• Korean Journal of Fisheries and Aquatic Sciences
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• v.42 no.6
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• pp.537-544
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• 2009

This study was conducted to improve yield and functional properties of autoclave-treated salmon frame extracts (SFETA) using commercial enzymes (Alcalase 2.4 L FG, Flavourzyme 500 MG, Neutrase 0.8 L and Protamex 1.5 MG). Yield and angiotensin I converting enzyme (ACE) inhibitory activity of all enzymatic hydrolysates improved compared to those of control (undigested extracts), which were the highest in hydrolysates incubated with Protamex 1.5 MG for 4 hrs (P4-treated hydrolysates) and 2 hrs (P2-treated hydrolysates), respectively. However, antioxidant activities of all enzymatic hydrolysates showed less than 29%. According to the trichloroacetic acid soluble-N, volatile component intensity and sensory evaluation, when compared to control, taste of P4-treated hydrolysates improved, while its fish odor strongly smelt. Therefore, for efficient use of P4-hydrolysates, the fish odor should be improved by Maillard reaction of extracts or pre-treatment of salmon frame.

• 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.

• Journal of Life Science
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• v.22 no.1
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• pp.117-125
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• 2012

This study investigated the potential hepatoprotective benefits of Crassostrea gigas oyster hydrolysates. Oysters are known to have many biofunctional properties. In particular, oyster enzymatic hydrolysates produce substances with beneficial functions. The potential hepatoprotective effects of C. gigas hydrolysates against damage induced by tacrine were evaluated in vitro in HepG2 cells. Peptides were generated from C. gigas by enzymatic hydrolysis with Neutrase, Flavourzyme, or Protamex enzyme preparations. Tacrine treatment induced considerable cell damage in HepG2 cells, as shown by significant leakage of glutamic oxaloacetic transaminase (GOT) and lactate dehydrogenase (LDH). Cells treated with C. gigas hydrolysates showed an increased resistance to oxidative challenge compared to control cells, as revealed by higher cell survival against tacrine-induced hepatotoxicity. In addition, treatment with C. gigas hydrolysates reduced the leakage of GOT and LDH. These findings indicate that enzyme hydrolysates derived from C. gigas may be of benefit for developing hepatoprotective foods and drugs.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.39 no.3
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• pp.269-277
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• 2006

This study prepared functional oyster hydrolysates using two-step enzymatic hydrolysis and investigated their functional properties. To prepare two-step enzymatic hydrolysates (TSEH), oysters were hydrolyzed using 1% Protamex (PR) at $40^{\circ}C$ and pH 6.0 for 1 hr before sequential treatment with one of the following enzymes for 1 hr: Alcalase (AL), Flavourzyme (FL), Neutrase (NE), pepsin (PE), and trypsin (TR). The PRAL, PRNE and PRTR hydrolysates had significantly greater angiotensin I converting enzyme (ACE) inhibitory activity than did PR and the other TSEHs. Only the antioxidant activity of the PRNE hydrolysate was significantly different (p<0.05), while none of the TSEHs had antimicrobial activity. The oyster hydrolysate prepared by sequential treatment with Protamex and Neutrase (PRNE) had the best ACE inhibitory activity and antioxidant activity, with $IC_{50}$ values of 0.40 and 0.94 mg/mL, respectively. The PRNE hydrolysate was processed through an ultrafiltration (UF) series with molecular weight cut-off (MWCO) membranes of 3, 5, 10, and 30 kDa, and the ACE inhibitory, antioxidant, and antimicrobial activities of the permeates were determined. The permeate through the 3-kDa MWCO membrane had greater ACE inhibitory activity and antioxidant activity than did the other PRNE permeates, with $IC_{50}$ values of 0.11 and 0.40 mg/mL, respectively.

• Food Science and Biotechnology
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• v.16 no.4
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• pp.565-571
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• 2007

This study was carried out to investigate an optimum condition for the high angiotensin-l converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity, Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The $R^2$ value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The $R^2$ value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.

• Journal of the Korean Society of Food Science and Nutrition
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• v.44 no.11
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• pp.1645-1652
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• 2015

We investigated the anti-wrinkle efficacy of hydrolysate from oyster protein by Protamex and Neutrase for the purpose of finding materials to assist skin health originating from marine organisms. There were about 7.9% free amino acids in the oyster hydrolysate, and contents of urea, taurine, alanine, and glycine were high. Oyster hydrolysate also showed collagenase inhibitory activity and was not toxic to CCD986sk human fibroblast cells. Yield of the fractions according to the molecular weight of oyster hydrolysate was 40% for less than 1,000 Da and 60.4% for less than 5,000 Da, respectively. Antioxidative effect, procollagen production, and matrix metalloproteinase-1 inhibitory activity were highest in 1,000~3,000 Da fractions. We observed that oyster hydrolysate and its less than 5,000 Da fraction are potential functional compounds for skin health and for improving wrinkles.

• Preventive Nutrition and Food Science
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• v.5 no.3
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• pp.148-152
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• 2000

Mussel adhesive protein (MAP) was extracted from Korean Mytilus edulis and then partially purified using Sephacryl S-300 gel permeation chromatography and reversed-phase high performance liquid chromatography. As an indicator of adhesiveness, is 3,4-dihydroxyphenylalanine (DOPA) content was determined. Its DOPA/protein ratio of 0.19 was higher than those of other reports, indicating a good adhesive. The partially purified MAP was confirmed by acid-urea polyacrylamide gel electrophoresis using cetylpiridinium bromide as a cationic detergent. Sea mussel hydrolysates were prepared using three commercial proteases to provide value-added functional materials and their angiotensin converting enzyme (ACE) inhibitory activities were determined. Among hydrolysates of sea mussel, Protamex was the best and further purification would improved ACE inhibitory activity.

• Nutrition Research and Practice
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• v.4 no.3
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• pp.183-190
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• 2010

Blueberry was enzymatically hydrolyzed using selected commercial food grade carbohydrases (AMG, Celluclast, Termamyl, Ultraflo and Viscozyme) and proteases (Alcalase, Flavourzyme, Kojizyme, Neutrase and Protamex) to obtain water soluble compounds, and their protective effect was investigated against $H_2O_2$-induced damage in Chinese hamster lung fibroblast cell line (V79-4) via various published methods. Both AMG and Alcalase hydrolysates showed higher total phenolic content as well as higher cell viability and ROS scavenging activities, and hence, selected for further antioxidant assays. Both AMG and Alcalase hydrolysates also showed higher protective effects against lipid peroxidation, DNA damage and apoptotic body formation in a dose-dependent fashion. Thus, the results indicated that water soluble compounds obtained by enzymatic hydrolysis of blueberry possess good antioxidant activity against $H_2O_2$-induced cell damage in vitro.

• ALGAE
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• v.18 no.4
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• pp.341-347
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• 2003

The potential antioxidative activity of water-soluble enzymatic hydrolyzates from a kelp, Ecklonia cava was evaluated by free radical scavenging and lipid peroxidation assays. To prepare water-soluble hydrolyzates from E. cava the seaweed was enzymatically hydrolyzed by five carbohydrases (Viscozyme, Celluclast, AMG, Termamyl and Ultraflo) and five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase). Among all the hydrolyzates, Celluclast hydrolyzate effectively scavenged free radicals released from DPPH (1,1-diphenyl-2- pricrylhydrazyl) and recorded around 73% scavenging activity at the concentration of 4 mg ${\cdot}ml^{-1}$. This hydrolyzate was thermally stable and DPPH radical scavenging activity remained 80% or higher at heating temperatures of 40 and 60$^{\circ}C$ up to 12 h and around 80% at 100$^{\circ}C$ up to 8 h. AMG and Ultraflo hydrolyzate inhibited the lipid peroxidation of fish oil as that of $\alpha$-tocopherol. These results suggested that an enzymatic extraction will be an effective way for the production of a potential antioxidant from seaweeds.

• Food Science of Animal Resources
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• v.32 no.5
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• pp.652-658
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• 2012

This study was carried out to identify the ACE (Angiotensin converting enzyme) inhibitory activity of casein hydrolysates for development of anti-hypertensive hydrolysates. Sodium caseinate was treated with six kinds of commercial proteases such as Flavourzyme, Protamex, Neutrase 1.5, Alcalase, Protease M, and Protease S for 8 h individually, and was then treated with the enzyme combination for 4 h at $45^{\circ}C$. The hydrolysate which had the highest ACE inhibitory effect was then hydrolysed successively with three digestive enzymes: pepsin, trypsin, and ${\alpha}$-chymotrypsin, at $37^{\circ}C$ for 4 h under conditions mimicking those of the gastrointestinal tract. UF (ultra filtration) treatment was applied to one of the secondary hydrolysates to determine ACE inhibitory activity. When sodium caseinate was hydrolysed by commercial proteases, the degree of hydrolysis (DH) showed 2.54 to 4.25% and after secondary hydrolysis, DH showed 4.30 to 5.22%. ACE inhibitory activity and $IC_{50}$ values decreased, and inhibition rates increased during hydrolysis. Protamex treatment showed the lowest $IC_{50}$ value ($516{\mu}g/mL$) and Flavourzyme hydrolysate showed the highest $IC_{50}$value ($866{\mu}g/mL$). As the first hydrolysate was treated with Flavourzyme, the ACE inhibitory activity increased. Neutrase hydrolysate had the highest activity with an $IC_{50}$ value ($282{\mu}g/mL$). When Neutrase plus Flavourzyme treatment was hydrolyzed by digestive enzymes, the $IC_{50}$ value ($597{\mu}g/mL$) was decreased statistically (p<0.05). As Neutrase plus Flavourzyme hydrolysate is treated by UF with MW cut-off 10,000, permeate showed $273{\mu}g/mL$ of $IC_{50}$ value, showed no difference, but retentate which has over MW 10,000 showed statistically different $IC_{50}$ value, $635{\mu}g/mL$ (p<0.05).