• Title/Summary/Keyword: protein Hydrolysates

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Production of Ready-to-Reconstitute Functional Beverages by Utilizing Whey Protein Hydrolysates and Probiotics

  • Kumar, Sabbini Kalyan;Jayaprakasha, Heddur Manjappa;Paik, Hyun-Dong;Kim, Soo-Ki;Han, Song-Ee;Jeong, A-Ram;Yoon, Yoh-Chang
    • 한국축산식품학회지
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    • 제30권4호
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    • pp.575-581
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    • 2010
  • This investigation was aimed at developing a ready-to-reconstitute beverage by utilizing probiotics and whey protein hydrolysates carrying bioactive peptides. Cheddar cheese whey was ultrafiltered. The 18% protein retentate was subjected to protein hydrolysis using Neutrase. The hydrolyzed retentate was further condensed to 35% total solids and spray-dried at $75^{\circ}C$ outlet air temperature. Different levels of sugar, citric acid and stabilizer were blended for spray-dried hydrolysates. Spray-dried hydrolysate was further inoculated with different levels of probiotics grown in a whey medium and dried in fluidized-bed drier at $40^{\circ}C$ to obtain a ready-to-reconstitute beverage. Hydrolysis was greatest at an enzyme:substrate ratio of 1:25 for 3 h. Spray-dried hydrolysate reconstituted to 1% protein and blended with 15% sugar, 0.2% citric acid and 0.15% xantham gum resulted in a superior product with no sedimentation. Accordingly, sugar, citric acid and xanthum gum were dry-blended with spray-dried hydrolysates. Bifidobacterium bifidum and Lactobacillus acidophilus that was grown separately in a whey medium, blended to produce 2% spray-dried hydrolysate and dried as described above resulted in a readyto-reconstitute beverage mix. The fluidized dried product typically exhibited a probiotic count of $10^8$colony forming units (CFU)/g. However, blending of probiotic to the retentate and direct spray-drying precipitously reduced the probiotic count to $10^4$ CFU/g of powder.

효소(酵素)에 의한 단백질(蛋白質) 가수분해물(加水分解物)의 항산화작용(抗酸化作用) (Antioxidative Effects of Food Protein Hydrolysates by Protease)

  • 김선봉;염동민;여생규;지청일;이용우;박영호
    • 한국식품과학회지
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    • 제21권4호
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    • pp.492-497
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    • 1989
  • 천연식품성분에 의한 항산화기작을 해명하기 위하여 어육단백질, 탈지대두박, egg albumin 및 casein등의 단백질 가수분해물을 사용하여 linoleic acid 와의 모델계 반응을 통하여 이들의 항산화능과 ${\alpha}-tocopherol$과의 상승작용 및 금속이온 봉쇄능 등에 대하여 연구 검토하였는데 그 결과 각 단백질 가수분해물은 항산화능이 매우 큰 것으로 나타났으며. 특히 egg albumin가수분해물의 항산화능이 매우 강한 것으로 나타났다. 또한 천연항산화제인 ${\alpha}-tocopherol$과의 상승작용도 우수한 것으로 나타났는데 단백질 가수분해물간의 차이는 거의 없는 것으로 나타났다. 금속이온 봉쇄능 또한 높게 나타났으며 단백질 가수분해물의 금속이온 봉쇄능은 금속이온의 종류에 따라 다소 차이가 있는 것으로 나타났다.

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Nutritional Value and Bioactive Properties of Enzymatic Hydrolysates prepared from the Livers of Oncorhynchus keta and Oncorhynchus gorbuscha (Pacific Salmon)

  • Yoon, Ho Dong;Karaulova, Ekaterina P.;Shulgina, Lilia V.;Yakush, Evgeni V.;Mok, Jong Soo;Lee, Su Seon;Xie, Chengliang;Kim, Jeong Gyun
    • Fisheries and Aquatic Sciences
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    • 제18권1호
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    • pp.13-20
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    • 2015
  • Calculated chemical scores (computed in relation to the FAO/WHO reference protein) for salmon liver protein hydrolysates indicated that all amino acids (other than methionine and threonine) were present in adequate or excess quantities; thus, the raw liver material is a good source of essential amino acids. The hydrophobic amino acids contents in hydrolysates prepared from Oncorhynchus keta and O. gorbuscha were 38.4 and 39.1%, respectively. The proportion of released peptides exceeding 500 kDa was reduced when hydrolysates were treated with the commercial enzyme Alcalase, although proportions in the following MW ranges were elevated: 100-500 kDa and <50 kDa. The optimal conditions for enzymatic hydrolysis were as follows: pH 7.0, $50^{\circ}C$, and a reaction time of 1 h. Of the different proteases tested, Alcalase was the most efficient for production of salmon liver hydrolysate with the highest 1,1-diphenyl-2-picrylhydrazyl (DPPH) scavenging activity. The hydrolysates prepared from salmon liver had a balanced amino acid composition. The liver protein hydrolysates contained low molecular weight peptides, some of which may be bio-active; this bio-active potential should be investigated. Inhibition of the DPPH radical increased with increased degree of hydrolysis (DH), regardless of protease type. DPPH radical scavenging abilities, antithrombotic effects and ${\alpha}$-glucosidase enzyme inhibition effects of O. keta liver hydrolysate increased in a dose-dependent manner. Thus, salmon liver hydrolysate may be useful in functional food applications and as a source of novel products.

고지방식을 섭취한 흰쥐의 체내지질함량에 대한 단백질 가수분해물의 섭취 효과 (Effects of Protein Hydrolysates on Blood and Liver Lipids in Rats fed Fat-enriched Diet)

  • 이연숙
    • Journal of Nutrition and Health
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    • 제30권6호
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    • pp.614-621
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    • 1997
  • The experiments were performed to investigate the effects of protein and protein hydrolysates on lipid metabolism in the hyperlipidemic/hypercholesterolemic rat model induced by feeding fat-enriched diet. In Except 1 male rats were fed four semi-purified high fat and cholesterol diets that contained different nitrogen source, casein(C), casein hydrolysate(CH), corn gluten(G) and corn gluten hydrolysate(GH), for 6 weeks. In Expt. 2 rats were fed high fat and cholesterol diet for 4 weeks to induce hyperlipidemia and hypercholesterolemia. Then the rats were divided into 4 groups and were fed the four kinds of above experimental diets for 4 weeks consecutively. The contents of total lipid , cholesterol and triglyceride in blood, liver and feces were determined. Serum lipid concentrations of CH, G and GH were significantly lower than that of C. Serum cholesterol concentrations of hydrolysate groups(CH and GH) were significantly lower than those of intact protein groups(C and G). Serum HDL -cholesterol concentration tended to increase by hydrolysate intake. The total lipid, cholesterol contents in liver showed similarity results as above. Fecal lipid excretions of CH, G, and GH groups were significantly higher than that of C group. These results indicate that hypolipidemic and /or hypocholesterolemic effect of corn gluten or protein hydrolysates were detected in the process of inducing hyperlipidemia by high-fat and cholesterol diet or after inducing hyperlipidemia.

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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.

Physical and functional properties of tunicate (Styela clava) hydrolysate obtained from pressurized hydrothermal process

  • Lee, Hee-Jeong;Chae, Sol-Ji;Saravana, Periaswamy Sivagnanam;Chun, Byung-Soo
    • Fisheries and Aquatic Sciences
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    • 제20권7호
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    • pp.14.1-14.8
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    • 2017
  • In this study, marine tunicate Styela clava hydrolysate was produced by an environment friendly and green technology, pressurized hot water hydrolysis (PHWH) at different temperatures ($125-275^{\circ}C$) and pressure 50 bar. A wide range of physico-chemical and bio-functional properties such as color, pH, protein content, total carbohydrate content, reducing sugar content, and radical scavenging activities of the produced hydrolysates were evaluated. The appearance (color) of hydrolysates varied depending on the temperature; hydrolysates obtained at $125-150^{\circ}C$ were lighter, whereas at $175^{\circ}C$ gave reddish-yellow, and $225^{\circ}C$ gave dark brown hydrolysates. The $L^*$ (lightness), $a^*$ (red-green), and $b^*$ (yellow-blue) values of the hydrolysates varied between 35.20 and 50.21, -0.28 and 9.59, and 6.45 and 28.82, respectively. The pH values of S. clava hydrolysates varied from 6.45 ($125^{\circ}C$) to 8.96 ($275^{\circ}C$) and the values were found to be increased as the temperature was increased. The hydrolysis efficiency of S. clava hydrolysate was ranged from 46.05 to 88.67% and the highest value was found at $250^{\circ}C$. The highest protein, total carbohydrate content, and reducing sugar content of the hydrolysates were found 4.52 mg/g bovine, 11.48 mg/g and 2.77 mg/g at 175, and 200 and $200^{\circ}C$, respectively. Hydrolysates obtained at lower temperature showed poor radical scavenging activity and the highest DPPH, ABTS, and FRAP activities were obtained 10.25, 14.06, and 10.91 mg trolox equivalent/g hydrolysate (dry matter basis), respectively. Therefore, S. clava hydrolysate obtained by PHWH at $225-250^{\circ}C$ and 50 bar is recommended for bio-functional food supplement preparation.

김 단백질 가수분해물의 Angiotensin Ⅰ 전환효소 저해 활성 (Angiotensin Ⅰ Converting Enzyme(ACE) Inhibitory Activities of Laver(Porphyra tenera) Protein Hydrolysates)

  • 김영명;도정룡;인재평;박종혁
    • 한국식품영양학회지
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    • 제18권1호
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    • pp.11-18
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    • 2005
  • Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.

해바라기씨박 단백질 가수분해물로부터 철분 결합 펩타이드의 분리 (Isolation of Iron-Binding Peptides from Sunflower (Helianthus annuus L.) Seed Protein Hydrolysates)

  • 최동원;김남호;송경빈
    • 한국식품영양과학회지
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    • 제42권7호
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    • pp.1162-1166
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    • 2013
  • 해바라기씨박 단백질 가수분해물로부터 철분 결합 펩타이드를 분리하기 위해 해바라기씨박 단백질을 단백 가수분해 효소인 alcalase와 flavourzyme을 이용하여 가수분해하였고, 가수분해물을 3 kDa 이하로 한외여과를 하였다. 한외여과된 가수분해물은 QAE Sephadex$^{TM}$ A-25 column과 Superdex$^{TM}$ peptide 10/300 GL column을 사용하여 철분 결합 펩타이드를 분리하였고, 분리된 분획 중 철분 결합력이 가장 높은 F22를 얻었다. 본 연구에서 얻어진 해바라기씨박 단백질 가수분해물로부터 분리된 분획들은 향후 기능성식품 소재 원료로 사용될 수 있다고 판단된다.

보리 단백질 가수분해물로부터 칼슘 결합 물질의 분리 (Isolation of Calcium-Binding Peptides from Barley Protein Hydrolysates)

  • 이지혜;최동원;송경빈
    • 한국식품저장유통학회지
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    • 제19권3호
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    • pp.438-442
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    • 2012
  • 칼슘보충제로 칼슘 결합 펩타이드를 만들기 위해, 보리 단백질에 Flavourzyme을 사용하여 18시간 동안 가수분해 하였고, 가수분해 된 보리 단백질은 3 kDa 이하로 한외여과 하였다. 한외여과 된펩타이드는 ion exchange chromatography와 normal-phase HPLC를 사용하여 칼슘 결합 펩타이드를 분리하였고, 분리된 각 분획의 칼슘결합력을 측정하였다. 그 결과 가장 높은 칼슘 결합력을 보인 분획을 칼슘 chelation을 위한 소재로 얻었고, 따라서 본 연구 결과 얻어진 보리 단백질 가수분해물은 칼슘보충제로의 사용이 가능하다고 판단된다.

Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes

  • Jeewanthi, Renda Kankanamge Chaturika;Kim, Myeong Hee;Lee, Na-Kyoung;Yoon, Yoh Chang;Paik, Hyun-Dong
    • 한국축산식품학회지
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    • 제37권1호
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    • pp.62-70
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    • 2017
  • The aim of this study was identifying a suitable food grade enzymes to hydrolyze whey protein concentrates (WPCs), to give the highest bioactivity. WPCs from ultrafiltration retentate were adjusted to 35% protein (WPC-35) and hydrolyzed by enzymes, alcalase, ${\alpha}-chymotrypsin$, pepsin, protease M, protease S, and trypsin at different hydrolysis times (0, 0.5, 1, 2, 3, 4, and 5 h). These 36 types of hydrolysates were analyzed for their prominent peptides ${\beta}-lactoglobulin$ (${\beta}-Lg$) and ${\alpha}-lactalbumin$ (${\alpha}-La$), to identify the proteolytic activity of each enzyme. Protease S showed the highest proteolytic activity and angiotensin converting enzyme inhibitory activity of IC50, 0.099 mg/mL (91.55%) while trypsin showed the weakest effect. Antihypertensive and antioxidative peptides associated with ${\beta}-Lg$ hydrolysates were identified in WPC-35 hydrolysates (WPH-35) that hydrolyzed by the enzymes, trypsin and protease S. WPH-35 treated with protease S in 0.5 h, responded positively to usage as a bioactive component in different applications of pharmaceutical or related industries.