Autoxidation of Methyl Linoleate in Freeze‐Dried Model Systems. III. Effects of Added Amino Acids

Karel, Marcus; Tannenbaum, Steven R.; Wallace, David H.; Maloney, Honore

doi:10.1111/j.1365-2621.1966.tb03266.x

Cited by 90 publications

(40 citation statements)

References 8 publications

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“…), (2200 -y) pi of 25 mM phosphate buffer (pH 7.1), 0.5 ml of I mg/ml of an albumin solution in the buffer solution, 50 pi of XOD (200 pi in 1.8 ml of the albumin soln. ), and y pI of an amino acid (I x 10-3 M) as a quencher in the buffer solution in a 16mmlj> quartz cell was placed on a photomultiplier tube (R464, Hamamatsu Photonics) at 25°C in a dark cell chamber (Aloka BLR-I02B Luminometer modified for computer 5 …”

Section: Methodsmentioning

confidence: 99%

Antioxidative Activity of Amino Acids and Sulfur-containing Compounds to Superoxide: Measurement by Quenching the Chemiluminescence of aCypridinaLuciferin Analogue

Suzuki

Kochi

Wada

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

Antioxidative Activity of Amino Acids and Sulfur-containing Compounds to Superoxide: Measurement by Quenching the Chemiluminescence of aCypridinaLuciferin Analogue

Suzuki

Kochi

Wada

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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“…Since the antioxidative effects of some amino acids have been shown (Karel et al ., 1966), we compared the antioxidative activity of the four peptides with those of each constituent amino acid. When these amino acids were mixed at the same concentration as the peptides, the antioxidative activity of the amino acid mixture of each corresponding peptide was much less than that of each peptide itself (Fig.…”

Section: Peptidementioning

confidence: 99%

Antioxidative Activity of Peptides Prepared from Okara Protein.

Yokomizo

Takenaka

2002

FSTR

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Protease hydrolyses of an Okara protein yielded antioxidative activity against the peroxidation of linoleic acid in an aqueous system at pH 7.0. Four antioxidative peptides were isolated from the hydrolysate prepared with Protease N by size exclusion chromatography and reversed-phase HPLC. The peptides were composed of two and three amino acid residues, including aromatic amino acid at the C terminal end. Their amino acid sequences were determined to be Ala-Tyr, Gly-Tyr-Tyr, Ala-Asp-Phe, and Ser-Asp-Phe, respectively. The antioxidative activity of Gly-Tyr-Tyr is nearly equal to that of carnosine.Keywords: antioxidative activity, amino acid, peptide, hydrolysate, OkaraIn the manufacturing of soymilk and tofu, the soymilk residue, Okara, is produced as a by-product with little market value. However, Okara still contains about 25% protein (dry basis) with high nutritive quality. Studies on the utility of Okara (Takenaka et al., 1996;Miyamura et al., 1998;Tamura & Takenaka, 1999) have been done, but utilization of the substance is still in the developmental stage. Antioxidative activity has recently been detected in peptides from the proteolytic hydrolysis of many food proteins (Suetsuna et al., 2000;Chen et al., 1995). In this study, we examined the antioxidative effects of enzymatic hydrolysates of Okara protein with seven different proteases. Materials and MethodsMaterials The Okara protein was prepared using the method of Yamauchi et al. (1984). Proteases were purchased from Amano Enzyme Co., Ltd (Nagoya, Japan): Protease A from Aspergillus oryzae, 10,000 u/g, pH 7.0; Protease M from Aspergillus oryzae, 150,000 u/g, pH 7.0; Protease N from Bacillus subtilus, 30,000 u/g, pH 7.0; Protease P from Aspergillus melleus, 30,000 u/g, pH 8.0; Protease S from Bacillus sp. 10,000 u/g, pH 7.0; Prolezer from Bacillus subtilus 10,000 u/g, pH 9.0; and Papain W-40 from Carica pancreas, 400 u/g, pH 8.0.Preparation of the Okara protein hydrolysate Okara protein (10 g) was dissolved in 200 ml of distilled water, and heated at 100˚C for 10 min. Protease (0.2 g) was added to the protein solution after the pH was properly adjusted. Enzymatic hydrolysis was performed under optimum pH conditions as the manufacturer recommended. After digestion, hydrolysates were heated in boiling water for 5 min to inactivate proteases, then neutralized and centrifuged (20,000¥g for 10 min). The supernatants were lyophilized and stored in 4˚C until use.Measurement of antioxidative activity Linoleic acid (10 mg) in 0.5 ml of ethanol, samples in 4.0 ml of 0.2 M phosphate buffer (pH 7.0), and 0.15 ml of 20 mM 2,2¢-azobis(2-amidinopropane) dihydrochloride (AAPH) were placed in a vial, which was then sealed tightly and kept at 50˚C in the dark. At regular intervals, an aliquot of the reaction mixture was withdrawn for measurement of the oxidation using the ferric thiocyanate method (Mitsuda et al., 1966). The time taken to attain an absorbance of 0.3 was defined as the induction period. The relative antioxidative activity was calculated by dividing the indu...

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“…Fermentation with A. oryzaecould improve the reducing power of minced horse mackerel paste via koji fermentation. Some amino acids such as lysine, glycine, valine, and histidine, which are present in fish miso peptides, have been reported to exhibit antioxidant activities [43,44,45]. Notably, histidine exhibits a strong radical-scavenging activity due to the decomposition of its imidazole ring.…”

Section: Discussionmentioning

confidence: 99%

Bioactive Properties of Japanese Fermented Fish Paste, Fish Miso, Using Koji Inoculated With Aspergillusoryzae

Giri¹,

Nasu²,

Ohshima

2012

IJNFS

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Abstract:This research was evaluated the antioxidant activity of fish miso, a newly developed fermented fish paste prepared from horse mackerel meat and the fermentation of traditional Japanese koji inoculated with Aspergillusoryzae. The antioxidant activities in different in vitro models, including DPPH, hydroxyl, nitric oxide and carbon-centered radical-scavenging activity (RSA), and reducing power ability (RPA), were investigated during the fermentation period along with 2 different storage conditions. The antioxidant activity of matured fish miso was also evaluated using a linoleic acid oxidation model system by monitoring hydrogen peroxide formation and oxygen absorption. The RSA against all the types of radicals measured by electron spin resonance showed an increase over prolonged fermentation periods and during storage at high temperatures. However, the RPA showed a rapid increase during the early stages of fermentation. The SDS-PAGE profile of fish miso peptides during the early stages of fermentation indicated the occurrence of hydrolysis, suggesting the involvement of low-molecular-weight peptides in the RSA and reducing power of fish miso. Partial purification of these peptides by using an online-HPLC-DPPH flow injection analysis system and further characterization by thin layer chromatography and molecular weight distribution clearly indicated that low-molecular-weight peptides (<500 Da) were potent antioxidants. These data suggest that the antioxidant activity of fish miso could be substantially improved by fermenting Aspergillus (koji) mold. This approach provides a novel strategy to enhance the value of trash fish, such as horse mackerel.

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Autoxidation of Methyl Linoleate in Freeze‐Dried Model Systems. III. Effects of Added Amino Acids

Cited by 90 publications

References 8 publications

Antioxidative Activity of Amino Acids and Sulfur-containing Compounds to Superoxide: Measurement by Quenching the Chemiluminescence of aCypridinaLuciferin Analogue

Antioxidative Activity of Amino Acids and Sulfur-containing Compounds to Superoxide: Measurement by Quenching the Chemiluminescence of aCypridinaLuciferin Analogue

Antioxidative Activity of Peptides Prepared from Okara Protein.

Bioactive Properties of Japanese Fermented Fish Paste, Fish Miso, Using Koji Inoculated With Aspergillusoryzae

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