• Journal of Apiculture
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• v.32 no.3
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• pp.269-273
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• 2017

We investigated whether purified bee venom increases the enzymatic activity of the alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). ADH and ALDH assay were tested by in vitro kits. The purified bee venom was assayed by ultra performance liquid chromatography, The contents of melittin, apamin and phospholipase A2, as main component of purified bee venom, were 63.9%, 2.3%, and 10.9%, respectively. The ADH and ALDH acitivity of purified bee venom(at 1mg/ml) were $88.6{\pm}7.34%$ and $94.6{\pm}0.57%$, respectively compared with positive control at 2mg/ml. These results showed that purified bee venom induces the activity of ADH and ALDH which reduce the aldehyde concentration in the blood, suggesting the possibility of purified bee venom as resource of medicine or functional beverage for hangover relieving.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.46 no.4
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• pp.349-360
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• 2020

Bio-conversion manufacturing technology has been developed to produce ginsenoside Rd which is increasingly in demand as a cosmetic material due to various possibilities related to improving skin function. In order to convert ginsenoside Rb1 which is contained in red ginseng saponin (RGS) into Rd, several commercial enzymes were tested. Viscoflow MG was found to be the most efficient. In order to optimize the conversion of RGS to ginsenoside Rd by enzymatic transition was carried out using response surface methodology (RSM) based on Box-Behnken design (BBD). The main independent variables were RGS concentration, enzyme concentration, and reaction time. Conversion of ginsenoside Rd was performed under 17 conditions selected according to BBD model and optimization conditions were analyzed. The concentration of the converted ginsenoside Rd ranged from 0.3113 g/L to 0.5277 g/L, and the highest production volume was obtained under condition of reacting 2% RGS and 1.25% enzyme for 13.5 hours. Consequently, RGS concentration, enzyme concentration which is 0.05 less than p-value and among the interactions between the independent variables, the interaction between enzyme concentration and reaction time was confirmed to be the most influential.

• Journal of the Korean Applied Science and Technology
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• v.38 no.1
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• pp.99-106
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• 2021

To circumvent the skin problem from phenylethanol (PhE), we have studied on the enzymatic synthesis of phenylethanol galactoside (PhE-gal) as an alternative to PhE. Base on the previous study, we optimized the reaction conditions for PhE-gal synthesis from PhE using E. coli β-galactosidase (β-gal). The optimal amount of β-gal, PhE concentration, pH, and temperature for PhE-gal synthesis were 0.45 U/ml, 1%, 8.0, 40℃, respectively. Under these conditions, about 81.9 mM PhE was converted into about 47.4 mM PhE-gal, in which the conversion yield was about 57.9%. Meanwhile, when the reaction mixture containing PhE and PhE-gal was mixed and fractionated with water-immiscible solvent (EA or MC), it was observed that PhE-gal was distributed in water phase, and PhE was distributed in solvent phase. Additionally, PhE-gal was clearly distributed into water phase when MC was used, but PE-gal was not when EA was used. In the future, we are planning to carried out the continuing study on developing an alternative cosmetic preservative using PhE-gal.

• Korean Chemical Engineering Research
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• v.60 no.1
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• pp.1-6
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• 2022

As the demand for wearable devices increases, many studies have been studied on the development of flexible electrode materials recently. In particular, the development of high-performance flexible electrode materials is very important for wearable sensors for healthcare because it is necessary to continuously monitor and accurately detect body information such as body temperature, heart rate, blood glucose, and oxygen concentration in real time. In this study, we fabricated the nonenzymatic glucose sensor based on polyaniline/carbon nanotube fiber (PANI/CNT fiber) electrode. PANI layer was synthesized on the flexible CNT fiber electrode through electrochemical polymerization process in order to improve the performance of a flexible CNT fiber based electrode material. Surface morphology of the PANI/CNT fiber electrode was observed by scanning electron microscopy. And its electrochemical characteristics were investigated by chronoamperometry, cyclic voltammetry, electrochemical impedance spectroscopy. Compared to bare CNT fiber electrode, this PANI/CNT fiber electrode exhibited small electron transfer resistance, low peak separation potential and large surface area, resulting in enhanced sensing properties for glucose such as wide linear range (0.024~0.39 and 1.56~50 mM), high sensitivity (52.91 and 2.24 ㎂/mM·cm²), low detection limit (2 μM) and good selectivity. Therefore, it is expected that it will be possible to develop high performance CNT fiber based flexible electrode materials using various nanomaterials.

• The Korean Journal of Physiology and Pharmacology
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• v.26 no.4
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• pp.263-275
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• 2022

There is a paucity of detailed data related to the effect of senescence on the mitochondrial antioxidant capacity and redox state of senescent human cells. Activities of TCA cycle enzymes, respiratory chain complexes, hydrogen peroxide (H₂O₂), superoxide anions (SA), lipid peroxides (LPO), protein carbonyl content (PCC), thioredoxin reductase 2 (TrxR2), superoxide dismutase 2 (SOD2), glutathione peroxidase 1 (GPx1), glutathione reductase (GR), reduced glutathione (GSH), and oxidized glutathione (GSSG), along with levels of nicotinamide cofactors and ATP content were measured in young and senescent human foreskin fibroblasts. Primary and senescent cultures were biochemically identified by monitoring the augmented cellular activities of key glycolytic enzymes including phosphofructokinase, lactate dehydrogenase, and glycogen phosphorylase, and accumulation of H₂O₂, SA, LPO, PCC, and GSSG. Citrate synthase, aconitase, α-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, isocitrate dehydrogenase, and complex I-III, II-III, and IV activities were significantly diminished in P25 and P35 cells compared to P5 cells. This was accompanied by significant accumulation of mitochondrial H₂O₂, SA, LPO, and PCC, along with increased transcriptional and enzymatic activities of TrxR2, SOD2, GPx1, and GR. Notably, the GSH/GSSG ratio was significantly reduced whereas NAD⁺/NADH and NADP⁺/NADPH ratios were significantly elevated. Metabolic exhaustion was also evident in senescent cells underscored by the severely diminished ATP/ADP ratio. Profound oxidative stress may contribute, at least in part, to senescence pointing at a potential protective role of antioxidants in aging-associated disease.

• Journal of Life Science
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• v.32 no.4
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• pp.285-289
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• 2022

In this study, the growth characteristics of an agar-degrading bacterium isolated from seawater samples collected from Yeongheungdo, Incheon, and the characteristics of its agarase were analyzed. The 16S rRNA gene sequence of the isolated strain was 95% similar to that of the genus Agarivorans, and thus the isolated strain was named Agarivorans sp. HY-1. When Agarivorans sp. HY-1 was cultured in a marine broth 2216 medium at 27℃ and 250 rpm, it showed maximum growth on day 1 and showed maximum enzymatic activity on day 2. A crude enzyme solution was prepared from secreted agarase in the culture medium. The extracellular agarase of the Agarivorans sp. HY-1 strain showed maximal activity at 40℃ and pH 7.0 (20 mM Tris-HCl) with 591.91 U/l. The agarase exhibited relative activities of 64, 91, 100, 97, 89, and 60% at 20, 30, 40, 50, 60, and 70℃, respectively. At pH 5, 6, 7, and 8, the relative activities were 79, 95, 100, and 55%, respectively. Furthermore, the agarase exhibited >86% residual activity at 20, 30, and 40℃ for 2 hr and >44% residual activity at 50℃ after 2 hr. A TLC analysis confirmed that Agarivorans sp. HY-1 produced α-agarase. As the degradation products of α-agarase have anticancer and antioxidant effects, Agarivorans sp. HY-1 and its agarase may well prove useful.

• Journal of Nutrition and Health
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• v.55 no.3
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• pp.348-358
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• 2022

Purpose: Hyperglycemia accelerates the formation of advanced glycation end products (AGEs), a group of compounds formed via non-enzymatic glycation/glycoxidation. Type 2 diabetes mellitus (T2DM) is related to oxidative stress, resulting in some overgeneration of AGEs. The accumulation of AGEs in T2DM patients leads to increased inflammation, DNA damage, tissue damage, progression of diabetic microvascular disease, and nephropathy. Heme oxygenase-1 (HO-1) is an intracellular enzyme that catalyzes the oxidation of heme. Expression of HO-1 in the endothelium and in muscle monocytes/macrophages was upregulated upon exposure to reactive oxygen species or oxidized low-density lipoprotein. Cells activated by oxidative stress are reported to release HO-1 in the serum. In the current study, we discuss the oxidative status according to the level of AGEs and the association of HO-1 with AGEs or urinary DNA damage marker in type 2 diabetic Korean patients. Methods: This study enrolled 36 diabetic patients. Subjects were classified into two groups by serum AGEs level (Low AGEs group: < 0.85 ng/mL serum AGEs; High AGEs group: ≥ 0.85 ng/mL serum AGEs). Body composition was measured using bioelectrical impedance analysis. Blood and urinary parameters were measured using commercial kits. Results: No significant differences were observed in the general characteristics and body composition between the two groups. Serum HO-1 concentration was significantly higher in the High AGEs group than in the Low AGEs group. After adjustment of age and gender, a correlation was performed to assess the association between serum HO-1 and serum AGEs or urinary 8-hydroxy-2'-deoxyguanosine (8-OHdG). Our results indicate that serum HO-1 is positively correlated with serum AGEs and urinary 8-OHdG. Conclusion: Taken together, our results indicate that in diabetes patients, a high level of HO-1 is associated with a high concentration of AGEs and 8-OHdG, probably reflecting a protective response against oxidative stress.

• Journal of Life Science
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• v.32 no.1
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• pp.51-55
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• 2022

Matrix metalloproteinase (MMP) enzymes are responsible for the degradation and formation of the extracellular matrix (ECM), and overproduction of MMPs is observed in several diseases, such as cancer and asthma, that progress with metastatic characteristics. Natural products, especially phytochemicals, have been an important source of MMP inhibitors with reduced side effects. Although the majority of phytochemicals inhibit the enzymatic activity of MMPs, some suppress MMP production. In this context, the current study evaluated the potential of Corydalis heterocarpa, a halophyte with reported bioactivities, to inhibit MMP expression in PMA-stimulated HT-1080 cells. A crude C. heterocarpa extract was shown to decrease the mRNA and protein expression of MMP-2 and MMP-9 while increasing the endogenous MMP inhibitors TIMP-1 and TIMP-2 which regulate MMP expression in healthy tissues. In addition, our results show that the inhibitory effects of C. heterocarpa might occur through suppression of the phosphorylation of MAPK signaling, the upstream activator of MMP overexpression. In conclusion, C. heterocarpa is a potential source of antimetastatic compounds that might serve as lead molecules to develop novel MMP inhibitors.

• Herbal Formula Science
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• v.30 no.2
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• pp.37-44
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• 2022

Objectives : The purpose of this study was to examine the effects of Alisma canaliculatum Extract (ACE) on pacemaker potentials of small and large intestinal interstitial Cells of Cajal (ICC) in mice. Methods : We used enzymatic digestions to dissociate the ICC in the small and large intestine in mice. The whole-cell patch-clamp method was used to record pacemaker potentials in ICC. Results : 1. The ICC generated the pacemaker potentials in small intestine in mice. ACE (0.1-1mg/ml) induced membrane depolarization and decreased frequency with concentration-dependent manners. 2. Pretreatment with a Ca²⁺ free solution, Na⁺ 5 mM solution or 2-APB, a nonselective cation channel blocker, stopped the small intestinal ICC pacemaker potentials. In the case of Ca²⁺-free solution, Na⁺ 5 mM solution or 2-APB, ACE had no effects on the membrane depolarizations in small intestinal ICC. 3. The ICC generated the pacemaker potentials in large intestine in mice. Membrane depolarization appears regularly in the small intestine, but irregularly in the large intestine. ACE induced membrane depolarization (0.1-1mg/ml) and increased frequency (0.1-0.5mg/ml). 4. Pretreatment with a Ca²⁺ free solution, Na⁺ 5 mM solution or 2-APB, stopped the large intestinal ICC pacemaker potentials. In the case of Ca²⁺-free solution, Na⁺ 5 mM solution or 2-APB, ACE depolarized the membrane depolarizations in large intestinal ICC. 5. In mice, intestinal transit rate (ITR) values were dose-dependently decreased by the intragastric administration of ACE. Conclusions : These results suggest that ACE can regulate the pacemaker activity of ICC and the reaction by ACE is different from the small and large intestinal ICC, and the control of the intestinal motion by ACE may be caused by many complex processes.

• Journal of Microbiology and Biotechnology
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• v.32 no.8
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• pp.1064-1071
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• 2022

Arabinogalactans have diverse biological properties and can be used as pharmaceutical agents. Most arabinogalactans are composed of β-(1→3)-galactan, so it is particularly important to identify β-1,3-galactanases that can selectively degrade them. In this study, a novel exo-β-1,3-galactanase, named PoGal3, was screened from Penicillium oxalicum sp. 68, and hetero-expressed in P. pastoris GS115 as a soluble protein. PoGal3 belongs to glycoside hydrolase family 43 (GH43) and has a 1,356-bp gene length that encodes 451 amino acids residues. To study the enzymatic properties and substrate selectivity of PoGal3, β-1,3-galactan (AG-P-I) from larch wood arabinogalactan (LWAG) was prepared and characterized by HPLC and NMR. Using AG-P-I as substrate, purified PoGal3 exhibited an optimal pH of 5.0 and temperature of 40℃. We also discovered that Zn²⁺ had the strongest promoting effect on enzyme activity, increasing it by 28.6%. Substrate specificity suggests that PoGal3 functions as an exo-β-1,3-galactanase, with its greatest catalytic activity observed on AG-P-I. Hydrolytic products of AG-P-I are mainly composed of galactose and β-1,6-galactobiose. In addition, PoGal3 can catalyze hydrolysis of LWAG to produce galacto-oligomers. PoGal3 is the first enzyme identified as an exo-β-1,3-galactanase that can be used in building glycan blocks of crucial glycoconjugates to assess their biological functions.