with molecular weights of 370.46 Da, 494.55 Da, 647.64 Da, and 646.66 Da, respectively. VPR, IEPH, LEEEE, and IEEEQ exhibited good scavenging activities on the DPPH radical (EC50 values of 4.61, 1.90, 3.69, and 4.01 mg/mL, respectively), hydroxyl radical (EC50 values of 0.77, 0.46, 0.70, and 1.30 mg/mL, respectively), superoxide anion radical (EC50 values of 0.08, 0.17, 0.15, and 0.16 mg/mL, respectively), and ABTS cation radical (EC50 values of 0.15, 0.11, 0.19, and 0.18 mg/mL, respectively). Among the four isolated antioxidant peptides, IEPH showed the strongest reducing power and lipid peroxidation inhibition activity, but LEEEE showed the highest Fe2+-chelating ability. The present results suggested that VPR, IEPH, LEEEE, and IEEEQ might have the possibility of being an antioxidant additive that is used in functional food and pharmaceuticals.

scholarly journals Preparation, Identification, and Activity Evaluation of Eight Antioxidant Peptides from Protein Hydrolysate of Hairtail (Trichiurus japonicas) Muscle

Marine Drugs ◽  
2019 ◽  
Vol 17 (1) ◽  
pp. 23 ◽  
Author(s):  
Xiu-Rong Yang ◽  
Lun Zhang ◽  
Dong-Ge Ding ◽  
Chang-Feng Chi ◽  
Bin Wang ◽  
...  
Keyword(s):  
Superoxide Anion ◽  
Protein Hydrolysate ◽  
Reducing Power ◽  
Model System ◽  
Amino Acid Sequences ◽  
Health Food ◽  
Antioxidant Peptides ◽  
Food Industries ◽  
Molecular Weights ◽  
Hydrolysis Process

In this report, protein of hairtail (Trichiurus japonicas) muscle was separately hydrolyzed using five kinds of proteases (alcalase, trypsin, neutrase, pepsin, and papain), and the papain- and alcalase-hydrolysates showed higher 2,2-diphenyl-1-picrylhydrazyl radicals (DPPH•) and hydroxyl radical (HO•) scavenging activity than other three protease hydrolysates. Therefore, the protein hydrolysate of hairtail muscle (HTP) was prepared using binary-enzymes hydrolysis process (papain + alcalase). Subsequently, eight antioxidant peptides were purified from HTP using membrane ultrafiltration and chromatography technology, and their amino acid sequences were identified as Gln-Asn-Asp-Glu-Arg (TJP1), Lys-Ser (TJP2), Lys-Ala (TJP3), Ala-Lys-Gly (TJP4), Thr-Lys-Ala (TJP5), Val-Lys (TJP6), Met-Lys (TJP7), and Ile-Tyr-Gly (TJP8) with molecular weights of 660.3, 233.0, 217.1, 274.1, 318.0, 245.1, 277.0, and 351.0 Da, respectively. TJP3, TJP4, and TJP8 exhibited strong scavenging activities on DPPH• (EC50 0.902, 0.626, and 0.663 mg/mL, respectively), HO• (EC50 1.740, 2.378, and 2.498 mg/mL, respectively), superoxide anion radical (EC50 2.082, 2.538, and 1.355 mg/mL, respectively), and 2,2′-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical (EC50 1.652, 0.831, and 0.586 mg/mL, respectively). Moreover, TJP3, TJP4, and TJP8 showed higher reducing power and inhibiting ability on lipid peroxidation in a linoleic acid model system. These results suggested that eight isolated peptides (TJP1 to TJP8), especially TJP3, TJP4, and TJP8 might serve as potential antioxidants applied in the pharmaceutical and health food industries.

Biochemical characterization of aspartate aminotransferase allozymes from common wheat

2013 ◽  
Vol 8 (12) ◽  
pp. 1183-1193 ◽  
Author(s):  
Marcin Maciąga ◽  
Michał Szkop ◽  
Andrzej Paszkowski
Keyword(s):  
Common Wheat ◽  
Aspartate Aminotransferase ◽  
Biochemical Characterization ◽  
Gel Filtration ◽  
Catalytic Efficiency ◽  
Amino Acid Sequences ◽  
Molecular Weights ◽  
Sds Page ◽  
Technique Comparison

AbstractSix allozymes of aspartate aminotransferase (AAT, EC 2.6.1.1): three plastidial (AAT-2 zone) and three cytosolic (AAT-3 zone) were isolated from common wheat (Triticum aestivum) seedlings and highly purified by a five-step purification procedure. The identity of the studied proteins was confirmed by mass spectrometry. The molecular weight of AAT allozymes determined by gel filtration was 72.4±3.6 kDa. The molecular weights of plastidial and cytosolic allozymes estimated by SDS-PAGE were 45.3 and 43.7 kDa, respectively. The apparent Michaelis constant (K m) values determined for four substrates appeared to be very similar for each allozyme. The values of the turnover number (k cat) and the k cat/K m ratio calculated for allozymes with L-aspartate as a leading substrate were in the range of 88.5–103.8 s−1/10,412–10,795 s−1 M−1 for AAT-2 zone and 4.6–7.0 s−1/527–700 s−1 M−1 for AAT-3 zone. These results clearly demonstrated much higher catalytic efficiency of AAT-2 allozymes. Therefore, partial sequences of cDNA encoding AATs from different zones were obtained using the RT-PCR technique. Comparison of the AAT-2 and AAT-3 amino acid sequences from active site regions revealed five non-conservative substitutions, which impact on the observed differences in the isozymes catalytic efficiency is discussed.

Characterization of an Aminopeptidase and a Proline Iminopeptidase from Cabbage Leaves

2008 ◽  
Vol 63 (1-2) ◽  
pp. 105-112 ◽  
Author(s):  
Margarita Marinova ◽  
Alexander Dolashki ◽  
Florian Altenberend ◽  
Stefan Stevanovic ◽  
Wolfgang Voelter ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Heavy Metal Ions ◽  
Gel Filtration ◽  
Amino Acid Sequences ◽  
Aminopeptidase Activity ◽  
Molecular Weights ◽  
Brassica Oleraceae ◽  
Sds Electrophoresis ◽  
Proline Iminopeptidase

Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2−7.5 for aminopeptidase activity and 8.0−8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by p-chloromercuribenzoic acid, heavy metal ions and urea. The molecular weights were determined by gel filtration to be 56 and 204 kDa, respectively. The iminopeptidase was decomposed during SDS electrophoresis to four subunits of 50 kDa. Minor impurities of myrosinase- associated protein (~70 kDa) were found in both preparations. Preliminary data of their amino acid sequences showed similarities to those of aminopeptidases N (family M1) and proline iminopeptidases (family S33).

scholarly journals Purification and Identification of Novel Antioxidant Peptides Isolated from Geoffroea decorticans Seeds with Anticoagulant Activity

Pharmaceutics ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1153
Author(s):  
Juliana Cotabarren ◽  
Brenda Ozón ◽  
Santiago Claver ◽  
Javier Garcia-Pardo ◽  
Walter David Obregón
Keyword(s):  
Anticoagulant Activity ◽  
Structural Features ◽  
Deciduous Tree ◽  
Antioxidant Peptides ◽  
Purification And Characterization ◽  
Molecular Weights ◽  
Ic50 Value ◽  
Dose Dependent ◽  
Direct Applicability

Geoffroea decorticans is a xerophilous deciduous tree present in most arid forests of southern South America, which is commonly used in traditional medicine. The seeds of this tree have been previously investigated for their singular chemical composition, but their protein content has been poorly investigated. Herein, we report the isolation, purification, and characterization of a set of thermostable peptides derived from Geoffroea decorticans seeds (GdAPs) with strong antioxidant and anticoagulant activities. The most potent antioxidant peptides showed a half maximal inhibitory concentration (IC50) of 35.5 ± 0.3 µg/mL determined by 1,1-diphenyl-2-picrylhydrazyl (DPPH). They also caused a dose-dependent prolongation of the aPTT clotting time with an IC50 value of ~82 µg/mL. Interestingly, MALDI-TOF/MS analysis showed the presence of three major peptides with low molecular weights of 2257.199 Da, 2717.165 Da, and 5422.002 Da. The derived amino-acid sequence of GdAPs revealed their unique structural features, exhibiting homology with various proteins present in the genome of Arachis hypogaea. All in all, our data suggest a direct applicability of GdAPs for pharmaceutical purposes.

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