• Korean Journal of Food Science and Technology
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• v.29 no.5
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• pp.1052-1056
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• 1997

When casein was hydrolyzed by trypsin, alcalase, neutrase, protamax, and S. aureus type V8, peptides $(100\;{\mu}g/mL)$ which were produced by trypsin and alcalase solubilized $6.42\;and\;2.37\;{\mu}g/mL)$ of added irons at pH 6, respectively, while peptides which were produced by other proteases solubilized less than $1\;{\mu}g/mL$. Peptides produced by trypsin and alcalase were fractionated to 10 fractions on a reverse phase column and each fraction was tested for its iron solubilizing ability at pH 6. Among peptides produced by trypsin, fraction 5 showed the highest iron solubilizing ability $(2.33\;{\mu}g/mL)$. In the case of alcalase, fraction 7 showed the highest iron solubilizing ability $(1.56\;{\mu}g/mL)$. To isolate iron binding peptides from peptides produced by trypsin and alcalase, immobilized iron affinity chromatography which irons were chelated to imino diacetic acids in chelating sepharose fast flow were utilized. Our results showed that immobilized iron affinity chromatography was an effective method to isolate iron binding peptides produced by either trypsin or alcalase from milk casein.

• Journal of the Korean Society of Food Science and Nutrition
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• v.36 no.7
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• pp.881-888
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• 2007

For the use of skipjack tuna cooking drip (STC) as a source of functional seasoning, the STC was hydrolyzed with various commercial enzymes, such as Alcalase, Flavourzyme, Neutrase and Protamex, and its hydrolysate was also investigated on the food component characteristics. The hydrolysate incubated with Alcalase for 30 min (HA30) showed 56.8% for angiotensin I converting enzyme (ACE) inhibitory activity and 1.18 for antioxidative activity, which were high or similar compared to the other enzymatic hydrolysates. There were no differences in ACE inhibitory activity and antioxidative activity among HA30, two-step enzymatic hydrolysates, and ultrafilterates (molecular weight cut off, 10 kDa). The HA30 was very stable on the digestive enzymes, such as chymotrypsin, pepsin, trypsin according to the TCA (trichloroacetic acid) soluble index. The results suggested that skipjack tuna cooking drip could be used as a source for preparing functional seasoning sauce.

• Journal of the Korean Society of Food Science and Nutrition
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• v.36 no.8
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• pp.1022-1030
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• 2007

For the improvement on the quality and functionality of red tanner crab cooking drip, the preparation of hydrolysates from red crab cooking drip using commercial enzymes (Alcalase, Flavourzyme, Neutrase and Protamex) was attempted and its taste, nutritional and functional characteristics were also investigated. According to the results of heavy metal contents and proximate composition, red tanner crab cooking drip (RTCCD) could be used as a food resource. From the results of the trichloroacetic acid soluble index (TSI), angiotensin I converting enzyme (ACE) inhibiting activity and antioxidative activity, RTCCD hydrolysates incubated with Alcalase for 2 hrs was superior to the other one-step hydrolysates. There were no differences in the ACE inhibiting activity and antioxidative activity between one-step hydrolysates, which was incubated with Alcalase for 2 hrs, and two-step hydrolysates sequentially incubated with Alcalase and other enzymes. Alcalase-treated hydrolysates was similar in proximate composition and Hunter color value, while high in free amino acid content compared with crab cooking drip. Total amino acid content of Alcalase-treated hydrolysates was 11.9 g/100 mL and the major amino acids were glutamic acid (10.2%), proline (10.1%) and glycine (10.7%).

• Journal of Life Science
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• v.16 no.1
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• pp.49-57
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• 2006

Enzymatic extracts were prepared from the blueberry (Vaccinium corymbosum L.) collected in Jeju, Korea. Five carbohydrases namely AMG, Celluclast, Termamyl, Ultraflo and Viscozyme, and five proteases namely Alcalase, Flavourzyme, Kojizyme, Neutrase and Protamex were used to prepare the enzymatic extracts. Antioxidant properties of each extracts were studied using stable 1,1-diphenyl 2-picrylhydrazyl (DPPH), reactive oxygen species (ROS), nitric oxide (NO) scavenging, metal chelating assays and lipid peroxidation inhibitory activity in hemoglobin-induced linoleic acid system. The phenolic content of all enzymatic extracts was in the range of 517.85-597.96 mg/100 g dried sample. DPPH and NO${\cdot}$scavenging, and metal chelating assays exhibited prominent activities. Viscozyme showed the highest DPPH activity $(0.046{\pm}0.002\;mg/mL)$ while AMG Showed the highest activity in NO${\cdot}$scavenging $(0.339{\pm}0.011\;mg/mL)$. All the extracts exhibited strong metal chelating activities. Blueberry enzymatic extracts also showed relatively good activity in hydrogen peroxide scavenging. AMG showed the highest lipid peroxidation inhibitory activity $(0.28{\pm}0.01\;mg/mL)$ in hemoglobin-induced linoleic acid system. In this results, the blueberry, which has potential antioxidant components, may be a good candidate as a natural antioxidant source.

• Journal of Dairy Science and Biotechnology
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• v.21 no.2
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• pp.97-104
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• 2003

It is extremely important to destroy the antigenicity of milk proteins for dietetic treatment of infants with milk allergy. Enzymatic digestion of milk protein is not only effective for destroying antigenicity, but it also is less liable to alter the nutritive value. Bovine casein was hydrolyzed with eight different commercial proteases derived from bacterias or fungi, either individually or in combination to eliminate protein allergenicity. The average molecular weight of casein hyrdolysates determined by size exclusion chromatography is about 550${\sim}$2,300 dalton range. Antigenicity of the casein hyrdolysates was not detected by heterologous passive cutaneous anaphylaxis in guinea pig-rabbit antiserum system. The inhibition test on the enzyme-linked immunosorbent assay(ELISA) showed that the antigenicity of casein hydrolysates is lowed up to 1/8,000 than that of intact bovine casein. As the enzyme reaction was carried out by the combination of bacterial and fungal protease, casein hydrolysates showed much lower bitterness and antigenicity. It suggests that these hydrolysates will be applied to many kinds of foods including the development of hypo-allergenic infant formula.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.7
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• pp.919-925
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• 2006

The study was carried out to prepare oyster hydrolysates by using Alcalase, Flavourzyme, Neutrase, Protamex, pepsin and trypsin, and to investigate its functional properties. The ACE inhibitory activity and antioxidant activity of enzymatic oyster hydrolysates did not increase with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex for 1 hr (OHP) showed the most excellent ACE inhibitory activity and antioxidant activity, and their $IC_{50}$ values were 1.16 mg/mL and 1.49 mg/mL, respectively. However, all enzymatic oyster hydrolysates were not detected in antimicrobial activity.

• Journal of Marine Bioscience and Biotechnology
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• v.7 no.1
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• pp.19-27
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• 2015

The objective of the current study was to evaluate the inhibitory and antioxidant activities of powdered katsuobushi (dried bonito) protein hydrolysates and their corresponding fractions. The powdered katsuobushi (dried bonito) hydrolysates were obtained by enzymatic hydrolysis using Alcalase, ${\alpha}$-chymotrypsin, Neutrase, pepsin, papain, and trypsin. The antioxidant efficacy of the respective hydrolysates were evaluated using 2,2-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, superoxide, and alkyl radical-scavenging activities. Among the hydrolysates, the peptic-derived hydrolysate exhibited the highest antioxidant activity compared to other enzymatic hydrolysates. Therefore, the peptic-derived hydrolysate was further analyzed, and was found to contain an active peptide with an amino acid sequence identified as Pro-Met-Pro-Leu-Asn-Ser-Cys (756 Da). The purified peptides from powdered katsuobushi (dried bonito) had an $EC_{50}$ value of $105.82{\mu}M$, and exhibited an inhibitory effect against DNA oxidation induced by hydroxyl radicals. Taken together, these results suggests that powdered katsuobushi (dried bonito) could be used as a natural antioxidant in functional foods and prevent oxidation reactions in food processing.

• ALGAE
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• v.19 no.1
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• pp.59-68
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• 2004

Hizikia fusiformis hydroysates by five carbohydrases (Viscozyme, Celluclast, Termamyl and Ultraflo) and five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) were investigated for their extraction efficacy (yield and total total polyphenolic content) and antioxidative activity (DPPH radical and hydrogen peroxide scavenging activity). Termamyl and Ultraflo of the carbohydrases and Flavourzyme and Alcalase of proteases were selected by their high eficacy of extraction and antioxidative activity. Selected enzymes were used to investigate the optimum enzymatic reaction time and dosage (enzyme/substrate ratio) suitable for hydorolysis. Optimum reaction time for the enzymatic hydrolysis was 3 days and optimum dosage of hydrolysis was observed as 5%. Simultaneously, Ultraflo of the two carbohydrases and Alcalse of the two proteases were selected as the most effective enzymes. Combination of Ultraflo and Alcalase under optimum hydrolysis conditions could intensify the extraction efficacy of antioxidative materials form H. fusiformis. The hydrolysate obtained by combining the enzymes was separated into four different molecular weight fractions (<1kD, 1-10 kD, 10-30 kD and >30 kD) and recorded the polyphenolic content distribution and respective antioxidative ability. The fraction <1kD was identified as less effective and those fractions > 1kD indicated comparatively higher antioxidative activities related to their polyphenolic content.

• KSBB Journal
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• v.15 no.1
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• pp.55-59
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• 2000

Protease-catalyzed liberation of sialyloligosaccharide from raw egg yolk was investigated in biphasic system, water-immiscible hexane system. Biphasic system 1, in which water was the continuous phase, was better than the opposite biphasic system ll in sialyloligosaccharide liberation. The optimal conditions of temperature, water content and reaction time were $30^{\circ}C$, 20% and 12 hours, respectively. Protease activity was strongly influenced by the amount of water present in the reaction mixture. The liberation of sialyloligosaccharide was accelerated by protease pre-treatment at $30^{\circ}C$ in 0.2 M NaCl solution, prior to addition of hexane (Biphasic system I).

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.623-625
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• 2000

Bacteriocin-producing lactic acid bacteria was isolated from Kimchi using MRS as selective media and Lactobacillus delbruekii subsp. delbruekii as an indicator strain. Strain JC-3 was tentatively identified as Lactococcus latis subsp. lactis through the API test and the bacteriocin produced by JC-3 showed the inhibitory activity against Grampositive pathogens and other lactic acid bacteria. The antimicrobial substance was inactivated by Protamax, Aroase AP-10, Neutrase, R-AMANO and was confirmed to be heating at $100^{\circ}C$. However, it was lost at high pH values showed the highest bacteriocin activity at a culture temperature of $30^{\circ}C$. The bacteriocin was partially purified by ammonium sulfate precipitation, Sep-pak $C_{18}$ cartridge. The apparent molecular mass of the bacteriocin was about 8 Kda, which was determined through the direct detection of bactericidal activity using SDS -PAGE.