• Korean Journal of Agricultural Science
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• v.46 no.1
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• pp.1-10
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• 2019

The objective of this study was to determine the effect of multi-enzyme supplementation in a corn and soybean meal-based diet on the growth performance, apparent nutrient digestibility, blood profile, fecal microbes and noxious gas emission in growing pigs. A total of 80 crossbred [(Landrace ${\times}$ Yorkshire) ${\times}$ Duroc] growing pigs with an average body weight (BW) of $25.04{\pm}1.44kg$ were used in a 6-week experiment. The experimental treatments were as follows: CON, basal diet and; T1, basal diet + 100 mg/kg multi-enzyme. During the experiment, the pigs fed the diet with multi-enzyme supplementation had a higher gain to feed ratio (G/F) (p < 0.05) than the pigs fed the diet without multi-enzyme supplementation. On day 42, the pigs fed the diet with multi-enzyme supplementation had decreased $H_2S$ and $NH_3$ emissions (p < 0.05) than the pigs fed the diet without multi-enzyme supplementation. However, no effect was observed on nutrient digestibility, blood profiles and fecal microbes among the treatments (p > 0.05). In conclusion, it is suggested that multi-enzyme supplementation in a corn and soybean meal based diet can partly improve the growth performance and noxious gas emission of growing pigs.

• Korean Journal of Agricultural Science
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• v.48 no.2
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• pp.201-207
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• 2021

This study evaluated the influence of enzyme mixture supplementation on the growth performance, nutrient digestibility, and fecal score of growing pigs. A total of 72 pigs with an initial body weight of 20.23 ± 1.46 kg were randomly assigned to two treatments consisting of a basal diet and the basal diet supplemented with 0.5% enzyme mixture. During a 19-day trial, no significant difference was observed in the body weight (BW) and average daily feed intake (ADFI) of the pigs. However, a gradual increase in the average daily gain (ADG) was observed during the period from day 14 to day 19 and the overall period in pigs fed a diet supplemented with the 0.5% enzyme mixture (p < 0.10) as compared to the pigs that were fed the control diet. From days 4 to 14 and in the overall experiment, a gradual increase in the feed conversion ratio (FCR) (p < 0.10) was observed with the inclusion of 0.5% enzyme mixture supplementation. The nutrient digestibility of dry matter (DM), nitrogen (N), and energy were not affected by enzyme mixture supplementation. In addition, dietary supplementation with the enzyme mixture had no significant effects on the fecal score of growing pigs. In summary, supplementation with the enzyme mixture had beneficial effects on the ADG performance but failed to have a significant effect on growth performance (BW), nutrient digestibility, and fecal score.

• Microbiology and Biotechnology Letters
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• v.28 no.6
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• pp.329-333
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• 2000

Alkaline bacterium producing a high pro-tease activity at low temperature was isolated by using enrichment culture from soil samples and identified as Bacil-lus sp. WRD-1 Cell growth was maximal at 10 hours and the optimal initial pH and culture time of culture condition for enzyme production was pH 7 and 10 hours, respectively. Temperature range of high enzyme activity were $10~40^{\circ}C$. The optimal pH and temperature for the enzyme activity were pH9 and $30^{\circ}C$.

• Mycobiology
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• v.33 no.3
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• pp.142-146
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• 2005

To produce a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitor from yeast, a yeast isolate, designated G-14 showing the highest ACE inhibitory activity was obtained and identified as Malassezia pachydermatis based on morphological, biochemical and cultural characteristics. The maximal extracellular ACE inhibitor production was obtained from M. pachydermatis G-14 when the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone and 2.0% glucose at $30^{\circ}C$ for 24 h and the final ACE inhibitory activity was 48.9% under the above condition.

• Korean Journal of Plant Resources
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• v.25 no.3
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• pp.349-356
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• 2012

The antioxidant potential and enzyme activities in Salicornia herbacea, Corylopsis coreana, Erythronium japonicum, Phragmites communis, Momordica Charantia, Nelumbo nucifera, Salvia plebeia, Portulaca oleracea, Ficus carica, Citrus junos and Cornus officinalis were determined. Their antioxidant activities were measured using DPPH radical scavenging and nitrite scavenging activity. Enzyme activities in investigated plants were evaluated as superoxide dismutase (SOD), catalase (CAT), peroxidase (POD), and ascorbate peroxidase (APX). The DPPH scavenging rate from 100 to 2500 $mgL^{-1}$ was the highest in the flower of Corylopsis coreana. However, it was not detected in most of the samples at concentration below 100 $mgL^{-1}$. The nitrite scavenging activity according to each kind of resource plants was significantly higher in the stem of Corylopsis coreana and leaf of Nelumbo nucifera. The root extract of Erythronium japonicum had the highest SOD enzyme activity of 94.0% while leaf of Salvia plebeia showed the lowest SOD enzyme activity of 30.4%. The activity of CAT and APX showed higher values in the stem of Corylopsis coreana, root of Erythronium japonicum and root of Phragmites communis in comparison with other plants. The activity of POD showed significantly high values in stem of Corylopsis coreana, Momordica Charantia and pericarp of Citrus junos extracts. The antioxidant enzyme activities differ significantly in different plants. In conclusion, we showed that Corylopsis coreana, Erythronium japonicum Cornus officinalis, and Momordica Charantia had the potent biological activities. Therefore, these plant resources showing antioxidant activity could be good materials for development of source of functional healthy food.

• Korean Journal of Plant Resources
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• v.24 no.6
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• pp.712-718
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• 2011

Ginseng (Panax ginseng) is frequently used in Asian countries as a traditional medicine. The major components of ginseng are ginsenosides. Among these, ginsenoside compound K has been reported to prevent the formation of malignancy and metastasis of cancer by blocking the formation of tumor and suppressing the invasion of cancer cells. In this study, ginsenoside $Rb_1$ was converted into compound K, via secreted ${\beta}$-glucosidase enzyme from the Leuconostoc lactis DC201 isolated, which was extracted from Kimchi. The strain DC201 was suspended and cultured in MRS broth at $37^{\circ}C$. Subsequently, the residue from the cultured broth supernatant was precipitated with EtOH and then dissolved in 20 mM sodium phosphate buffer (pH 6.0) to obtain an enzyme liquid. Meanwhile, the crude enzyme solution was mixed with ginsenoside $Rb_1$ at a ratio of 1:4 (v/v).The reaction was carried out at $30^{\circ}C$ and 190 rpm for 72 hours, and then analyzed by TLC and HPLC. The result showed that ginsenoside Rb1 was transformed into compound K after 72 hours post reaction.

• Journal of Microbiology and Biotechnology
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• v.29 no.8
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• pp.1310-1315
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• 2019

Hyaluronidases enhance therapeutic drug transport by breaking down the hyaluronan barrier to lymphatic and capillary vessels, facilitating their tissue absorption. Commercially available hyaluronidases are bovine in origin; however, they pose risks such as bovine spongiform encephalopathy. The present study aimed to develop a novel, highly active hyaluronidase and assess its function. Therefore, in order to find the most efficient active hyaluronidase, we produced several shortened hyaluronidases with partial removal of the N- or C-terminal regions. Moreover, we created an enzyme that connected six histidines onto the end of the hyaluronidase C-terminus. This simplified subsequent purification using $Ni^{2+}$ affinity chromatography, making it feasible to industrialize this highly active recombinant hyaluronidase which exhibited catalytic activity equal to that of the commercial enzyme. Therefore, this simple and effective isolation method could increase the availability of recombinant hyaluronidase for research and clinical purposes.

• Microbiology and Biotechnology Letters
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• v.39 no.4
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• pp.357-363
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• 2011

This study focus was primarily the development of liquid starters for Aspergillus oryzae and Aspergillus niger prepared with wheat bran as a low cost culture medium. For the preparation of the liquid media wheat bran was added at rates of 0, 5, 10, 15 and 20% and the Aspergillus sp. strains were then inoculated to these prepared broths. The results indicated that the more that wheat bran was contained in the medium, the more mycelia was produced for A. oryzae and A. niger. The highest enzyme activities were obtained with a 10~15% adding rate of wheat bran for both strains. Changes in the enzyme activities of the liquid starters during various incubation times (0, 24, 48, 72 and 96 hrs), indicated that the highest enzyme activities were seen between 48 and 72 hrs of culture. In addition, a comparative study was carried out on the production of enzymes using wheat as a substrate in nuruk, with liquid starter made from fermented agents according to the same concentrations used with the wheat bran. The pH, acidity, amino acidity, reducing sugar content and enzyme activity (${\alpha}$-amylase, glucoamylase, acidic protease) of wheat nuruk made with liquid starter were compared with those of wheat nuruk made with solid starter. The results suggest that the liquid starter is superior in both cases.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1318-1323
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• 2004

This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.

• Journal of Ginseng Research
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• v.36 no.3
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• pp.291-297
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• 2012

Ginsenoside (ginseng saponin), the principal component of ginseng, is responsible for the pharmacological and biological activities of ginseng. We isolated lactic acid bacteria from Kimchi using esculin agar, to produce ${\beta}$-glucosidase. We focused on the bio-transformation of ginsenoside. Phylogenetic analysis was performed by comparing the 16S rRNA sequences. We identified the strain as Lactobacillus (strain 6105). In order to determine the optimal conditions for enzyme activity, the crude enzyme was incubated with 1 mM ginsenoside Rb1 to catalyse the reaction. A carbon substrate, such as cellobiose, lactose, and sucrose, resulted in the highest yields of ${\beta}$-glucosidase activity. Biotransformations of ginsenoside Rb1 were analyzed using TLC and HPLC. Our results confirmed that the microbial enzyme of strain 6105 significantly transformed ginsenoside as follows: Rb1${\rightarrow}$gypenoside XVII, Rd${\rightarrow}$F2 into compound K. Our results indicate that this is the best possible way to obtain specific ginsenosides using microbial enzymes from 6105 culture.