• Title/Summary/Keyword: 단백질 가수분해 효소

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Process Development for the Recovery of Sialic Acid Fraction by Enzymatic Hydrolysis of Egg Yolk Protein (난황 단백질의 효소 가수분해에 의한 sialic acid의 회수 공정 개발)

  • Kang Byung Chul;Lee Kwang Hyun
    • Journal of Life Science
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    • v.15 no.1 s.68
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    • pp.9-14
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    • 2005
  • Batch enzymatic hydrolysis of egg yolk protein by protease was carried out at laboratory scale coupled to an ultrafiltration module. Effect of ethanol concentrations on the performance of enzymatic hydrolysis was studied to determine the optimum condition of recovery of hydrolysate. The enzymatic hydrolysis was conducted stepwise with following conditions, $50^{\circ}C$, pH 10.0 and pH 6.5. Ethanol concentration was changed from 10 to $40\%$ (w/w). As ethanol concentration was increased, the recovery yield of total solid and protein in enzymatic hydrolysate was also increased. The content of sialic acid and protein in hydrolysate was independent of ethanol concentration. We also investigated the effect of ethanol concentration on the performance of ultrafiltration. As the concentration of ethanol in yolk protein was increased, the recovery yield of product was increased. Ultra­filtration of egg yolk protein hydrolysate was conducted to increase the content of sialic acid. Four ultrafiltation modules were used in this study, and we evaluated the performance of the UF modules. When Amicon module was used, the recovery percentage of total solid in retentate was $6.0\%$, which is the highest among the modules used. In spite of the difference in the recovery yield of total solid, the purity of sialic acid in retentate was about $2.0\%$, which was 5 times higher than that in feed. It was concluded that the recovery yield and the purity of sialic acid did not correlate with the types of modules and the size of MWCO.

A Study on the Proteolysis of Mussel Protein by a Commercial Enzyme Preparation (단백질 분해효소에 의한 홍합 단백질의 분해에 관한 연구)

  • Choi, In-Jae;Nam, Hee-Sop;Shin, Zae-Ik;Lee, Byong-Hoon
    • Korean Journal of Food Science and Technology
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    • v.24 no.6
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    • pp.519-523
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    • 1992
  • The patterns on the proteolysis of mussel protein using a commercial enzyme preparation were investigated. The best one among six commercial enzyme preparations for the manufacture of mussel extract was Corolase PP, based on the degree of hydrolysis (DH). When the raw mussel paste, without water addition, was adjusted to pH 6.5, added 0.1% (w/w dry basis) of Corolase PP. and reacted at $50^{\circ}C$ for four hours, it reached the maximum value of DH (79%). The precooking of raw mussel decreased the efficiency of extraction and hydrolysis of the protein, due to the inactivation of the autolytic enzymes contained in the mussel. During the course of proteolysis, major free amino acids such as glycine, alanine, glutamic acid and lysine, representing a characteristic brothy taste of mussel were replaced with free hydrophobic amino acids including valine, methionine, isoleucine, and leucine. The electrophoretic pattern and HPLC-GPC pattern of mussel protein hydrolysates during the hydrolysis were observed and also discussed.

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Optimal Conditions for the Enzymatic Hydrolysis of Isolated Sesame Meal Protein (효소에 의한 참깨박 단백질의 최적 가수분해 조건)

  • Lee, S.H.;Cho, Y.J.;Kim, S.;Ahn, B.J.;Choi, C.
    • Applied Biological Chemistry
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    • v.38 no.3
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    • pp.248-253
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    • 1995
  • Optimum conditions for the enzymatic hydrolysis of isolated sesame meal protein were investigated. Optimum conditions by papain were $60^{\circ}C$, pH 6.0, 3% enzyme concentration to substrate and 1.5% substrate concentration, respectively. The optimum operating conditions using pepsin were $55^{\circ}C$, pH 9.0, 3% enzyme concentration to substrate and 1% substrate concentration. The optimum operating conditions using trypsin were $60^{\circ}C$, pH 9.0, 1% enzyme concentration to substrate and 1% substrate concentration.

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Study on Utilization of Animal By-products from Food Processing by Enzyme Treatment (효소를 이용한 동물성 식품가공부산물의 식품 소재화 탐색)

  • Chae, Hee-Jeong;In, Man-Jin
    • Applied Biological Chemistry
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    • v.47 no.2
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    • pp.197-201
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    • 2004
  • In order to recycle animal by-products from food processing as food seasonings, pig bone (PB), chicken bone (CB) and tuna dark flesh (TDF) were studied. PB and CB extract prepared by hot water extraction for 18 h were hydrolyzed with protease and lipase. The DHs of PB and CB extract were increased to 70% and 80%, respectively, when Flavourzyme was treated after pancreatic enzyme treatment. When TDF was hydrolyzed with Alcalase and Flavourzyme, dry matter yield and total protein yield were around 22% and 9%, respectively. Also the free ammo acid content in hydrolysate reached up to 27% of total solid. The sensory properties of three hydrolysates containing 1% NaCl were, in order of their overall acceptance, TDF, PB and CB. Therefore, tuna dark flesh turned out to be the suitable animal by-product as raw material for seasoning ingredient.

Enzymatic Hydrolysis Optimization of a Snow Crab Processing By-product (홍게 가공부산물의 효소적 단백질 가수분해 최적화)

  • Jang, Jong-Tae;Seo, Won-Ho;Baek, Hyung-Hee
    • Korean Journal of Food Science and Technology
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    • v.41 no.6
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    • pp.622-627
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    • 2009
  • The objectives of this study were to evaluate a protease suitable for the enzymatic hydrolysis of a snow crab processing by-product (SPB) and to optimize the hydrolysis conditions using response surface methodology (RSM). The SPB was hydrolyzed at $50^{\circ}C$ and pH 7.0-7.2 to obtain various degree of hydrolysis (DH) using Flavourzyme at an enzyme/substrate (E/S) ratio of 3.0%. The reaction progress curve exhibited an initial fast reaction rate followed by a slowing of the rate. The DH was increased to 30% at 90 min with a final DH 32 to 36%. A central composite experimental design having three independent variables (reaction temperature, reaction time, and E/S ratio) with five levels was used to optimize the enzymatic hydrolysis conditions. Based on the DH data, the optimum reaction conditions for the enzymatic hydrolysis of the SPB were a temperature of $51.8^{\circ}C$, reaction time of 4 hr 45 min, and an E/S ratio of 3.8%. It was demonstrated that the enzymatic hydrolysate of SPB could be used as a flavoring agent or a source of precursors for the production of reaction flavors.

Effect of Enzyme Treatments on the Extraction Efficacy and Antioxidant Activity of Haematococcus Extract from Haematococcus pluvialis (Haematococcus pluvialis로부터 Haematococcus 추출물 제조 공정에서 효소 처리가 추출 효율과 항산화 활성에 미치는 영향)

  • In, Man-Jin
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.10 no.1
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    • pp.194-199
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    • 2009
  • An efficient production method of food-grade heamatococcus extract was developed based on stepwise enzymatic hydrolysis. In the first step, Haematococcus pluvialis cells hydrolysis carried out with commercially available exopeptidase(Flavourzyme) and endopeptidase (Alcalase), resulted in increased astaxanthin content. In the second step, proteolytic hydrolyzed H. pluvialis cells treated with hetero-polysaccharides hydrolytic enzyme (Viscozyme). By two-stage treatments using Alcalase and Flavourzyme and Viscozyme, the highest astaxanthin content was obtained. The astaxanthin content was remarkably enhanced by 320% $(529{\mu}g/g\rightarrow2,256{\mu}g/g)$ than that of the non-treated extract. And then, antioxidative activities determined by DPPH method were increased with increasing the astaxanthin content in haematococcus extract prepared by enzymatic hydrolysis.

Characteristics of protein from red crab (Chionoecetes japonicus) shell by commercial proteases (효소적 가수분해에 의한 홍게껍질 단백질의 특성)

  • Noh, Kyung-Hee;Min, Kwan-Hee;Seo, Bo-Young;Kim, So-Hee;Seo, Young-Wan;Song, Young-Sun
    • Journal of Nutrition and Health
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    • v.45 no.5
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    • pp.429-436
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    • 2012
  • This study was performed to examine the characteristics of protein of red crab (Chionoecetes japonicus) shell powder hydrolyzed by commercial proteases. Red crab shell was digested by commercial proteases, such as Protamex (P), Neutrase (N), Flavourzyme (F), Alcalase (A), Protease M (PM) and Protease A (PA). Protein yield analyzed by Biuret assay, absorbance at 280 nm and brix revealed that PA was the enzyme having the highest proteolytic activity. SDS PAGE showed that molecular weight of proteins produced by protease treatments was various and below 150 kDa. Combinational treatment of proteases (PA + P, PA + PM, PA + F, PA + A) was tried whether these increase protein hydrolysis from red crab shell powder compared to a PA single treatment. Soluble protein content was similar, but amino acid concentration by combinational treatments was higher than PA single treatment [PA + P 247.4 mg/g > PA + F (206.4 mg/g) > PA + A (133.4 mg/g) > PA + PM (59.1 mg/g) > PA (54.9 mg/g)]. Amino acid composition by combinational treatments was slightly different. Most abundant essential amino acids were phenylalanine, glycine, alanine, and leucine, whereas tyrosine and cystine were not detected.

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

  • Choi, Dong Won;Kim, Nam Ho;Son, Kyung Bin
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.42 no.7
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    • pp.1162-1166
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    • 2013
  • Proteins from sunflower seeds were hydrolyzed with Alcalase and Flavourzyme to isolate iron-binding peptides. The optimal hydrolysis conditions were determined. Hydrolysates were filtered under a 3 kDa membrane and iron-binding peptides separated from the hydrolysates using ion exchange and gel permeation chromatographic methods. A fraction with the highest iron-binding activity (Fe/peptide, 0.69), F22, was obtained. These results suggest that fractions isolated from sunflower seed protein hydrolysates can be applied toward the production of iron supplements.

Reaction Characteristics and Kinetic Analysis of Enzymatic Hydrolysis of Corn Gluten Meal Using Alkaline Protease (Alkaline Protease를 이용한 Corn Gluten Meal의 효소가수분해 반응특성 및 반응속도론적 분석)

  • 김성진;이은규남충희
    • KSBB Journal
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    • v.10 no.5
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    • pp.540-546
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    • 1995
  • Dry corn gluten meal of 70% protein content was enzymatically hydrolyzed by alkaline protease in a pH-state reactor. Such process variables as temperature, pH, and enzyme-to-substrate ratio were varied, and at each condition degree of hydrolysis was monitored and calculated. The ultimate degree of hydrolysis, which ranged between 25 and 28% based on gluten protein mass, was not significantly affected by the process variables. However, $50^{\circ}C$ and pH 9-10 appeared optimum. Kinetic analysis indicated enzyme deactivation was negligible during the hydrolysis, and the experimental data were near perfectly fitted to the model kinetic equation which was modified after neglecting enzyme deactivation term. The enzyme reaction was 1$100\times$ scaled up and basically the same hydrolysis performance was resulted. Amino acid analysis showed the hydrolyzate was relatively rich in glutamine/glutamic acid, leucine, and alanine at 19.6, 16.1, and 12.3 mole %, respectively.

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Solubilization of Tofu-Residue Using Multienzyme Derived from Aspergillus niger CF-34 (Aspergillus niger CF-34 효소를 이용한 두부 또는 두유비지의 가용화)

  • Kim, Kang-Sung;Park, Eun-Ha;Choi, Yeon-Bae;Kim, Kyo-Chang;Lee, Sang-Hwa;Sohn, Heon-Soo
    • Korean Journal of Food Science and Technology
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    • v.26 no.5
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    • pp.484-489
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    • 1994
  • Solubilization of plant ceil wall(tofu-residue) using enzyme complex obtained by Aspergillus niger CF-34 was attempted. The hydrolysis reaction was done at pH 4.0, $50^{\circ}C$, which were optimum pH and temperature of the enzyme, respectively. At the enzyme dosage of 2.5% (in terms of solid content of tofu-residue) and reaction time of 3 hr, the solubilizing percent of protein and carbohydrate were 62% and 50% respectively. Homogenization prior to enzyme reaction did not have much effect on tofu-residue solubilization. To improve solubility of tofu-residue, additional treatment such as alkali with 0.1% NaOH solution was found to be useful. The results showed that tofu-residue, which mainly consists of cell wall component of cellulose and hemicellulose, was not accessible to enzyme reaction and some prior treatment is required to enhance enzyme hydrolysis.

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