• Korean journal of food and cookery science
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• v.9 no.4
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• pp.278-283
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• 1993

This study was attempted to investigate the effects of enzymatic modification of milk protein with protease on functional properties. The selected functional properties were solubility, emulsifying activity (EA), emulsion stability(ES), foam expansion(FE), and foam stability(FS). These properties were measu-red from pH 3.0 to pH 8.0. The proteases used in this study were iaolated from Meju(fermemted soybean) and had specific activity of 250 units/㎎ protein at pH 7.0, 1600 units of pretense was used for 1gr. of skim milk protein. Skim milk showed 30.5％ degree of hydrolysis for 1 hr. and 36.4% degree of hydrolysis for 3.5 hrs. of protease treatment at pH 7.0. Solubility of native skim milk, control, 1 hr. and 3.5 hrs. groups were 3.37, 3.64, 10.21, 14.34％o at pH 4.0 respcetively. The emulsifying activity of native skim milk, control, 1 hr. and 3.5 hrs. groups were 38.8,42.0,43.0,46.7ft at pH 4.0, respectively. Enzymatic modification resulted in the increase of solubility and emulsifying activity at pH 4.0. However at pH 5.0 emulsifying activity of 1 hr. and 3.5 hr. group were lower than native skim milk and control groups. 1 hr. protease treatment was found to be most effective way of increasing foam expansion at pH 4.0 to 6.0. It was supported that, protease treated skim milk can be used to improve solubility, emulsifying activity, foam expansion at acid pH. meju protease. skim milk, solubility, emulsion, foam.

• Journal of Pharmacopuncture
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• v.17 no.1
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• pp.44-50
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• 2014

Objectives: This study was undertaken to isolate a fibrinolytic enzyme from the snake venom of Gloydius blomhoffii siniticus and to investigate its enzymatic characteristics and hemorrhagic activity as a potential pharmacopuncture agent. Methods: The fibrinolytic enzyme was isolated by using chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and fibrin plate assay. The characteristics of the enzyme were investigated using fibrin plate assay, protein hydrolysis analysis, and hemorrhage assay. Its amino acid composition was determined. Results: The fibrinolytic enzyme with the molecular weight of 32kDa (FE-32kDa) from Gloydius blomhoffii siniticus showed a fibrin hydrolysis zone at the concentration of 0.2 mg/mL in the fibrin plate assay. The fibrin hydrolysis activity of the enzyme was inhibited completely by ethylenediaminetetraacetic acid (EDTA), ethyleneglycoltetraacetic acid (EGTA), and 1, 10-phenanthroline, thiothreitol and cysteine, and partially by phenylmethanesulfonylfluoride (PMSF). Metal ions such as $Fe^{2+}$ and $Hg^{2+}$ inhibited the fibrin hydrolysis completely, but $Zn^{2+}$ enhanced it. FE-32kDa hydrolyzed ${\alpha}$-chain but did not hydrolyze ${\beta}$-chain and ${\gamma}$-chain of fibrinogen. High-molecular-weight polypeptides of gelatin were hydrolyzed partially into low-molecular-weight polypeptides, but the extent of hydrolysis was limited. FE-32kDa induced hemorrhage beneath back skin of mice at the dose of $2{\mu}g$. Conclusions: FE-32kDa is a ${\alpha}$-fibrin(ogen)olytic metalloprotease that requires $Zn^{2+}$ for fibrinolytic activity and causes hemorrhage, suggesting that the enzyme is not appropriate for use as a clinical pharmacopuncture.

• The Korean Journal of Mycology
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• v.9 no.1
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• pp.25-29
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• 1981

To investigate antitumor components of Korean higher fungi, the carpophores of Schizophyllum commune and Auricularia auricula-judae collected in Kyeong Buk Province were extracted with hot water or 0.1N-NaOH solution. The concentrated extracts were precipitated by addition of ethanol, and the precipitates were purified by dialyzing through visking tube and polysaccharide fractions were obtained. They were found to show antitumor activity against sarcoma 180 implanted in mice. Especially, the inhibition ratio of the extract of Auricularia adicula-judae was 90.8% in the doses of 100mg/kg/day for the period of ten days. The tumor in five of the eight mice was completely regressed. The components of these aqueous extracts were found to be polysaccharide and protein. The hydrolysis of the respective polysaccharide yielded four monosaccharides. After hydrolysis of the protein fraction, 15 amino acids were identified in the respective fraction of S. commune and A. auricula-judae.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.332-339
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• 2010

The lipase from Mucor racemosus NRRL 3631 was partially purified by fractional precipitation using 60% ammonium sulfate, which resulted in a 8.33-fold purification. The partially purified lipase was then immobilized using different immobilization techniques: physical adsorption, ionic binding, and entrapment. Entrapment in a 4% agar proved to be the most suitable technique (82% yield), as the immobilized lipase was more stable at acidic and alkaline pHs than the free enzyme, plus 100% of the original activity was retained owing to the thermal stability of the immobilized enzyme after heat treatment for 60 min at $45^{\circ}C$. The calculated half-lives (472.5, 433.12, and 268.5 min at 50, 55, and $60^{\circ}C$, respectively) and the activation energy (9.85 kcal/mol) for the immobilized enzyme were higher than those for the free enzyme. Under the selected conditions, the immobilized enzyme had a higher $K_m$ (11.11 mM) and lower $V_{max}$ (105.26 U/mg protein) when compared with the free enzyme (8.33 mM and 125.0 U/mg protein, respectively). The operational stability of the biocatalyst was tested for both the hydrolysis of triglycerides and esterification of fatty acids with glycerol. After 4 cycles, the immobilized lipase retained approximately 50% and 80% of its original activity in the hydrolysis and esterification reactions, respectively.

• KSBB Journal
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• v.28 no.3
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• pp.151-156
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• 2013

${\beta}$-Glucan type oligomers which have angiotensin I converting enzyme (ACE) inhibitory activity were isolated and characterized from Capsosiphon fulvescens. After C. fulvescens was hydrolysis with Alcalase at $50^{\circ}C$, supernatant was harvested and separated with ultrafiltration membrane (MWCO 2 kDa). Oligomers which were less than 2 kDa of molecular weight were harvested for characterization. The nutrient composition of Alcalase hydrolysate was 89.9% carbohydrate, 4.2% protein and 5.9% sulfate. After ultrafiltration, the nutrient composition of oligomers was changed to 99.88% carbohydrate, 0.07% protein and 0.05% sulfate. The carbohydrate composition of oligomer was glucose (97.2%) and mannose (1.5%). The ACE inhibitory activities of Alcalase hydrolysate and oligomer were 72.1% and 82%, respectively. The molecular weight of oligomer was about 1 kDa. The oligomer was analyzed with FT-IR, $^1H$-NMR and methylation. The oligomers were ${\beta}$-1,3-glucans with ${\beta}$-(1,3)-linked glucose units.

• The Korean Journal of Food And Nutrition
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• v.6 no.3
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• pp.189-198
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• 1993

This study was carried out to investigate the effect of medium-cooked rice on brewing of yakju which was a traditional rice wine in Korea. The influences of cooking temperature of rice on hydrolysis of rice starch and rice protein were tested, and experimental brewings were done according to the traditional brewing method of Bangmunju in which some medium-cooked rice was used. The results obtained were as follows The hydrolysis of starch and protein in medium-cooked rice at 60~$65^{\circ}C$ was easier than that of full-cooked rice at 80~10$0^{\circ}C$. The amounts of saccharides, total amino acids and extracts In Yakju brewed with the combined use of medium-cooked rice and full-cooked rice were twice as much as those brewed with full-cooked rice only. The results of sensory test of Yakju brewed with the combined use of medium-cooked rice and full-cooked rice were better in taste, color and flavor than those brewed with full-cooked rice only. It was thought that our ancestor's traditional brewing method of Yakju in which medium cooked rice and full-cooked rice were used combinedly was excellent Judging from zymological point of views.

• Preventive Nutrition and Food Science
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• v.10 no.2
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• pp.134-139
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• 2005

Seven brown algal species (Ecklonia cava, Ishige okamurae, Sargassum fulvellum, Sargassum horneri, Sargassum coreanum, Sargassum thunbergii and Scytosiphon lomentaria) were hydrolyzed using five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and screened for angiotensin 1-converting enzyme (ACE) inhibitory activities. Most algal species examined showed good ACE inhibitory activities after the enzymatic hydrolysis. However, E. cava was the most potent ACE inhibitor of the seven species. Flavourzyme digest of E. cava exhibited an $IC_{50}$ of around $0.3\;{\mu}g/mL$ for ACE; captopril has an $IC_{50}$ of $\~0.05\;{\mu}g/mL$. The Flavourzyme digest was separated to three fractions by an ultrafiltration membrane (5, 10, 30 kDa MWCO) system according to the molecular weights. The active components were mainly concentrated in >30 kD fraction which are composed of the highest protein content $(27\%)$ and phenolic content (261 mg/100 mL) compared to the other two smaller molecular weight fractions. Therefore, the active compounds appear to be relatively high molecular weight complex molecules associated with protein (glycoprotein) and polyphenols. Therefore, E. cave is a potential source of antihypertensive compound.

• The Korean Journal of Food & Health Convergence
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• v.6 no.6
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• pp.1-7
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• 2020

We compared the fermentation of 0 to 4 weeks by manufacturing a rapid low salt-fermented seahorse with a commercial Protamex added to the functional food, Hippocampus abdominalis. We studied amino acid composition, content and major amino acids related to flavor during the fermentation process of salt-fermented seahorse. In the enzyme-free group, it showed little change in the content of non-protein nitrogenous compounds, the content of amino acids and degree of hydrolysis. The Protamex enzyme treatment group was rapidly hydrolyzed in one week of ripening, resulting in increased non-protein nitrogenous compounds content, amino acid content and degree of hydrolysis, and minimal changes in the four weeks. The total amino acid contents ratio showed the highest content of glutamic acid in the enzyme additive group, glycine, alanine, which indicates sweet taste, and serine, the content of glycine, alanine, serine, and lysine, indicating sweet taste, has increased significantly over the enzyme-free group. Twenty species of free amino acid in the four-week of salt-fermented seahorse were detected. It detected 43.0% (6 species) in the enzyme-free group and 63.96% (7 species) in the enzyme additive group.

• Journal of Dairy Science and Biotechnology
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• v.39 no.1
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• pp.36-50
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• 2021

This study aimed to evaluate the biological potential of functional food, i.e., specific peptides obtained from the hydrolysis of milk protein, by assessing their antioxidant and antibacterial properties. For the preparation of casein hydrolysates, commercial enzymes were added to 10% casein solution in a 1:200 (w/v) ratio, and samples were collected each hour. Based on the assessment of the degree of hydrolysis (DH) of casein hydrolysates, it was observed that the concentration of all enzymatic hydrolysates increased rapidly from 30 to 40 minutes. However, no change was observed in their concentrations after 150 minutes. Protamex® and Neutrase® exhibited the highest DH when compared to other enzymes. Furthermore, SDS-PAGE was performed for analyzing the proteolytic pattern of each enzyme, except for Flavourzyme®, and peptides in the size range of 20-25 kDa were identified. Subsequently, peptides produced by two enzymes were isolated using a preparative liquid chromatography system. Overall, NF3, NF4, PF5, and PF6 showed higher antioxidant potential than other peptide fractions. Moreover, NF7 and PF3 exhibited the highest antibacterial activity. In this study, we evaluated the biological potential of novel casein-derived peptides that may find application in the food and healthcare industry.

• Fisheries and Aquatic Sciences
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• v.20 no.7
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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.