• Journal of Life Science
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• v.22 no.2
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• pp.220-225
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• 2012

The peptides of enzymatic hydrolysates from oyster were determined by inhibitory activity against angiotensin-converting enzyme. The ACE inhibitory activity of enzymatic oyster hydrolysates increases with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex showed the best ACE inhibitory activity after 10 h. Hydrolysates were filtered through a HiSep ultrafiltration membrane (M.W. cut-off 30 kDa, 10 kDa) to obtain the peptide fractions with ACE inhibition activity. These fractions were applied to an HPLC column (watchers 120 ODS-AP $250{\times}4.6$ ($5{\mu}m$)). Six active fractions were collected and the range of ACE inhibition was from 29.56 to 85.85%. Peptide was purified from fraction B, showing the highest ACE inhibitory activity, and its sequence was Leu-Gln-Pro. These results suggest that PEH may be beneficial for developing antihypertensive food and drug.

• Journal of Microbiology and Biotechnology
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• v.10 no.3
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• pp.307-311
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• 2000

Abstract Extracellular chitinase was purified from the culture liquid of the marine bacterium, Bacillus sp. LJ-25 , and its enzymatic properties were examined. The purified chitinase exhibited a single band on SDS-PAGE and the molecular weight was estimated to be approximately 50 kDa. The optimum pH and temperature for the enzymatic activity were 7.0 and $35^{\circ}C$, respectively. The activity of the chitinase was strongly inhibited by $Zn^{2+}$ and slightly inhibited by $Ba^{2+},{\;}Co^{2+},{\;}Mn^{2+},{\;}and{\;}Cu^{2+}$. The purified chitinase did not hydrolyze $p-nitrophenolN-acetyl-{\bata}-D-glucosaminide{\;}(GlcNAc)_2$ and Micrococcus lysodeikticus cells, which are known to be the substrates for exo-type chitinase. Among the hydrolyzates of colloidal chitin, $(GlcNAc)_2$ was in the highest concentration with small amounts of GlcNAc and $(GlcNAc)_3$..

• Journal of Microbiology and Biotechnology
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• v.13 no.5
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• pp.773-777
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• 2003

The color of Congo red hinders the spectrometric measurements of a concentration of hydrogen peroxide and enzyme activity (Horseradish peroxidase; HRP) during enzymatic decoloring of Congo red. In this study, a method was developed to measure peroxidase activity and hydrogen peroxide concentration in the presence of Congo red. The oxidation product of HRP/hydrogen peroxide and ABTS(2,2'-azino-bis-(3-ethylbenzotriazoline-6-sulfonic acid)) formed a dark green color. The spectrum of this product showed absorption bands at 420 nm and 734 nm. When compared with the Congo red spectrum, the absorption at 734 nm of this product did not overlap with Congo red, thus making the hydrogen peroxide measurement possible even in the presence of Congo red. Kinetic study of decoloring of Congo red performed by this method showed that the decoloring reaction followed the Michaelis-Menten kinetics. Pulse feeding of hydrogen peroxide, upon depletion, significantly increased the decoloring of Congo red. This result shows that this newly developed technique can monitor, predict, and improve the enzymatic decoloring process.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.1
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• pp.6-13
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• 2001

The study was conducted to investigate the effect of the browning inhibitors such as PVPP(polyvinylpoly-pyrrolidone), A.A.(ascorbic acid) on nonezymatic browning factors [free sugar, total amino acid, organic acid, A.A., HMF (hydroxymethylfurfural)] and enzymatic browning factors [PRO (polyphenoloxidase) activity, polyphenol compounds] in concentrated apple juice during 90 days storage. Considering color value (L value, $\Delta$E), absorbance at 420 nm, concentrated apple juice during 90 days storage. Considering color the effect of browning inhibition. According to the storage period, the changes of nonenzymatic factors in concentrated apple juice added with browning inhibitors were similar to those in control (concentrated apple juice without browning inhibitors), which were the decreased of sucrose(0.24~0.35% at 90 days), the slight increase of glucose and fructose, the decrease of total amino acid (530.4~573.1 mg/10g at 90 days), same value of A.A. at 90 days (38.5~78.6 mg/100g), and the increase of HMF (27.8~30.6 mg/100g at 90 days). On the contrary, enzymatic browning factors were significantly inhibited in concentrated apple juice added with PVPP, judging from the slow increase of PRO activity and the significant decrease of initial value in polyphenol compounds (especially chlorogenic acid). These results suggest that PVPP plays an important role as enzymatic browning inhibitor, that is, a scavenger of polyphenol compounds by adsorption in concentrated apple juice.

• Preventive Nutrition and Food Science
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• v.20 no.1
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• pp.67-72
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• 2015

Squid is one of the most important commercial fishes in the world and is mainly utilized or consumed as sliced raw fish or as processed products. The biofunctional activities of enzymatic squid meat hydrolysate were determined to develop value-added products. Enzymatic squid hydrolysate manufactured by Alcalase effectively quenched 1,1-diphenyl-2-picrylhydrazyl radical, hydroxyl radical, and hydrogen peroxide radical with $IC_{50}$ values of 311, 3,410, and $111.5{\mu}g/mL$, respectively. Angiotensin I-converting enzyme inhibitory activity of squid hydrolysate was strong with an $IC_{50}$ value of $145.1{\mu}g/mL$, while tyrosinase inhibitory activity with an $IC_{50}$ value of 4.72 mg/mL was moderately low. Overall, squid meat hydrolysate can be used in food or cosmetic industries as a bioactive ingredient and possibly be used in the manufacture of seasoning, bread, noodle, or cosmetics.

• Journal of Marine Bioscience and Biotechnology
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• v.10 no.1
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• pp.1-8
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• 2018

The objective of this study was to purify and characterize the ${\beta}-secretase$ inhibitor from enzymatic hydrolysates of blackfin flounder muscle, for development of a novel anti-dementia agent that may be used in the drug or functional food industries. ${\beta}-secretase$ inhibitory peptide was purified from various enzymatic hydrolysates of blackfin flounder muscle. Among six enzymatic hydrolysates, the Alcalase hydrolysate revealed highest ${\beta}-secretase$ inhibitory activity. Consecutive purification of the blackfin flounder muscle hydrolysate using Sephadex G-25 column chromatography and octadecylsilane C18 reversed phase HPLC techniques were used to isolate a potent ${\beta}-secretase$ inhibitory peptide composed of 5 amino acids, Leu-Thr-Gln-Asp-Trp (MW: 526.7 Da). The $IC_{50}$ value of purified ${\beta}-secretase$ inhibitory peptide was $126.93{\mu}M$. Results of this study suggest that peptides derived from blackfin flounder muscle may be beneficial as anti-dementia compounds in functional foods or as pharmaceuticals.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.6 no.3_4
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• pp.97-100
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• 1973

In the previous work(Kim et al, 1973), the quality of sun-dried Alaska pollack, Theragra chalch-ogramma, was discussed in the aspect of non-enzymatic discoloration as a function of relative humidity during storage at room temperature($20^{\circ}C$). In this paper, sun-dried squid, Ommastrephes steam pacificus was investigated at the same aspect mentioned above. Fresh squid from the whole sale market was dressed, filleted, dried for 48 hours in the open air and finally stored in the humidistat chamber. Lipid oxidation ana development of non-enzymatic browning were tested by the same methods described in the previous paper. The TBA value showed a maximum peak on 30 day storage, hereafter tended to decrease gradually. The rate of browning, however, in water soluble fraction as well as in chloroform-methanol fraction was lower at 0.34 to 0.45 water activity than at any other case, and propagation of lipid oxidation was also diminished at the above level of water activity. From the results, it is recognized that storage at Aw=0.34 to 0.45 provides higher quality stability for sun-dried squid.

• Preventive Nutrition and Food Science
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• v.20 no.3
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• pp.183-189
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• 2015

In the present study, an optimum protease was selected to hydrolyze the egg white liquid protein for the antioxidant peptides. Alcalase treatment yielded the highest amount of ${\alpha}$-amino groups (15.27 mg/mL), while the control (no enzymatic hydrolysis) showed the lowest amount of ${\alpha}$-amino groups (1.53 mg/mL). Alcalase also gave the highest degree of hydrolysis (DH) value (43.2%) and was more efficient for egg white liquid hydrolysis than the other enzymes. The Alcalase hydrolysate had the highest radical-scavenging activity (82.5%) at a concentration of 5.0 mg/mL. The conditions for enzymatic hydrolysis of egg white liquid with Alcalase were selected as substrate : water ratio of 2:1. Five percent Alacalse treatment did not show significant (P>0.05) increases of DH and ${\alpha}$-amino nitrogen content after 24 hhydrolysis. Thirty two hour-hydrolysis with 5% Alcalase is sufficient to make antioxidative egg white liquid hydrolysate from egg white liquid. DPPH and ABTS radical-scavenging activities were significantly (P<0.05) higher after enzymatic digestion. These results suggest that active peptides released from egg-white protein are effective radical-scavengers. Thus, this approach may be useful for the preparation of potent antioxidant products.

• Journal of Applied Biological Chemistry
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• v.66
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• pp.462-466
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• 2023

After treating spent coffee grounds with alkali, extracts were prepared by using Viscozyme and Alcalase, respectively. Treatment of spent coffee grounds with alkali and enzymes increased the content of phenolic compounds in the extracts, thus possessing the good scavenging activities on free and cation radicals. In particular, the extract obtained by continuous treatment with alkali and Alcalase on spent coffee grounds had the best content of phenolic compounds and antioxidant activity, and inhibited the growth of Streptococcus mutans in proportion to the concentration. In conclusion, the Alcalase-enzymatic hydrolysate of alkali-treated spent coffee grounds showed excellent antioxidant and anticariogenic effects.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.597-600
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• 2000

In this study the enzymatic synthesis of ester-linked conjugates of amino acid and monosaccharide in pyridine was tested by the catalysis of Optimase M-440, an alkaline serine pretense. Optimase M-440 showed the higher activity in the reaction of monosaccharides which have one or more primary -OH groups. And also Optimase M-440 showed high regioselectivity; The transesterification of primary -OH group selectively occurred.