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Anti-Inflammatory and Antioxidant Properties of Peptides Released from ?-Lactoglobulin by High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis.

ABSTRACT: BACKGROUND:?-lactoglobulin hydrolysates (BLGH) have shown antioxidant, antihypertensive, antimicrobial, and opioid activity. In the current study, an innovative combination of high hydrostatic pressure and enzymatic hydrolysis (HHP-EH) was used to increase the yield of short bioactive peptides, and evaluate the anti-inflammatory and antioxidant properties of the BLGH produced by the HHP-EH process. METHOD:BLG was enzymatically hydrolyzed by different proteases at an enzyme-to-substrate ratio of 1:100 under HHP (100 MPa) and compared with hydrolysates obtained under atmospheric pressure (AP-EH at 0.1 MPa). The degree of hydrolysis (DH), molecular weight distribution, and the antioxidant and anti-inflammatory properties of hydrolysates in chemical and cellular models were evaluated. RESULTS:BLGH obtained under HHP-EH showed higher DH than the hydrolysates obtained under AP-EH. Free radical scavenging and the reducing capacity were also significantly stronger in HHP-BLGH compared to AP-BLGH. The BLGH produced by alcalase (Alc) (BLG-Alc) showed significantly higher antioxidant properties among the six enzymes examined in this study. The anti-inflammatory properties of BLG-HHP-Alc were observed in lipopolysaccharide-stimulated macrophage cells by a lower level of nitric oxide production and the suppression of the synthesis of pro-inflammatory cytokines. Peptide sequencing revealed that 38% of the amino acids in BLG-HHP-Alc are hydrophobic and aromatic residues, which contribute to its anti-inflammatory properties. CONCLUSIONS:Enzymatic hydrolysis of BLG under HHP produces a higher yield of short bioactive peptides with potential antioxidant and anti-inflammatory effects.

SUBMITTER: Bamdad F

PROVIDER: S-EPMC6152616 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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Anti-Inflammatory and Antioxidant Properties of Peptides Released from β-Lactoglobulin by High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis.

Bamdad Fatemeh F Bark Seonghee S Kwon Chul Hee CH Suh Joo-Won JW Sunwoo Hoon H

Molecules (Basel, Switzerland) 20170607 6

<h4>Background</h4>β-lactoglobulin hydrolysates (BLGH) have shown antioxidant, antihypertensive, antimicrobial, and opioid activity. In the current study, an innovative combination of high hydrostatic pressure and enzymatic hydrolysis (HHP-EH) was used to increase the yield of short bioactive peptides, and evaluate the anti-inflammatory and antioxidant properties of the BLGH produced by the HHP-EH process.<h4>Method</h4>BLG was enzymatically hydrolyzed by different proteases at an enzyme-to-subs ...[more]

PMID: 28590420

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Project description:The objective of this study was to investigate the biochemical antioxidant potential of peptides derived from enzymatically hydrolyzed mung bean (Vigna radiata) albumins using an 2,2'-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging assay, a ferrous ion chelating assay and an oxygen radical absorbance capacity (ORAC) assay. Peeled raw mung bean was ground into flour and mixed with buffer (pH 8.3, 1:20 w/v ratio) before being stirred, then filtered using 3 kDa and 30 kDa molecular weight cut-off (MWCO) centrifugal filters to obtain albumin fraction. The albumin fraction then underwent enzymatic hydrolysis using either gastrointestinal enzymes (pepsin and pancreatin) or thermolysin. Peptides in the hydrolysates were sequenced. The peptides showed low ABTS radical-scavenging activity (90-100 μg ascorbic acid equivalent/mL) but high ferrous ion chelating activity (1400-1500 μg EDTA equivalent/mL) and ORAC values (>120 μM Trolox equivalent). The ferrous ion chelating activity was enzyme- and hydrolysis time-dependent. For thermolysin hydrolysis, there was a drastic increase in ferrous ion chelating activity from t = 0 (886.9 μg EDTA equivalent/mL) to t = 5 min (1559.1 μg EDTA equivalent/mL) before plateauing. For pepsin-pancreatin hydrolysis, there was a drastic decrease from t = 0 (878.3 μg EDTA equivalent/mL) to t = 15 (138.0 μg EDTA equivalent/mL) after pepsin was added, but this increased from t = 0 (131.1 μg EDTA equivalent/mL) to t = 15 (1439.2 μg EDTA equivalent/mL) after pancreatin was added. There was no significant change in ABTS radical scavenging activity or ORAC values throughout different hydrolysis times for either the thermolysin or pepsin-pancreatin hydrolysis. Overall, mung bean hydrolysates produced peptides with high potential antioxidant capacity, being particularly effective ferrous ion chelators. Other antioxidant assays that use cellular lines should be performed to measure antioxidant capacity before animal and human studies.

Dataset Information

Anti-Inflammatory and Antioxidant Properties of Peptides Released from ?-Lactoglobulin by High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis.

Publications

Anti-Inflammatory and Antioxidant Properties of Peptides Released from β-Lactoglobulin by High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis.

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