• Title/Summary/Keyword: Gelatin hydrolysate

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Fractionation and Angiotensin I-converting Enzyme (ACE) Inhibitory Activity of Gelatin Hydrolysates from by-products of Alaska Pollock Surimi

  • Park, Chan-Ho;Kim, Hyung-Jun;Kang, Kyung-Tae;Park, Jae-W.;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • v.12 no.2
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    • pp.79-85
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    • 2009
  • Gelatin hydrolysates with a high inhibitory activity against angiotensin I-converting enzyme (ACE) were fractionated from Alaska pollock surimi refiner discharge. The ACE-inhibitory activity, expressed as $IC_{50}$ (mg/mL), was highest (0.49 mg/mL) in gelatin hydrolysates formed by sequential 2-hr treatments of Pronase and Flavourzyme. After fractionation through four different membrane filters with molecular weight cut-offs of 3, 5, 10, and 30 kDa, the highest ACE-inhibitory activity (0.21 mg/mL) was observed with the 3-kDa filtrate.

Antioxidant Activity of Porcine Skin Gelatin Hydrolyzed by Pepsin and Pancreatin

  • Chang, Oun Ki;Ha, Go Eun;Jeong, Seok-Geun;Seol, Kuk-Hwan;Oh, Mi-Hwa;Kim, Dong Wook;Jang, Aera;Kim, Sae Hun;Park, Beom-Young;Ham, Jun-Sang
    • Food Science of Animal Resources
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    • v.33 no.4
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    • pp.493-500
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    • 2013
  • Gelatin is a collagen-containing thermohydrolytic substance commonly incorporated in cosmetic and pharmaceutical products. This study investigated the antioxidant activity of gelatin by using different reagents, such as 2,2-azinobis-(3-ethylbenzothiazoline- 6-sulfonic acid) (ABTS), 2,2-di (4-tert-octylphenyl)-1-picrylhydrazyl (DPPH), and oxygen radical absorbance capacity-fluorescein (ORAC-FL) in a porcine gelatin hydrolysate obtained using gastrointestinal enzymes. Electrophoretic analysis of the gelatin hydrolysis products showed extensive degradation by pepsin and pancreatin, resulting in an increase in the peptide concentration (12.1 mg/mL). Antioxidant activity, as measured by ABTS, exhibited the highest values after 48-h incubation with pancreatin treatment after pepsin digestion. Similar effects were observed at 48 h incubation, that is, 61.5% for the DPPH assay and 69.3% for the ABTS assay. However, the gallic acid equivalent (GE) at 48 h was $87.8{\mu}M$, whereas $14.5{\mu}M$ GE was obtained using the ABTS and DPPH assays, indicating about sixfold increase. In the ORACFL assay, antioxidant activity corresponding to $45.7{\mu}M$ of trolox equivalent was found in the gelatin hydrolysate after 24 h hydrolysis with pancreatin treatment after pepsin digestion, whereas this activity decreased at 48 h. These antioxidant assay results showed that digestion of gelatin by gastrointestinal enzymes prevents oxidative damage.

Bitterness and Solubility of Soy Protein, Casein, Gluten, and Gelatin Hydrolysates Treated with Various Enzymes (효소종류에 따른 대두단백, 카제인, 글루텐, 젤라틴 단백질 가수분해물의 쓴맛과 용해도 특성)

  • Kim, Mi-Ryung
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.4
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    • pp.587-594
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    • 2010
  • To develop commercially available food protein hydrolysates, the effects of different types of enzymes and substrates on bitterness and solubility of partially hydrolyzed food proteins were investigated. Four types of proteins (casein, isolated soy protein (ISP), wheat gluten, and gelatin) and five types of proteolytic enzymes (a microbial alkaline protease (alcalase), a microbial neutral protease (neutrase), papain, bromelain, trypsin) were used. To profile the pattern of hydrolysis, the degree of hydrolysis (DH) were monitored during 180 min of reaction time by pH-stat method. Casein showed the highest susceptibility to hydrolysis for all five proteases compared to those of ISP, gluten, and gelatin. In addition, the bitter intensity and solubility (nitrogen soluble index, NSI) of each protein hydrolysate were compared at DH 10%. Bitterness and solubility of protein hydrolysates were highly affected by DH and the types of enzymes and substrates. At DH=10%, casein hydrolysate by trypsin, ISP and gluten hydrolysates by either bromelain or neutrase, and gelatin hydrolysates by the five proteases tested in this study were highly soluble and less bitter.

Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Alaskan Pollack Skin

  • Byun, Hee-Guk;Kim, Se-Kwon
    • BMB Reports
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    • v.35 no.2
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    • pp.239-243
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    • 2002
  • Angiotensin I that converts the enzyme (ACE) inhibitory peptide, Gly-Pro-Leu, previously purified and identified from the Alaskan pollack skin gelatin hydrolysate, were synthesized. In addition, the peptides Gly-Leu-Pro, Leu-Gly-Pro, Leu-Pro-Gly, Pro-Gly-Leu, Pro-Leu-Gly, Gly-Pro, and Pro-Leu, which consisted of glycine, proline, and leucine, were synthesized by the solid-phase method. The $IC_{50}$ values of each tripeptide - namely Leu-Gly-Pro, Gly-Leu-Pro, Gly-Pro-Leu, Pro-Leu-Gly, Leu-Pro-Gly, and Pro-Gly-Leu - were 0.72, 1.62, 2.65, 4.74, 5.73, and $13.93{\mu}M$, respectively. The ACE inhibitory activity of these tripeptides was higher than that of dipeptides, such as Gly-Pro and Pro-Leu with $IC_{50}$ values of 252.6 and $337.3\;{\mu}M$, respectively. Among the tripeptides, Leu-Gly-Pro and Gly-Leu-Pro had higher inhibitory activity than Gly-Pro-Leu that was isolated from the Alaskan pollack skin gelatin hydrolysate. Among the different types of tripeptides that were examined, the highest ACE inhibitory activity was observed for Leu-Gly-Pro. It had the leucine residue at the N-terminal and proline residue at the C-terminal.

Proteolytic Conditions for the Hydrolysate of Flounder Skin Gelatin (효소에 의한 가자미피 젤라틴 가수분해물의 제조 조건)

  • 강태중;양현필;김세권;송대진
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.21 no.4
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    • pp.398-406
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    • 1992
  • In order to develop a new flavourant using the fish skin gelatin, the proteolytic renditions for the gelatin hydrolysate of the alkali (B-type) and Alcalase (E-type) pretreated flounder (Limanda aspera) skin gelatin were investigated, and some physical properties, molecular weight and amino acid compositions of the hydrolysates were, also, compared with each other. The proteolytic conditions of the gelatins (B-type and E-type) by trypsin were as follows : reaction temperature, 55$^{\circ}C$ : pH, 9.0 : enzyme concentration, 0.1% : re-action time, 4hrs for B-type and 1 hr for E-type. The degrees of hydrolysis of the B-type and E-type gelatin un-der the renditions stated above were 63% and 82%, respectively. The rnajor molecular weights of the hydrolysates were 15,000 dalton for B-type and 12,400 dalton for E-type. Among the amino acids in the hydrolysates, glycine, alanine, proline, hydroxyproline and serine having a sweet taste were responsible for 57% of the total amino acid. But valine, leucine, phenylalanine, tyrosine, methionine, arginine and histidine having a bitter taste were only 18%.

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Processing and Biological Activity of Gelatin Hydrolysate from Branchiostegus japonicus Scales (옥돔(Branchiostegus japonicus) 비늘 유래 젤라틴의 가수분해 및 가수분해물의 기능성)

  • Ahn, Yong-Seok;Lee, Won-Woo;Lee, Seung-Hong;Ahn, Gin-Nae;Ko, Chang-Ik;Oh, Chang-Kyung;Oh, Myung-Cheol;Kim, Dong-Woo;Jeon, You-Jin;Kim, Soo-Hyun
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.42 no.5
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    • pp.417-425
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    • 2009
  • The potential utility of fish scales to the functional food industry has been investigated due to its antioxidant and antihypertensive characteristics. In this study, we report on the reactive oxygen species (ROS) scavenging and angiotensin I converting enzyme (ACE) inhibitory activities of gelatin hydrolysates processed from Branchiostegus japonicus scales, which are also high in protein content (about 46.1%). We prepared the enzymatic gelatin hydrolysates with four proteases (${\alpha}$-chymotrypsin, Alcalase, Neutrase and trypsin) from B. japonicus scale gelatin, which was prepared according to different reaction times, substrate/enzyme ratios and substrate concentrations. The enzymatic hydrolytic degrees of the gelatin increased time-dependently up to 6 hrs, while the Alcalase gelatin hydrolysates showed the highest hydrolysis degrees compared to the others. Furthermore, gelatin hydrolysates of Neutrase and ${\alpha}$-chymotrypsin showed the highest DPPH radical and $H_2O_2$ scavenging activities ($IC_{50}$ value; 9.18 mg/mL and 9.74 mg/mL), respectively. However, the activities were not significant (P<0.05). We also observed that the four gelatin hydrolysates significantly increased ACE inhibitory activities from approximately 20% to 60% (P<0.05), Among them, the Alcalase gelatin hydrolysates showed the higher ACE inhibitory activity ($IC_{50}$ value; 0.73 mg/mL) compared to the others. These results suggest that the enzymatic gelatin hydrolysates prepared from B. japonicus scales may possess a potentially useful function as an ACE inhibitory agent. As such, the utility of B. japonicus scales should be given due consideration for application in the functional food industry.

Isolation and Characterization of Antioxidative Peptides from Enzymatic Hydrolysates of Yellowfin Sole Skin Gelatin (가자미피 젤라틴 가수분해물로부터 항산화성 펩티드의 분리${\cdot}$정제 및 특성)

  • KIM Se-Kwon;LEE Hyun-Chel;BYUN He-Guk;JEON Yon-Jin
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.29 no.2
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    • pp.246-255
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    • 1996
  • To develop a natural antioxidative peptide, the gelatin was extracted from fish (Yellowfin sole) skin by hot $water(50^{\circ}C)$ extraction method and hydrolyzed with Alcalase, pronase and collagenase through a continuous 3-step membrane reactor. Each step enzymatic hydrolysates were determined the antioxidative activity and their synergistic effects, compared with $\alpha-tocopherol$ and butylated hydroxytoluene (BHT). Also, we tried to investigate the antioxidative disposition of peptide which was successfully separated by gel filtration, ion-exchange chromatography, and HPIC in cultured rat hepatocytes intoxicated with tert-butyl hydroperoxide (TBHP). Second step enzymatic hydrolysate (SSEH) among all hydrolysates and $\alpha-tocoperol$ was showed the strongest antioxidative activity. The optimum concentration of antioxidative activity for SSEH was $1\%(w/w)$ in linoleic acid. The synergistic effects were increased in using the hydrolysate with tocopherol and BHT. In the presence of the peptide isolated from SSEH, supplemented hepatocytes exposed to TBHP showed that delayed cell killing and decreased significantly the lipid peroxidation, compared with hepatocytes not cultured with isolated peptide.

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Improvement of the Antioxidative and ACE-inhibiting Activities of Commercial Soy Sauce using Gelatin Hydrolysates from the By-products of Alaska Pollock (명태 수리미 부산물 유래 젤라틴 가수분해물을 이용한 시판 간장의 항산화성 및 ACE 저해활성의 개선)

  • Heu, Min-Soo;Park, Chan-Ho;Kim, Jeong-Gyun;Kim, Hyung-Jun;Yoon, Min-Seok;Park, Kwon-Hyun;Kim, Jin-Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.43 no.3
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    • pp.179-187
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    • 2010
  • This study examined ways to improve the functional properties of commercial soy sauce using gelatin hydrolysates from the refiner discharge of Alaska pollock, Theragra chalcogramma. The total nitrogen content and pH of gelatin sauce prepared by dissolving the second-step gelatin hydrolysates (15 g), salt (20 g), sugar (5 g), glucose (2.5 g), inosine monophosphate (IMP) (0.5 g), black pepper (0.1 g), caramel powder (0.1 g), ginger powder (0.05 g), garlic powder (0.05 g), vinegar (3 mL), and fructose (3 mL) in water(100 mL) were 1.71% and 5.35, respectively. The results of a sensory evaluation indicated that when preparing blended soy sauce, the optimal blending ratio of gelatin sauce to commercial soy sauce was 20:80 (v/v). Because the total nitrogen content and pH of the blended soy sauce were 1.52% and 5.31, respectively, the blended soy sauce could be sold as a soy sauce. The oxidative property of the blended soy sauce was similar to that of 20 mM ascorbic acid, and its angiotensin-converting enzyme (ACE) -inhibiting activity was 1.5 mg/mL. The results suggest that the antioxidative and ACE-inhibiting activities of commercial soy sauce can be improved by blending gelatin sauce (20) with commercial soy sauce (80). The total amino acid content of the blended soy sauce was 9,107.3 mg/mL, which was higher than that (8,992.4 mg/100 mL) of commercial soy sauce. However, the taste value of the blended soy sauce was 415.8, which was lower than that (431.2) of commercial soy sauce.

Effect of Porcine Collagen Peptides on the Rheological and Sensory Properties of Ice Cream

  • Li, Liying;Kim, Jae-Hyeong;Jo, Yeon-Ji;Min, Sang-Gi;Chun, Ji-Yeon
    • Food Science of Animal Resources
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    • v.35 no.2
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    • pp.156-163
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    • 2015
  • The effects of low molecular-weight collagen peptides derived from porcine skin were investigated on the physicochemical and sensorial properties of chocolate ice cream. Collagen peptides less than 1 kDa in weight were obtained by sub-critical water hydrolysis at a temperature of $300^{\circ}C$ and a pressure of 80 bar. Ice cream was then prepared with gelatin powder and porcine skin hydrolysate (PSH) stabilizers mixed at seven different ratios (for a total of 0.5 wt%). There was no significant difference in color between the resulting ice cream mixtures. The increase in apparent viscosity and shear thinning of the ice cream was more moderate with PSH added than with gelatin. Moreover, the samples containing more than 0.2 wt% PSH had enhanced melting resistance, while the mixture with 0.2 wt% PSH had the lowest storage modulus at $-20^{\circ}C$ and the second highest loss modulus at 10℃, indicating that this combination of hydrocolloids leads to relatively softer and creamier chocolate ice cream. Among the seven types of ice creams tested, the mixture with 0.2 wt% PSH and 0.3 wt% gelatin had the best physicochemical properties. However, in sensory evaluations, the samples containing PSH had lower chocolate flavor scores and higher off-flavor scores than the sample prepared with just 0.5 wt% gelatin due to the strong off-flavor of PSH.

Fractionation and Characterization of Fractions with High Antioxidative Activity from the Gelatin Hydrolysates of Korean Rockfish Sebastes schlegelii Skin

  • Kim, Hyung-Jun;Park, Kwon-Hyun;Shin, Jun-Ho;Lee, Ji-Sun;Heu, Min-Soo;Lee, Dong-Ho;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • v.14 no.3
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    • pp.168-173
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    • 2011
  • The purpose of this study was to obtain a fraction with high antioxidative activity from second rockfish gelatin hydrolysates (SRSGHs), which were hydrolyzed with Alcalase and Flavourzyme through ultrafiltration membranes with serial digestions for 1 and 2 h, respectively, and to investigate the feasibility of this fraction as a potential functional food ingredient. Among various fractions that were ultrafiltered from the SRSGH with four types of membrane (1, 5, 10, and 30 kDa), the SRSGH-III fraction, which permeated the 10 kDa membrane but not the 5 kDa membrane, showed the highest antioxidant activity (protection factor=5.13) and angiotensin-I-converting enzyme-inhibiting activity ($IC_{50}$=0.82 mg/mL). These results suggest that the SRSGH-III fraction from the SRSGH can be used as a functional food ingredient. However, further studies examining its antioxidant activity in vivo as well as the different antioxidant mechanisms are needed.