• Asian-Australasian Journal of Animal Sciences
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• v.16 no.1
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• pp.70-76
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• 2003

Three experiments were conducted to determine the effects of a sorghum-specific enzyme system, derived from an Aspergillus niger and Bacillus subtilis fermentation extract (carbohydrase activity of 1,650 $\alpha$-amylase units and cellulase activity of 30 fibrinolytic units/mL), on growth performance of finishing pigs. In Exp. 1,192 pigs (average initial BW of 46.1 kg) were fed sorghum-based diets without or with 360 mL of enzyme system per ton of sorghum in a 78 d growth assay. For d 0 to 39, gain/feed was improved (p<0.03) with enzyme supplementation, but ADG was not affected (p>0.15). For d 39 to 78 and overall (d 0 to 78), ADG, gain/feed, and digestibilities of DM and N were not affected (p>0.13) by enzyme supplementation. Backfat thickness, fat-free lean index, and scores for stomach keratinization and ulcers also were not affected (p>0.15) by the dietary treatments. In Exp. 2,168 pigs (average initial BW of 58.4 kg) were fed diets without or with 150, 300, or 450 mL/ton of the same enzyme system used in Exp. 1. Adding as much as 450 mL enzyme system / ton of sorghum did not affect (p>0.15) ADG or gain/feed for d 0 to 29 of the growth assay. However, during d 29 to 63, ADG increased by 11% (linear effect, p<0.02) and gain/feed increased by 10% (linear effect, p<0.06) as enzyme concentration was increased from none to 450 mL/ton of sorghum. For the overall period (d 0 to 63), ADG tended to increase (p<0.08) with enzyme supplementation, but gain/feed and digestibilities of DM and N were not affected (p>0.14). Carcass characteristics (dressing percentage, backfat thickness, and fat free lean index) also were not affected (p>0.20) by addition of the enzyme system. In Exp. 3,176 pigs (average initial BW of 46.7 kg) were fed diets without or with 450, 900, or 1,350 mL/ton of the same enzyme system used in Exp. 1 and 2 in a 71 d growth assay. Adding up to 1,350 mL/ton of enzyme had no effects (p>0.15) on ADG, gain/feed, digestibilities of DM and N, and carcass characteristics (dressing percentage, backfat thickness, and fat-free lean index). In conclusion, finishing pigs fed diets with a sorghum-specific enzyme system showed some positive trends for improved growth performance, but those effects were not large and (or) consistent.

• Proceedings of the KSAR Conference
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• 2002.06a
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• pp.69-69
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• 2002

To investigate the effects of two antioxidants, aesculeitin and taurine, expression of apoptosis related genes and antioxidant enzyme gene in preimplantation Hanwoo embryos was determined by modified semi-quantitative single cell RT-PCR. Hanwoo embryos derived from in vitro maturation /in vitro fertilization were cultured in 5% CO₂ and 5% O₂ in CR₁aa medium at 37℃. Aesculeitin and taurine were added to medium at concentration of l㎍/㎖ and 2.5mM, respectively. (omitted)

• Food Science and Preservation
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• v.23 no.6
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• pp.797-803
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• 2016

In this study, we investigated the effect of fermentation conditions on the amylolytic and proteolytic activities of Aspergillus luchuensis strain 74-5 and Aspergillus oryzae strain 75-2, which are used in the preparation of the starter culture, for Takju (Korean traditional rice wine). The starter culture was optimized using different conditions, such as inoculum size, inoculation temperature, and incubation time. The enzyme activities under each condition were measured. In the A. luchuensis strain 74-5 starter culture, the ${\alpha}-amylase$ and glucoamylase activities increased, however the activity of acidic protease decreased as the diluent to starter culture ratio increased. In the A. oryzae 75-2 starter culture, all enzyme activities were maintained at a higher level even at 5% inoculation ratio. Higher enzyme activities were observed in the middle range of inoculation temperature (35, $40^{\circ}C$), than in the lower range (20, $30^{\circ}C$). Enzyme activity in the starter culture varied with incubation time, however it was the highest at 144 and 120 hr, respectively, for A. luchuensis strain 74-5 and A. oryzae strain 75-2. The spore count of the starter culture was approximately $2{\times}10^7$ during fermentation, out of which contamination by aerobic bacteria was about $3{\times}10^3$. The results suggested that the starter culture of each strain could be used as an inoculum for fermentation. However, we needs to conduct further research for the selection of suitable diluting agents as well as drying methods to reduce the contamination by aerobic bacteria, while retaining the enzyme activity.

• 한국약용작물학회:학술대회논문집
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• 2008.11a
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• pp.123-124
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• 2008

• Proceedings of the Plant Resources Society of Korea Conference
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• 2010.10a
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• pp.15-15
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• 2010

Ginseng contained many different kinds of saponin which was the most valuable for people, but its yield cannot satisfy the demand using traditional extract methods. Enzyme transformation is a conformable and highly performed method which was fit for today. A ${\beta}$-glucosidase producing bacterium ($DCY51^T$) was isolated from Korean fermented-vegetable food kimchi. The 16S rRNA gene sequence analysis revealed that the strain $DCY51^T$ belongs to the genus Lactobacillus. The highest sequence similarity was found with Lactobacillus paracollinoides LMG $22473^T$ and Lactobacillus collinoides LMG $9194^T$ with levels of 16S rDNA similarity of 97.4% and 97.3%, respectively. Based on the above results the strain $DCY51^T$ placed in the genus Lactobacillus and proposed a new species, Lactobacillus kimchicus sp. nov. $DCY51^T$ (= KCTC $12976^T$ = JCM $15530^T$). It was culture solution reacted with Red Ginseng extract and $Rb_1$, respectively. The medium of bacteria was the liquid of MRS, the temperatures of growing and reacting between bacteria liquid and saponin were samely $37^{\circ}C$, there spective reacting time were 12 hours and 48 hours. Thus we got different saponins, and TLC and HPLC analysis showed that: enzyme respectively reacted with $Rb_1$ and Red Ginseng extract got the transformed saponin, respectively. The polarity position in TLC was a little higher than Rd; and the polarity position was the same as that of Compound K's, the saponin obtained from HPLC and other experimental results was not Compound K. The constitution of its saponin was hoped to be further confirmed.

• Journal of Microbiology and Biotechnology
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• v.22 no.11
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• pp.1557-1567
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• 2012

Glutathione reductase (GR, E.C. 1.6.4.2) is an important enzyme that reduces glutathione disulfide (GSSG) to a sulfydryl form (GSH) in the presence of an NADPH-dependent system. This is a critical antioxidant mechanism. Owing to the significance of GR, this enzyme has been examined in a number of animals, plants, and microbes. We performed a study to evaluate the molecular properties of GR (OsGR) from rice (Oryza sativa). To determine whether heterologous expression of OsGR can reduce the deleterious effects of unfavorable abiotic conditions, we constructed a transgenic Saccharomyces cerevisiae strain expressing the GR gene cloned into the yeast expression vector p426GPD. OsGR expression was confirmed by a semiquantitative reverse transcriptase polymerase chain reaction (semiquantitative RT-PCR) assay, Western-blotting, and a test for enzyme activity. OsGR expression increased the ability of the yeast cells to adapt and recover from $H_2O_2$-induced oxidative stress and various stimuli including heat shock and exposure to menadione, heavy metals (iron, zinc, copper, and cadmium), sodium dodecyl sulfate (SDS), ethanol, and sulfuric acid. However, augmented OsGR expression did not affect the yeast fermentation capacity owing to reduction of OsGR by multiple factors produced during the fermentation process. These results suggest that ectopic OsGR expression conferred acquired tolerance by improving cellular homeostasis and resistance against different stresses in the genetically modified yeast strain, but did not affect fermentation ability.

• Journal of Life Science
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• v.28 no.2
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• pp.187-194
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• 2018

Eritadenine (EA), derived from Lentinus edodes (LE), reduced low-density lipoprotein (LDL), triglyceride (TG), and phospholipids in bloods, and fatty acid depositions in animals and humans. Previously, we reported that EA inhibited angiotensin-converting enzyme (ACE) activity in vitro. Now, we report that EA reduced blood pressures in spontaneous hypertension rats (SHR). EA-containing LE mycelial culture enzyme extract (EA-LEMSCEE) was prepared from LE mycelial solid cultures and the hot-water extract of LE fruit bodies. Both EA and EA-LEMSCEE inhibited ACE activity in immortalized human umbilical endothelial cells (EA.hy926). EA-LEMSCEE treatments (7.5 mg/kg, 22.5 mg/kg) significantly reduced systolic and diastolic blood pressure in SHR. At five weeks of treatment, EA-LEMSCEE treatment significantly reduced systolic and diastolic blood pressure, similar to the positive control (captopril, CP; 4 mg/kg) treatment. In addition, the LEMSCEE without EA decreased systolic and diastolic blood pressures compared to the control, but not significant. EA-LEMSCEE decreased renin and ACE activities, and angiotensin II (Ang II) contents in SHR compared to the control. After five weeks of treatment, the effect of EA-LEMCEE was similar to that of CP. These results indicate that EA and EA-LEMSCEE reduce blood pressure by inhibiting the renin and ACE activity of SHR. Furthermore, these results imply that EA or EA-LEMSCEE could be used as an antihypertension agent in humans.

• KSBB Journal
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• v.27 no.6
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• pp.341-346
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• 2012

Indican (indoxyl-${\beta}$-D-glucoside) is a colorless natural compound and can be used as a precursor for the production of indigo. This production step only require an enzyme, ${\beta}$-glucosidase, that readily screened from microbial resource by using selective media supplemented with indican as a sole carbon source. Agrobacterium tumefaciens was well grown in this media and thus presumed to produce a related enzyme. The corresponding gene, encoding a protein with a calculated molecular mass of 51 kDa, was cloned and overexpressed as MBP fusion proteins. The purified enzyme was determined to be a dimer and showed the maximum activity for indican at pH 7.0 and $40^{\circ}C$. The kinetic parameters for indican, Km and Vmax, were determined to be 1.4 mM and 373.8 ${\mu}M/min/mg$, respectively. The conversion yield of indican into indigo using this enzyme was about 1.7-1.8 folds higher than that of previously isolated enzyme from Sinorhizobium meliloti. Additionally, this enzyme was able to hydrolyze various ${\beta}$-1,4 glycoside substrates.

• Journal of the Korean Wood Science and Technology
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• v.39 no.2
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• pp.187-195
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• 2011

In this study, dilute acid pretreatment of $Liriodendron$ $tulipifera$ was performed for enzymatic hydrolysis. As the pretreatment temperature was increased, enzymatic hydrolysis and enzyme adsorption yield also increased. The highest enzymatic hydrolysis yield was 57% (g/g) and enzyme adsorption was 44% (g/g). Enzymatic hydrolysis yield was determined with weight loss of pretreated biomass by enzyme, and enzyme adsorption was a percentage of enzyme weight attaching on pretreated biomass compared with input enzyme weight. When $L.$ $tulipifera$ was pretreated with 1% sulfuric acid at $160^{\circ}C$ for 5 min., hemicellulose was significantly removed in pretreatment, but the lignin contents were constant. Other changes in surface morphology were detected on biomass pretreated at $160^{\circ}C$ by a field emission scanning electron microscope (FESEM). A large number of spherical shapes known as lignin droplets were observed over the entire biomass surface after pretreatment. Hemicellulose removal and morphological changes improved enzyme accessibility to cellulose by increasing cellulose exposure to enzyme. It is thus evidence that enzyme adsorption is a significant factor to understand pretreatment effectiveness.

• Journal of Microbiology and Biotechnology
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• v.22 no.3
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• pp.343-351
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• 2012

In this paper, the kinetics of a cloned special glucosidase, named ginsenosidase type III hydrolyzing 3-O-glucoside of multi-protopanaxadiol (PPD)-type ginsenosides, were investigated. The gene (bgpA) encoding this enzyme was cloned from a Terrabacter ginsenosidimutans strain and then expressed in E. coli cells. Ginsenosidase type III was able to hydrolyze 3-O-glucoside of multi-PPD-type ginsenosides. For instance, it was able to hydrolyze the 3-O-${\beta}$-D-(1${\rightarrow}$2)-glucopyranosyl of Rb1 to gypenoside XVII, and then to further hydrolyze the 3-O-${\beta}$-D-glucopyranosyl of gypenoside XVII to gypenoside LXXV. Similarly, the enzyme could hydrolyze the glucopyranosyls linked to the 3-O-position of Rb2, Rc, Rd, Rb3, and Rg3. With a larger enzyme reaction $K_m$ value, there was a slower enzyme reaction speed; and the larger the enzyme reaction $V_{max}$ value, the faster the enzyme reaction speed was. The $K_m$ values from small to large were 3.85 mM for Rc, 4.08 mM for Rb1, 8.85 mM for Rb3, 9.09 mM for Rb2, 9.70 mM for Rg3(S), 11.4 mM for Rd and 12.9 mM for F2; and $V_{max}$ value from large to small was 23.2 mM/h for Rc, 16.6 mM/h for Rb1, 14.6 mM/h for Rb3, 14.3 mM/h for Rb2, 1.81mM/h for Rg3(S), 1.40 mM/h for Rd, and 0.41 mM/h for F2. According to the $V_{max}$ and $K_m$ values of the ginsenosidase type III, the hydrolysis speed of these substrates by the enzyme was Rc>Rb1>Rb3>Rb2>Rg3(S)>Rd>F2 in order.