• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.126-130
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• 1989

In 14 kinds of ginsenosides in ginseng saponin, ginsenoside Rbr is contained the most abundantly. But ginsenoside Rd which is similar to ginsenoside R $b_1$in structure, was known to be superior to ginsenoside R $b_1$pharmaceutically. The convertible enzyme which can transform ginsenoside R $b_1$to Binsenoside Rd specifically among ginseng saponin, was purified homogeneously from Rhizopus japonicus. The optimal pH for the action of the enzyme was pH 4.8 to 5.0, and optimal temperature was 45$^{\circ}C$. The enzyme was stable in the range of pH 4.0 to 9.0, and the half activity of enzyme was remained by the thermal treatment at 6$0^{\circ}C$ for 2 hours. The enzyme activity was enhanced by addition of M $n^{++}$ or Fe, though inhibited by EDTA or o-phenanthroline. On the substrate specificity, the enzyme was. able to hydrolyze gentiobiose, cellobiose, amygdalin and prunasin, but not to hydrolyze any other kinds of Binsenosides besides Binsenoside R $b_1$. Km values of the enzyme for ginsenoside R $b_1$, gentiobiose and amygdalin were 5.0mM, 4.8mM and 3.7mM, respectively.3.7mM, respectively.y.

• Microbiology and Biotechnology Letters
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• v.45 no.3
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• pp.236-242
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• 2017

The conversion of marine biomass to renewable energy has been considered an alternative to fossil fuels. Butanol, in particular, can be used directly as a fuel. In this experiment, the brown alga Undaria pinnatifida was selected as a biomass for biobutanol production. Hyper thermal (HT) acid hydrolysis was used as an acid hydrolysis method to produce monosaccharides. The optimal pretreatment conditions for U. pinnatifida were determined as slurry with 10% (w/v) U. pinnatifida content and 270 mM $H_2SO_4$, and heating at $160^{\circ}C$ for 7.5 min. Enzymatic saccharification was carried out with Celluclast 1.5 L, Viscozyme L, and Ultraflo Max. The optimal saccharification condition was 12 U/ml Viscozyme L. Fermentations were carried out for the production of acetone, butanol, and ethanol by Clostridium acetobutylicum KCTC 1724, Clostridium beijerinckii KCTC 1785, and Clostridium tyrobutyricum KCTC 5387. The fermentations were carried out using a pH-control. The optimal ABE fermentation condition determined using C. acetobutylicum KCTC 1724 adapted to 160 g/l mannitol. An ABE concentration of 9.05 g/l (0.99 g/l acetone, 5.62 g/l butanol, 2.44 g/l ethanol) was obtained by the consumption of 24.14 g/l monosaccharide with $Y_{ABE}$ of 0.37 in pH 5.0.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.24 no.2
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• pp.111-116
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• 1991

The effective p.eduction of 5'-GMP(5'-Guanylic acid) by enzymatic conversion of 5'-XMP(5'-Xanthyic acid) was investigated. The Iyophilized Brevibacterium ammoniagenes ATCC 19216 which were used as the XHP aminase source, was immobilized by entrapping in K-carrageenan, agar, polyacrylamide or Ca-alginate. $3\%$ K-carrageenan was selected as the most suitable matrix. In the production of 5'-GMP using the free cells of 3. ammoniagenes ATCC 19216, the optimum conditions were $42^{\circ}C$, PH 7.0, 100mg/ml glucose, 120mg/ml cell ,8mg/ml $MgSO_4\cdot7H_2O$, 5mg/ml POESA, 5mg/ml phytic acid. Under the conditions, $94.5\%$ of 5'-GMP was converted within 8 hours. In the production of 5'-GMP using the immobilized whole cells of B. ammoniagenes ATCC 19216, the optimum conditions were $37^{\circ}C$, pH 7.5, 50mg/ml glucose, 1mg/ml $KH_2PO_4$, 10mg/ml phytic acid, 60mg/ml cell, 8mg/ml $MgSO_4\;\cdot\;7H_2O$, 5mg/ml POESA. Under the conditions, $64.7\%$ of 5'-GMP was converted within 40 hours.

• Journal of Microbiology and Biotechnology
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• v.30 no.5
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• pp.785-792
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• 2020

ʟ-Theanine, found in green tea leaves has been shown to positively affect immunity and relaxation in humans. There have been many attempts to produce ʟ-theanine through enzymatic synthesis to overcome the limitations of traditional methods. Among the many genes coding for enzymes in the ʟ-theanine biosynthesis, glutamylmethylamide synthetase (GMAS) exhibits the greatest possibility of producing large amounts of production. Thus, GMAS from Methylovorus mays No. 9 was overexpressed in several strains including vectors with different copy numbers. BW25113(DE3) cells containing the pET24ma::gmas was selected for strains. The optimal temperature, pH, and metal ion concentration were 50℃, 7, and 5 mM MnCl₂, respectively. Additionally, ATP was found to be an important factor for producing high concentration of ʟ-theanine so several strains were tested during the reaction for ATP regeneration. Baker's yeast was found to decrease the demand for ATP most effectively. Addition of potassium phosphate source was demonstrated by producing 4-fold higher ʟ-theanine. To enhance the conversion yield, GMAS was additionally overexpressed in the system. A maximum of 198 mM ʟ-theanine was produced with 16.5 mmol/l/h productivity. The whole-cell reaction involving GMAS has greatest potential for scale-up production of ʟ-theanine.

• Applied Biological Chemistry
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• v.43 no.1
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• pp.12-17
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• 2000

For the enzymatic production of $2-O-{\alpha}-D-glucopyranosyl-L-ascorbic$ acid (AA-2G) from ascorbic acid, rice seed was used as the source of ${\alpha}-glucosidase$ having transglucosylation activity. Among six rice varieties, cultivated in Korea, ${\alpha}-glucosidase$ activity of Oryza savita L. cv. Ilpumbyeo was the highest with 125.03 unit/ml and it had maximum specific activity with 8.52 unit/mg protein when rice seeds were grown for 3 days after germination. For the production of AA-2G using crude extract of O. savita L. cv. Ilpumbyeo, maltose was most effective glucose donor. The optimum concentration of maltose and ascorbic acid were 125 mM and 175 mM, respectively. The optimum concentration of ${\alpha}-glucosidase$ was 100 unit. The most effective buffer was 100 mM sodium citrate. The optimum pH and temperature were 5.0 and $60^{\circ}C$, respectively. Under the optimum condition, $108.43\;{\mu}M/unit$ of AA-2G was produced from ascorbic acid after 35 minutes of reaction, which corresponds to 6.2% of conversion ratio based on the amount of ascorbic acid used.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 2011.10a
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• pp.167-177
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• 2011

Renewable energy resources and technologies have the potential to provide long-lasting solutions of the global energy-requirements faced by the economic and environmental sectors of a nation. Therefore, waste money bills were used as renewable energy source for the production of bio-ethanol. In this study, different concentrated NaOH 0.5%. 1.0%, 2.0%, 3.0% and 0.0% (as a control) were used for 10, 20 and 30 mins at $121^{\circ}C$/15 psi in an autoclave. Saccharification and fermentation (aerobic and anaerobic) were carried out through commercial enzyme Celluclast 1.5 L, Novozymes 188 and Saccharomyces cerevisiae KCCM 11304 respectively. The results of pretreatment showed that the NaOH pre-treated substrate enhanced enzyme action and released more amount of glucose. The amount of glucose was found with the increasing concentration of NaOH and time $44996.95{\pm}6.30$, $46763.10{\pm}3.56$, $53421.32{\pm}4.72$, $63431.25{\pm}6.95$ and $56850.98{\pm}6.75\;ng/{\mu}l$ for 30 min respectively. As for bioethanol, the conversion rate of NaOH resulted $1010.08{\pm}4.71$, $1050.25{\pm}4.37$, $1109.49{\pm}4.39$, $1139.25{\pm}3.26$ and $1020.77{\pm}3.89$ ppm for aerobic; $16730.54{\pm}6.67$, $17076.45{\pm}6.25$, $17516.17{\pm}4.49$, $19782.68{\pm}6.19$ and $17973.39{\pm}7.50$ ppm for anaerobic and $18935.02{\pm}4.59$, $19895.45{\pm}5.39$, $21912.95{\pm}4.83$, $24895.21{\pm}6.72$ and $18961.21{\pm}4.90$ ppm for anaerobic condition with benzoic acid for respective condition. Thus, the results of the present work clearly revealed that with the increasing of alkali concentration might be more effective for bio-ethanol production from waste money bill, which is economic and environmental friendly.

• The Korean Journal of Food And Nutrition
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• v.28 no.6
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• pp.1026-1032
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• 2015

This study attempted to find an efficient method for the preparation of high-purity galactooligosaccharides (HP-GOS) using ${\beta}$-galactosidase and yeast fermentation. GOS prepared using Lactozym 3000L showed the greatest enhancement in total GOS of the six ${\beta}$-galatosidases tested. GOS alone achieved 51% conversion of initial lactose. GOS production was enhanced by fermentation with commercial yeast (Saccharomyces cerevisiae); its concentration reached 71% after 36h fermentation with 8% yeast. Component sugar analysis with HPLC indicated that HP-GOS fermented with S. cerevisiae showed significantly increased levels of 4'/6'-galactosyllactose and total GOS as well as a significantly decreased glucose level. HP-GOS facilitated the growth of Lactobacillus sp. (L. acidophilus and L. casei) and Bifidobacterium sp. (B. longum and B. bifidum). In sum, high-purity GOS has been successfully produced through both an enzymatic process and yeast fermentation. GOS encourages the growth of bacteria such as Lactobacillus and Bifidobacterium that may be beneficial to human gastrointestinal health.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.43 no.4
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• pp.373-379
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• 2017

We carried out the enzymatic synthesis of 1, 2-hexanediol galactoside (HD-gal) by transgalactosylation reaction using recombinant Escherichia coli ${\beta}-galactosidase$ (${\beta}-gal$). The amounts of ${\beta}-gal$ and 1, 2-hexanediol (HD), pH, and temperature, respectively, were first optimized (${\beta}-Gal$, 4.8 U/mL; HD, 75 mM; pH, 7.0; temperature, $37^{\circ}C$). Under these optimal conditions, about 96% HD was converted to HD-gal. When we investigated the water holding capacities (WHCs) of HD and HD-gal using pig epidermis in the concentrations of 84.4, 126.6, 168.8, 211.0 mM, WHC of HD-gal was superior to HD. In particular, at 168.8 mM HD and HD-gal, WHC of HD-gal showed about 20% greater than that of HD. However, it was observed that MIC values against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus of HD-gal were about three to ten times greater than those of HD, although MIC value of HD-gal against Enterococcus faecalis was almost the same as that of HD. Finally, it was concluded that the covalent bonding of a galactose molecule to HD (transgalactosylation) resulted in an increase in WHC of HD-gal and a decrease in anti-bacterial activity.

• Microbiology and Biotechnology Letters
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• v.42 no.1
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• pp.11-17
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• 2014

Selenium is an essential trace element for mammals, but it is very toxic. Therefore, the control of selenium concentrations should be precisely and effectively monitored. Selenium is naturally obtained through foods and seleno-L-methionine (LSeMet) is a major form of selenium. It has been reported that L-SeMet is only converted into Se-adenosyl-L-SeMet. However, a recent study suggested that L-SeMet was directly metabolized into methylselenol ($CH_3SeH$) in mouse liver extract by the reaction of cystathionine ${\gamma}$-lyase (CGL). The canonical reaction of CGL was known to catalyze the cleavage of L-cystathionine to L-cysteine, ${\alpha}$-ketobutyrate and $NH_3$. In the present study, we found that L-SeMet could be directly converted to $CH_3SeH$ using purified homogenous human CGL instead of mouse liver cytosol. Authentic $CH_3SeH$ was prepared by reduction of dimethyldiselenide with sodium tetrahydroborate. The gaseous product of the enzymatic reaction with L-SeMet was analyzed by GC/MS spectrometry. The GC/MS data was identical to that of authentic dinitrophenyl selenoether. We also analyzed the kinetic parameters for the formation of $CH_3SeH$ from L-SeMet by human and mouse CGL. These results suggest that human CGL is a critical enzyme which is responsible for L-SeMet metabolism.

• Food Engineering Progress
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• v.14 no.4
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• pp.292-298
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• 2010

Wheat germ contains the glycosylated forms of 2-methoxy-p-benzoquinone (2-MBQ) and 2,6-dimethoxy-p-benzoquinone (2,6-DMBQ), both of which have antimicrobial and immunostimulatory effects. Conversion of glycosylated 2-MBQ and 2,6-DMBQ to their more functional unglycosylated forms requires enzymatic action of $\beta$-glucosidase. We investigated the applications of lactic acid bacteria and yeast that produce $\beta$-glucosidase as starters for production of unglycosylated 2-MBQ and 2,6-DMBQ from wheat germ. Lactobacillus zeae and Pichia pijperi were selected through $\beta$-glucosidase enzyme assays for 37 yeast strains and five strains of lactic acid bacteria. Lb. zeae was more efficient than P. pijperi at producing 2-MBQ and 2,6-DMBQ from wheat germ. After 48 hr of fermentation with a mixed culture of Lb. zeae and P. pijperi, the concentration of 2-MBQ was 0.46${\pm}$0.07 mg/g, indicating an approximately 1.6-fold higher concentration than that obtained by pure culture of Lb. zeae. However, the concentration of 2,6-DMBQ was not significantly enhanced by fermentation with a mixed culture of Lb. zeae and P. pijperi.