• Food Science and Preservation
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• v.19 no.3
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• pp.438-442
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• 2012

To prepare calcium-binding peptides as calcium supplement, barley proteins were hydrolyzed using Flavourzyme for 18 h and the hydrolysates were ultra-filtered under 3 kDa as a molecular weight. The resultant filtered peptides were fractionated using ion exchange and normal-phase high performance liquid chromatography. Then each fraction that was obtained was determined for its calcium-binding activity to isolate the calcium-binding peptides. As a result, the highest calcium-binding peptide fraction was obtained, and the results suggest that barley protein hydrolysates can be used as a calcium supplement.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.1
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• pp.35-39
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• 1998

An enzymatic process was developed to produce protein hydrolysater form defatted soya protein. Various unit operations were tried, and the effects of pre- and post-treatments on the product characteristics such as degree of hydroylsis (DH), free amino acid content (%FAA) and average molecular weight (MW) were investigated. The use of acid washes showed no difference in %DH. Increasing pH during pre-cooking gave lower %DH. Alkaline cooking made too much insoluble protein, thus the protein yield was too small. A better hydrolysis with more acceptable taste was obtained when the combination of Neutrase/Alcalase/Flavourzyme was used in place of Alcalase/Flavourzyme combination; Untoasted defatted soya was more effective on the proteolysis than toasted one. The MW of the evaporated and spray dried product was higher than that of undried product, due to precipitation of low-solubility components. When ultrafiltration and the product concentration carried out the product separation by reverse osmosis, the solubility and the taste of the product were improved. The difference between enzyme hydrolysate and acid hydrolysate was significant in free amino acid composition, especially in tyrosine, phenylalanine, glutamine and asparagine.

• Food Science and Biotechnology
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• v.17 no.4
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.

• Journal of the Korean Applied Science and Technology
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• v.34 no.2
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• pp.338-348
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• 2017

Protein hydrolysates derived from plants and animals having antioxidant, suppression of hypertension, immunodulatory, alleviation of pain, and antimicrobial activity has been known as playing important role like hormone. This study was performed to optimize the hydrolysis of protein of sea of cucumber by a flavourzyme. The ranges of processes were the reaction temperature of 40 to $60^{\circ}C$, pH 6 to 8, and enzyme concentration 0.5 to 1.5%(w/v). As a result, the optimization of process was determined at temperature of $48-50^{\circ}C$, pH of 7.0-7.2, and enzyme concentration of 1.0-1.1%(w/v), and degree of hydrolysis was 43-45 at above conditions. The molecular weight of hydrolysate was distributed to 500-3,500 Da and showed typical peptides. Inhibition concentration ($IC_{50}$) of peptides of DPPH radical scavenging activity, Superoxide anion radical scavenging activity, Hydroxy radical scavenging activity, $Fe^{2+}$ cheating activity was 1.25, 3.40, 10.3, and 22.11 mg/mL, respectively. Therefore, we expect that those products are useful as functional food ingredients.

• Journal of the Korean Society of Food Science and Nutrition
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• v.45 no.9
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• pp.1279-1284
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• 2016

To obtain enzyme hydrolyzed vegetable protein (EHVP) with a salty and umami taste, defatted soybean meal was treated with proteases such as Flavourzyme$^{(R)}$ (F), Neutrase$^{(R)}$ (N), Alcalase$^{(R)}$ (A), and Protamex$^{(R)}$ (P) in various reaction orders. The highest soluble solid content of EHVP was 5.60% in enzyme reaction order NAFP although there was no significant difference. Amino type nitrogen was highest in ANFP (102.76 mg%) and APNF (102.85 mg%). In the sensory descriptive analysis, salty taste was highest in PNFA (11.81), followed by NPAF (10.14), FPNA (10.00), APNF (9.80), NAFP (9.76), AFNP (9.57), APFN (9.52), and NPFA (9.50) with no significant difference among treatment. Umami taste was not significantly different among the various enzyme treatments. Bitter aftertaste was highest in AFPN (5.67) and lowest in FAPN (2.38), PNAF (2.62), and NAPF (2.48). In the principle component analysis, EHVPs of PNFA, NAFP, APFN, NPAF, FPNA, NPFA, and APNF showed a strong salty and umami taste. Therefore, the PNFA, NAFP, APFN, NPAF, FPNA, NPFA, and APNF are desirable methods for making EHVP with a salty and umami taste.

• Journal of Animal Science and Technology
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• v.52 no.5
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• pp.435-440
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• 2010

Whey protein concentrate (WPC) is widely used to increase the nutritional and functional properties of food. In this study, the physiochemical and functionality of WPC-30 hydrolysates were examined to evaluate the possibility of application in the food industry. The WPC-30 was manufactured using ultrafiltration and spray-drying, and then hydrolyzed with proteolytic enzyme including alcalase, flavourzyme, nuetrase and protamex. Enzymatic hydrolysis had a significant influence on the physicochemical properties as evident from the increased foaming capacity, solubility. Alcalase caused highest protein hydrolysis (3.26%) and the bitterness. Foaming capacity was largest in WPC-30 hydrolysate treated with flavourzyme. Protein solubility at various levels of pH was highest in protamex-treated WPC-30 hydrolysate. However, the solubility of WPC-30 hydrolysates was significantly improved in alkaline condition than in acidic and neutral conditions. The study revealed that spray dried enzyme modified WPC can be used in various functional food.

• Journal of Applied Biological Chemistry
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• v.53 no.3
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• pp.174-178
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• 2010

Calcium and iron binding peptides were prepared by enzymatic hydrolysis and ultrafiltration of rice bran protein (RBP), which was isolated from defatted rice bran by phytase and xylanase treatment and ultrasonication. The isolated RBP had a molecular weight in the range of 10-66 kDa. The extracted proteins were hydrolyzed using Flavourzyme for 6 hr. After ultrafiltration under 5 kDa as molecular weight, the peptides were fractionated into 4 peaks by Sephadex G-15 gel permeation chromatography, and each fraction was determined for calcium and iron binding activity. As the result, Fl and F2 fractions were the best candidate for calcium and iron chelation, respectively. These results suggest that the calcium and iron binding peptides can be used as functional food additives in food industry.

• Journal of Applied Biological Chemistry
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• v.55 no.4
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• pp.263-266
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• 2012

Isolation of iron and calcium-binding peptides derived from cottonseed meal protein (CMP) hydrolysates was investigated. The degree of hydrolysis of CMP by Flavourzyme was monitored using trinitrobenzenesulfonic acid method and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Enzymatic hydrolysis of CMP for 12 h was sufficient for the preparation of CMP hydrolysates, and the hydrolysates were membrane-filtered under 3 kDa as a molecular weight. The filtered solution was fractionated using Q-Sepharose fast flow, Sephadex G-15, and reversed phase-high performance liquid chromatography for iron and calcium-binding peptides. As a result, F51 fraction was obtained as the best candidate for calcium and iron chelation, and the isolated iron and calcium-binding peptides can be used as functional food additives, similar to iron and calcium supplements.

• Fisheries and Aquatic Sciences
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• v.14 no.1
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• pp.1-10
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• 2011

This study was conducted to obtain hydrolysates with potent antioxidative activity from rockfish skin gelatin. Gelatin was extracted under high temperature/high pressure using a two-step enzymatic hydrolysis with commercial enzymes such as Alcalase, Flavourzyme, Neutrase, and Protamex. The second rockfish-skin gelatin hydrolysate (SRSGH) was prepared by further incubating the first gelatin hydrolysate (FRSGH), which had been hydrolyzed with Alcalase for 1-h (FRSGH-A1), with Flavourzyme for 2-h (SRSGH-F2). The second gelatin hydrolysate showed higher antioxidative activity of 3.72 as measured by a Metrohm Rancimat and superior angiotensin I-converting enzyme (ACE) inhibiting activity of 0.82 mg/mL. Compared with the gelatin, the relative proportion in SRSGH-F2 was markedly decreased in the 100-kDa peak, whereas it was increased in that less than 100-kDa. The amino acid composition of SRSGH-F2 was rich in glycine (25.9%), proline (10.8%), alanine (9.1%), and glutamic acid (9.1%). In contrast, it was poor in cystine (not detected), methionine (1.6%), tyrosine (0.4%), hydroxylysine (0.9%), and histidine (0.9%). In recent years, demand for natural functional foods has been increasing, and SRSGH-F2 can be used as a functional food ingredient in the food industries. However, further detailed studies on SRSGH-F2 with regard to its antioxidant activity in vivo and the various antioxidant mechanisms are needed.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.40 no.4
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• pp.341-347
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• 2014

This study was aimed to investigate skin whitening effects of Nomura's jellyfish (Nemopilema nomurai) hydrolyzed extracts (NHE). The extracts were prepared through the hydrolysis of N. nomurai using commercial proteolytic enzymes such as Protamex, Alcalase, Flavourzyme and Neutrase with optimum pHs (pH 5-8) at $55^{\circ}C$. Their whitening activities were examined from the inhibition of melanin synthesis using B16-F1 cell lines. Among the examined samples, Neutrase-treated extract (N-NHE) showed the most significant inhibition effect on melanin synthesis by 89.9% at a concentration of $100{\mu}g/mL$. This sample decreased the expression of tyrosinase and TRP-1 (tyrosinase related protein-1) proteins as well. These results suggested the potential application of NHE as whitening ingredients in cosmetic preparation.