• 제목/요약/키워드: egg white protein hydrolysate

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Preparation of Egg White Liquid Hydrolysate (ELH) and Its Radical-Scavenging Activity

  • Noh, Dong Ouk;Suh, Hyung Joo
    • Preventive Nutrition and Food Science
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    • 제20권3호
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    • pp.183-189
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    • 2015
  • In the present study, an optimum protease was selected to hydrolyze the egg white liquid protein for the antioxidant peptides. Alcalase treatment yielded the highest amount of ${\alpha}$-amino groups (15.27 mg/mL), while the control (no enzymatic hydrolysis) showed the lowest amount of ${\alpha}$-amino groups (1.53 mg/mL). Alcalase also gave the highest degree of hydrolysis (DH) value (43.2%) and was more efficient for egg white liquid hydrolysis than the other enzymes. The Alcalase hydrolysate had the highest radical-scavenging activity (82.5%) at a concentration of 5.0 mg/mL. The conditions for enzymatic hydrolysis of egg white liquid with Alcalase were selected as substrate : water ratio of 2:1. Five percent Alacalse treatment did not show significant (P>0.05) increases of DH and ${\alpha}$-amino nitrogen content after 24 hhydrolysis. Thirty two hour-hydrolysis with 5% Alcalase is sufficient to make antioxidative egg white liquid hydrolysate from egg white liquid. DPPH and ABTS radical-scavenging activities were significantly (P<0.05) higher after enzymatic digestion. These results suggest that active peptides released from egg-white protein are effective radical-scavengers. Thus, this approach may be useful for the preparation of potent antioxidant products.

Increase of Antioxidant Activities of Egg White Protein Hydrolysate by Fractionation without Using Toxic Chemicals

  • Park, Eun Young;Sato, Kenji
    • 한국조리학회지
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    • 제24권2호
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    • pp.103-111
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    • 2018
  • The objectives of the present study were to examine the antioxidant activity of autofocusing fractions from egg white protein hydrolysates and obtain higher antioxidant peptide fraction, which could be applied to the food model system. Alkaline protease hydrolysate of egg white protein exerted higher antioxidant activities than other protein hydrolysates and were fractionated on the basis of the amphoteric nature of sample peptides by preparative isoelectric focusing without toxic solvents and reagents, which is termed autofocusing. Neutral and basic fractions showed higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity than the acidic fractions. The acidic and neutral fractions showed higher hydroxyl (OH) radical scavenging activity and oxygen radical absorbance capacity (ORAC) values than the basic fractions. The acidic fractions showed higher metal chelating activity than basic fractions. Antioxidant activities of some autofocusing fractions except for ORAC showed higher compared to the crude hydrolysate. These results suggest that peptides fractions from egg white protein are effective antioxidant, and that autofocusing could be useful to increase antioxidant activity for application to food system.

Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein

  • Cho, Dae-Yeon;Jo, Kyungae;Cho, So Young;Kim, Jin Man;Lim, Kwangsei;Suh, Hyung Joo;Oh, Sejong
    • 한국축산식품학회지
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    • 제34권3호
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    • pp.362-371
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    • 2014
  • This study utilized commercially available proteolytic enzymes to prepare egg-white protein hydrolysates (EPHs) with different degrees of hydrolysis. The antioxidant effect and functionalities of the resultant products were then investigated. Treatment with Neutrase yielded the most ${\alpha}$-amino groups (6.52 mg/mL). Alcalase, Flavourzyme, Protamex, and Ficin showed similar degrees of ${\alpha}$-amino group liberation (3.19-3.62 mg/mL). Neutrase treatment also resulted in the highest degree of hydrolysis (23.4%). Alcalase and Ficin treatment resulted in similar degrees of hydrolysis. All hydrolysates, except for the Flavourzyme hydrolysate, had greater radical scavenging activity than the control. The Neutrase hydrolysate showed the highest 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity ($IC_{50}=3.6mg/mL$). Therefore, Neutrase was identified as the optimal enzyme for hydrolyzing egg-white protein to yield antioxidant peptides. During Neutrase hydrolysis, the reaction rate was rapid over the first 4 h, and then subsequently declined. The $IC_{50}$ value was lowest after the first hour (2.99 mg/mL). The emulsifying activity index (EAI) of EPH treated with Neutrase decreased, as the pH decreased. The EPH foaming capacity was maximal at pH 3.6, and decreased at an alkaline pH. Digestion resulted in significantly higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ABTS radical scavenging activity. The active peptides released from egg-white protein showed antioxidative activities on ABTS and DHHP radical. Thus, this approach may be useful for the preparation of potent antioxidant products.

Enzymatic Hydrolysis of Egg White Protein Exerts a Hypotensive Effect in Spontaneously Hypertensive Rats

  • Lee, Da-Eon;Jung, Tae-Hwan;Jo, Yu-Na;Yun, Sung-Seob;Han, Kyoung-Sik
    • 한국축산식품학회지
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    • 제39권6호
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    • pp.980-987
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    • 2019
  • This study was conducted to investigate the hypotensive effect of egg white protein (EWP) hydrolysate (EWH) in spontaneously hypertensive rats (SHRs). The hydrolysis of EWP was effectively performed with a combination of 0.5% bromelain and 1% papain at 50℃ for 60 min. The resulting hydrolysate did not elicit an allergic reaction as confirmed by human mast cell activation test. The systolic and diastolic blood pressures of the SHRs fed the EWH diet were observed to be significantly or numerically lower than those of the other groups during the experimental period of 28 d. EWH treatment significantly (p<0.05) upregulated the nitric oxide levels in hCMEC/D3 cells and the plasma of the SHRs compared to those in the control. Moreover, EWH ingestion significantly (p<0.01) reduced the plasma angiotensin II level of the SHRs compared with that in the control. In conclusion, beyond its basic nutritional value, EWH prevents and manages hypertension, and thus can be an invaluable resource for functional food development.

Hydrolysate Preparation with High Content of 5-Hydroxytryptophan from Liquid Egg Protein and Its Sleep-Potentiating Activity

  • Kwon, Jung Il;Park, Yooheon;Han, Sung Hee;Suh, Hyung Joo
    • 한국축산식품학회지
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    • 제37권5호
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    • pp.646-653
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    • 2017
  • Alcalase hydrolysis of liquid egg white was used to produce 5-hydroxytryptophan (HTP) under various conditions and investigate the sleep-potentiating activity of liquid egg white hydrolysate (LEH) on pentobarbital-induced sleep. Alcalase hydrolysis yielded the highest content of 5-HTP ($13.50{\mu}g/mL$), while neutrase hydrolysis showed the lowest 5-HTP content ($5.23{\mu}g/mL$). The liquid egg white to water ratio (1:1) was optimal for the production of 5-HTP with high amino-nitrogen (A-N) content and degree of hydrolysis. The 5-HTP, amino-nitrogen, and degree of hydrolysis increased until 24 h of hydrolysis and slightly increased thereafter during hydrolysis with 2% and 5% enzyme addition. 5-HTP administration at doses of 6 and 9 mg/kg significantly increased sleep duration and decreased sleep latency time compared to that in the control (p<0.05). LEH (150 mg/mouse), which was equivalent to 5-HTP at 6 mg/kg, significantly decreased sleep latency time and increased sleep duration time compared to that in the control (p<0.05). Oral administration of LEH showed sleep-potentiating effects because of 5-HTP. The sleep-potentiating activity of LEH may have occurred through 5-HTP in our pentobarbital-induced sleep model. LEH may be a valuable alternative to sleep enhancement and may be used as a sleep-potentiating agent.

Rapid Formation of biologically Active Neoglycoprotein from Lysozyme and Xyloglucan Hydrolysates through Naturally Occurring Maillard Reaction

  • Soichiro Nakamura;Masayoshi Saito;Tetsuhisa Goto;Hiroki Seaki;Masahiro Ogawa;Masayuki Gotoh;Yasuhide Gohya;Hwang, Jae-Kwan
    • Preventive Nutrition and Food Science
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    • 제5권2호
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    • pp.65-69
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    • 2000
  • Hen egg-white lysozyme was conjugated with 7~9 mers xyloglucan hydrolysates(MW-1,400) at 6$0^{\circ}C$ and 79% relative humidity for 3 days. SDS-PAGE showed that the conjugation between lysozyme and the oligosaccharide began from 1-day incubation, and three molecules of carbohydrate chains were attached to a protein molecule after 30day incubation. The enzymatic activity of lysozyme was totally conserved in the neoglycoprotein, when measured by using glycol chitin as substrate. Besides, the emulsifying properties of lysozyme were vastly improved by the conjugation with the oligosaccharide, in which emulsifying activity of the neoglycoprotein was five times higher than that of native one.

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Improvement of Rheological and Functional Properties of Salmon FPC by Enzymatic Partial Hydrolysis 2. Rheological and functional properties of salmon FPC hydrolysates

  • LEE Jong-Ho;LEE Keun-Tai;PARK Seong-Min;PARK Chan-kyu
    • 한국수산과학회지
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    • 제30권6호
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    • pp.956-963
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    • 1997
  • To enhance application of FPC in food industry, salmon FPC hydrolysates were produced and their functional properties were investigated. Hydrolysates of salmon FPC showed high solubilities ranged from approximately $80\~95\%$. Emulsifying activity index (EAI) values of hydrolysates were higher than that of egg white, however sugar ester showed the highest EAI value of 32.5. Though sugar ester had the best emulsifying stability value $({\Delta}EAI)$ of 9.65, hydrolysates showed better ${\Delta}EAI$ value than that of egg white. Foam Activity of hydrolysates was predominantly better than those of controls and also foam stability value showed similiar trend. Osmolality of hydrolysates was increased with the increase of degree of hydrolysis (DH) and concentration of protein, but it showed very lower osmolality than that of NaCl. Flow property of hydrolysates showed different upward-downward curves, and hysteresis loop increased with the increase of DH. ACE inhibitory activity showed similiar value ranged from $21.1\~24\%$ at all DH values.

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Ovalbumin Hydrolysates Inhibit Nitric Oxide Production in LPS-induced RAW 264.7 Macrophages

  • Kim, Hyun Suk;Lee, Jae Hoon;Moon, Sun Hee;Ahn, Dong Uk;Paik, Hyun-Dong
    • 한국축산식품학회지
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    • 제40권2호
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    • pp.274-285
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    • 2020
  • In this study, ovalbumin (OVA) hydrolysates were prepared using various proteolytic enzymes and the anti-inflammatory activities of the hydrolysates were determined. Also, the potential application of OVA as a functional food material was discussed. The effect of OVA hydrolysates on the inhibition of nitric oxide (NO) production was evaluated via the Griess reaction, and their effects on the expression of inducible NO synthase (inducible nitric oxide synthase, iNOS) were assessed using the quantitative real-time PCR and Western blotting. To determine the mechanism by which OVA hydrolysates activate macrophages, pathways associated with the mitogen-activated protein kinase (MAPK) signaling were evaluated. When the OVA hydrolysates were added to RAW 264.7 cells without lipopolysaccharide (LPS) stimulation, they did not affect the production of NO. However, both the OVA-Protex 6L hydrolysate (OHPT) and OVA-trypsin hydrolysate (OHT) inhibited NO production dose-dependently in LPS-stimulated RAW 264.7 cells. Especially, OHT showed a strong NO-inhibitory activity (62.35% at 2 mg/mL) and suppressed iNOS production and the mRNA expression for iNOS (p<0.05). Also, OHT treatment decreased the phosphorylation levels of Jun amino-terminal kinases (JNK) and extracellular signal-regulated kinases (ERK) in the MAPK signaling pathway. These findings suggested that OVA hydrolysates could be used as an anti-inflammatory agent that prevent the overproduction of NO.