• YAKHAK HOEJI
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• v.49 no.3
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• pp.198-204
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• 2005

Human foamy virus (HFV) integrase mediates integration of viral c-DNA into cellular DNA. In this process, HFV integrase recognizes its own viral DNA specifically and catalyzes insertion of viral c-DNA. In order to study catalytic domains and residues, three deletion mutants and two point mutants of HFV integrase were constructed and analyzed with respect to enzymatic activities. The C-terminal deletion mutant showed decreased enzymatic activities while the N-terminal deletion mutant lost the activities completely, indicating that the N-terminal domain is more important than the C-terminal domain in enzymatic reaction. The point mutants, in which an aspartic acid at the 164th position or a glutamic acid at the 200th position of the HFV integrase protein was changed to an alanine, lost the enzymatic activities completely. However, they were well complemented with other defective deletion mutants to recover enzymatic activities partially. Therefore, these results suggest that the aspartic acid and glutamic acid at the respective 164th and 200th positions are catalytic residues for enzymatic reaction.

• BMB Reports
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• v.32 no.6
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• pp.599-604
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• 1999

A highly conserved amino acid, glutamic acid (Glu), present at position 152 in the catalytic domain of the human immunodeficiency virus type 1 (HIV-1) integrase (IN) protein has been known to be critical for enzymatic function since substitution of Glu 152 with other residues results in a complete loss of enzymatic activities. In order to better understand the role of Glu 152 as a conserved residue in enzymatic action, intragenic second site mutations have been introduced around residue 152 of a mutant IN (E152A), and their biochemical properties were analyzed in terms of enzymatic activities. Disintegration activities were found to be significantly restored in several second site mutant INs, while integration activities were only recovered weakly. However, endonucleolytic activities were not discovered in all the mutant INs. These findings indicate that the second site mutations can partially restore that catalytic structure of the active site disturbed by the E152A mutation and lead to the regaining of integration and disintegration activities. In addition, it is also suggested that endonucleolytic activity requires a more accurate structure of the catalytic site than that for the integration and disintegration activities.

• YAKHAK HOEJI
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• v.47 no.1
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• pp.46-51
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• 2003

Baicalein and baicalin are flavonoid compounds isolated from medicinal herb Scutellaria baicalensis Georgi (Labiatae) and have been known to possess antiviral activities. In the present study, we investigated the in vitro effects of baicalein and baicalin on the three distinctive enzymatic activities of the human immunodeficiency virus type-1 (HIV-1) integrase-endonucleolytic, integration, and disintegration activities. Both compounds inhibited the three enzymatic activities in a dose-dependent manner. The 50％ inhibitory concentrations of baicalein and baicalin for endonucleolytic activities of HIV-1 integrase were 4.4$\pm$3.3 and 25.9$\pm$4.0$\mu$M, respectively. In general, baicalein exhibited nearly 6- to 10-fold stronger inhibition than baicalin for the three enzymatic activities. These data demonstrate that baicalein or baicalin can be used as a leading compound to develop anti-AIDS chemotherapeutic agents targeting to the HIV-1 integrase.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.2
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• pp.172-178
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• 2010

This study was conducted to investigate total polyphenol contents and antioxidative effects of the enzymatic hydrolysates digested by several kinds of carbohydrases from the powder of ripened pumpkin (Cucurbita moschata), sweet pumpkin (C. maxima) and green pumpkin (C. moschata). The total polyphenol contents of all enzymatic hydrolysates from green pumpkin powder were higher than those of ripened and sweet pumpkins. DPPH radical scavenging activities of the enzymatic hydrolysates digested by AMG and Termamyl from green pumpkin were also very strong compared to ripened and sweet pumpkins. However, the most enzymatic hydrolysates of ripened and sweet pumpkin powders, except Viscozyme digestion, were higher superoxide anion scavenging activities than green pumpkin powder. Hydrogen peroxide scavenging activities in the enzymatic digests (not Ultroflo) of green pumpkin were potent compared to other pumpkin powders whereas hydroxyl radical scavenging activities were low at less than 14% in hydrolysates of all pumpkin species. Nitric oxide scavenging activities were very effective in Viscozyme digests of sweet and green pumpkin, and other enzymatic hydrolysates also showed higher activity than $\alpha$-tocopherol control (not BHT).

• Journal of the Korean Society of Food Science and Nutrition
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• v.28 no.1
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• pp.67-73
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• 1999

In order to increase the enzymatic activity of malt used as a source of traditional processing foods, the enzymatic activities of various barley were examined and the effects of ozone and light illumination treatment on the enzymatic activities of amylase, amylase, and glucanase in malt during man ufacture were also examined. Barley didn't show amylase activity prior to soaking, but the activity of barley increased quickly after soaking. Glutinous barley showed the highest amylase activity among Duru barley, Ol barley, two rowed barley and naked barley. Naked barley showed the lowest activity. The amylase activity was the highest in Duru barley and decreased in the order of in glutinous barley, naked barley and two rowed barley. It was showed that the enzymatic activity of malt was higher than that of control when malt was soaked for 24hr at the concentration of 0.3ppm of ozone. The enzymatic activity of malt treated with light illumination was higher than that of control. The bud and root of light illuminated malt was much stronger than that of control. The root of light illuminated malt was much shorter than that of control. In addition, light illuminated malt showed a little green color which matches the demand of consumer. These studies demonstrated that both ozone and light illumination treatment increased the enzymatic activity of malt to result in high quality of malt manufacture.

• Korean Journal of Microbiology
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• v.9 no.4
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• pp.155-162
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• 1971

A comparison of dextrinogenic amylase activities in the Asp. niger group was made with their crude and ethanol dialized enzymes before and after heating at high temperature (60-$65^{\circ}C$). The results obtained are as follows ; 1. THe dextrinogenic amylase activity of crude enzymes of Asp. kawachii and Asp. foetidus was strong, but Asp. phoernicis, Asp. carbonarius and Asp.japonicus showed weak activity. The others showed medial grades of activity. 2. The ethanol dialized enzymes of Asp. kawachii, Asp. foetidus and Asp. japonicus was very sesitive to high temperature (60 or $65^{\circ}C$) and their enzymatic activities were diminished greatly. The others did not show diminution of enzymatic activity at 60 or 65.deg.C, but diminished greatly at 70 or $75^{\circ}C$. 3. The ethanol dialized enzymes of the Asp.niger group heated to 65.deg.C was more sensitive at pH 6.0 and 6.5 than at pH 4.5, 5.0 and 5.5. 4. Tested strains in the Asp.niger group were subdivided into 4 subgroups by their dextrinogenic amylase activities before and after heating at 60 or $65^{\circ}C$. The first group showed a medial grade of activity before heating and no diminution of their enzymatic activities after heating. Asp. niger, Asp.pulverulentus, Asp. awamori and Asp. usmii were included in this group. The second group had strong enzymatic activity before heating, but diminished greatly after heating. Asp rawachii and Asp. phoenicis were included in this group. The fourth group showed very weak enzymatic activity before heating, and was inactivated easily by heating. Asp.oryzae of the Asp. flavus group showed a very strong dextrinogenic amylase activity before heating. After the heat treatment, however, its enzymatic activity was diminished greatly.

• Fisheries and Aquatic Sciences
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• v.19 no.7
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• pp.29.1-29.6
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• 2016

In the present study, we investigated to the antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities of the northern shrimp (Pandalus borealis) by-products (PBB) hydrolysates prepared by enzymatic hydrolysis. The antioxidant and ACE inhibitory activities of five enzymatic hydrolysates (alcalase, protamex, flavourzyme, papain, and trypsin) of PBB were evaluated by the 2, 2'-azino-bis [3-ethylbenzothiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities, reducing power and Li's method for ACE inhibitory activity. Of these PBB hydrolysates, the protamex hydrolysate exhibited the most potent ACE inhibitory activity with $IC_{50}$ value of $0.08{\pm}0.00mg/mL$. The PBB protamex hydrolysate was fractionated by two ultrafiltration membranes with 3 and 10 kDa (below 3 kDa, between 3 and 10 kDa, and above 10 kDa). These three fractions were evaluated for the total amino acids composition, antioxidant, and ACE inhibitory activities. Among these fractions, the < 3 kDa and 3-10 kDa fractions showed more potent $ABTS^+$ radical scavenging activity than that of > 10 kDa fraction, while the > 10 kDa fraction exhibited the significant reducing power than others. In addition, 3-10 kDa and > 10 kDa fractions showed the significant ACE inhibitory activity. These results suggested that the high molecular weight enzymatic hydrolysate derived from PBB could be used for control oxidative stress and prevent hypertension.

• Journal of Oral Medicine and Pain
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• v.39 no.4
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• pp.127-132
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• 2014

Purpose: Many substances in saliva or oral health care products interact with each other. The aim of this study was to investigate interactions between hyaluronic acid (HA), lysozyme, peroxidase, and glucose oxidase (GO) in enzymatic activities at low pH levels. Methods: HA (0.5 mg/mL), hen egg-white lysozyme (HEWL, $30{\mu}g/mL$), bovine lactoperoxidase (bLPO, $25{\mu}g/mL$), and GO ($50{\mu}g/mL$) were used. The influences of HA, bLPO, and GO on HEWL activity were determined by measuring the turbidity of a Micrococcus lysodeikticus suspension. The influences of HA and HEWL on bLPO activity were determined by the NbsSCN assay, measuring the rate of oxidation of 5-thio-2-nitrobenzoic acid (Nbs) to 5,5'-dithiobis(2-nitrobenzoic acid) $(Nbs)_2$. The influences of HA and HEWL on GO activity were determined by measuring oxidized o-dianisidine production. All experiments were performed at pH 4, 5, and 6. Results: HA and GO did not affect the enzymatic activity of HEWL at pH 4, 5, and 6. bLPO enhanced the enzymatic activity of HEWL at pH 5 (p<0.05) and pH 6 (p<0.05) significantly. The enzymatic activity of bLPO was not affected by HA and HEWL at pH 4, 5, and 6. HA and HEWL did not affect the enzymatic activity of the GO at pH 4, 5, and 6. Conclusions: Peroxidase enhances lysozyme activity at low pH, otherwise there were no significant interactions in enzymatic activities between HA, lysozyme, peroxidase, and GO at low pH levels.

• Horticultural Science & Technology
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• v.33 no.3
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• pp.309-316
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• 2015

In this experiment, five commercial cultivars and one wild species of loquat were used to investigate frost tolerance and enzymatic activities in leaves and young fruits under cold stress at $-3^{\circ}C$. The frost injury, malondialdehyde (MDA) content, and oxygen-scavenging enzyme activities of superoxide dismutase (SOD), peroxidase (POD), catalase (CAT) and ascorbate peroxidase (APX) were studied. This results showed that the wild species 'Wild Oak-leaf' loquat was the most frost tolerant among accessions tested, followed by the cultivar 'Golden Block'. Other cultivars, 'Wu Gong Bai', 'Taicheng 4', 'Xiangzhong 11' and 'Zaozhong 6', were relatively weak in frost tolerance. The enzymatic activities of SOD, POD and CAT increased initially and then decreased as the exposure time increased. However, the enzymatic peak occurred later in the frost-tolerant accession than in the frost-sensitive accession. The correlation coefficients of MDA contents between leaves and immature fruits were from 0.93 to 0.99 in the five commercial loquat cultivars. For the 'Wild Oak-leaf' loquat, the correlation coefficients of MDA and POD were 0.98 and 0.95, respectively, but the coefficients for SOD, CAT and APX were relatively low. In general, there were good correlations between loquat leaves and immature fruits in MDA content and enzyme activities. These results indicate that analysis of these physiological and biochemical activities in loquat leaves could potentially be used to predict the cold tolerance in loquat at immature fruit stage and to accelerate breeding programs for cold tolerance in loquat.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.425-431
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• 1996

The enzymatic characteristics of Alcaligenes latus were investigated by measuring the variations of various enzyme activities related to biosynthesis and degradation of poly-${\beta}$-hydroxybutyrate (PHB) during cultivation. All PHB biosynthetic enzymes, ${\beta}$-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase, were activated gradually at the PHB accumulation stage, and the PHB synthase showed the highest value among three enzymes. This indicates that the rate of PHB biosynthesis is mainly controlled by either ${\beta}$-ketothiolase or acetoacetyl-CoA reductase rather than PHB synthase. The enzymatic activities related to the degradation of PHB were also measured, and the degradation of PHB was controlled by the activity of PHB depolymerase. The effect of supplements of metabolic regulators, citrate and tyrosine, was also investigated, and the activity of glucose-6-phosphate dehydrogenase was increased by metabolic regulators, especially by tyrosine. The activities of ${\beta}$-ketothiolase and acetoacetyl-CoA reductase were also activated by citrate and tyrosine, while the activity of PHB depolymerase was depressed. The increased rate and yield of PHB biosynthesis by metabolic regulators may be due to the increment of acetyl-CoA concentration either by the repression of the TCA cycle by citrate through product inhibition or by the activation of sucrose metabolism by the supplemented tyrosine.