• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.435-438
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• 2003

Epoxide hydrolase(EH) catalyze the enantioselective hydrolysis of racemic epoxides to corresponding diols. A recombinant Pichia pastoris with EH from Rhodotorula glutinis has been constructed by reverse transcriptase-polymerase chain reaction(RT-PCR). The recombinant biocatalyst enantioselectively hydrolyze (R)-styrene oxide faster than (S)-enantiomer. The catalytic activity of recombinant biocatalyst was 7-fold higher than that of wild-type strain. The recombinant EH biocatalyst can be used for kinetic resolution for the production of enantiopure styrene oxide.

• Journal of Applied Biological Chemistry
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• v.43 no.4
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• pp.207-210
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• 2000

As a typical example of the screening for a microbial biocatalyst from nature, isolation of nitrilesynthesizing microorganisms, characterization of a new enzyme aldoxime dehydratase, and its function in the aldoxime-nitrile pathway are introduced. Catalytic properties of some of our enzymes were improved through a direct evolutionary approach.

• 제어로봇시스템학회:학술대회논문집
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• 1987.10b
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• pp.637-642
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• 1987

In immobilized cell reactors, effective cell mass is a very important parameter which must be estimated during operation for control and regeneration of biocatalyst. In this report, the effective cell mass in immobilized cell reactor was studied using a sequential estimation method. An immobilized yeast reactor was operated in batch recycle mode. The states of the immobilized cell reactor could be estimated from the process data using an extended Kalman filter.

• Textile Coloration and Finishing
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• v.32 no.4
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• pp.193-198
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• 2020

In this study, the validity of extracts from food waste as biocatalyst for indigo reduction was examined. Dried food wastes such as apple peel and corn waste were water-extracted and freeze-dried. The reducing power of extracts for indigo was evaluated by the oxidation-reduction potential(ORP) measurement of reduction bath and color strength(K/S value) of the fabrics dyed in the indigo reduction bath. Total sugar contents of the apple peel and corn waste extracts were 60.56% and 62.36%, respectively. Antioxidant activity was 64.78% for the extract of apple peel and 7.96% for the extract of corn waste. Indigo reduction took place quickly with both extracts, and maximum color strength was obtained up to 15.91 and 12.11 within 1-3 days, respectively. The oxidation-reduction potential of reduction bath was stabilized in the range of -500 ~ -620 mV according to the kinds of food waste and the extract concentration. At higher concentration of the extracts, reduction power was maintained for longer time and stronger color strength was obtained. Compared to sodium dithionite, the reducing power of the studied extracts was lower, but the reduction stability was superior to it. The studied extracts were effective biocatalyst as biodegradable and safe alternatives to sodium dithionite for indigo reduction.

• Journal of Life Science
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• v.16 no.3 s.76
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• pp.375-381
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• 2006

Aldehyde reductase was purified to electrophoretic homogeneity from Saccharomyces cerevisiae, and then enzymatic reduction of substituted carbonyl compounds was carried out by using the purified aldehyde reductase as a biocatalyst. Under preparative scale reaction renditions, the enzymatic reduction proceeded in high chemical yield with excellent chemoselectivity. The enzymatic reduction product was identified by TLC, GC, Mass, NMR and FT-IR. Benzoic acid, an inhibitor of aldehyde reductase, also potently inhibited the reduction of substituded carbonyl compounds. This enzyme exhibited a broad substrate specificity , and can utilize both NADH and NADPH as cofactors. The enzyme was strongly inhibited by benzoic acid and quercetin. The apparent Km for 4-cyanobenzaldehyde and 3-nitrobenzamide were 4.894 mM and 0.305 mM, respectively.

• Journal of Microbiology and Biotechnology
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• v.26 no.7
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• pp.1267-1277
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• 2016

Currently, enzymatic synthesis of lactulose, a synthetic prebiotic disaccharide, is commonly performed with glycosyl hydrolases. In this work, a new type of lactulose-producing biocatalyst was developed by displaying β-galactosidase from Bacillus stearothermophilus IAM11001 (Bs-β-Gal) on the surface of Bacillus subtilis 168 spores. Localization of β-Gal on the spore surface as a fusion to CotX was verified by western blot analysis, immunofluorescence microscopy, and flow cytometry. The optimum pH and temperature for the resulting spore-displayed β-Gal was 6.0 and 75℃, respectively. Under optimal conditions, it showed maximum activity of 0.42 U/mg spores (dry weight). Moreover, the spore-displayed CotX-β-Gal was employed as a whole cell biocatalyst to produce lactulose, yielding 8.8 g/l from 200 g/l lactose and 100 g/l fructose. Reusability tests showed that the spore-displayed CotX-β-Gal retained around 30.3% of its initial activity after eight successive conversion cycles. These results suggest that the CotX-mediated spore-displayed β-Gal may provide a promising strategy for lactulose production.

• Journal of Microbiology and Biotechnology
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• v.28 no.8
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• pp.1346-1351
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• 2018

Oxidoreductases are effective biocatalysts, but their practical use is limited by the need for large quantities of NAD(P)H. In this study, a whole-cell biocatalyst for NAD(P)H cofactor regeneration was developed using the economical substrate glycerol. This cofactor regeneration system employs permeabilized Escherichia coli cells in which the glpD and gldA genes were deleted and the gpsA gene, which encodes $NAD(P)^+-dependent$ glycerol-3-phosphate dehydrogenase, was overexpressed. These manipulations were applied to block a side reaction (i.e., the conversion of glycerol to dihydroxyacetone) and to switch the glpD-encoding enzyme reaction to a gpsA-encoding enzyme reaction that generates both NADH and NADPH. We demonstrated the performance of the cofactor regeneration system using a lactate dehydrogenase reaction as a coupling reaction model. The developed biocatalyst involves an economical substrate, bifunctional regeneration of NAD(P)H, and simple reaction conditions as well as a stable environment for enzymes, and is thus applicable to a variety of oxidoreductase reactions requiring NAD(P)H regeneration.

• KSBB Journal
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• v.8 no.4
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• pp.320-327
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• 1993

Latex microspheres of styrene/acryl copolymer with acrylamide functional group were used for the stable covalent immobilization of an enzyme applicable for enzymatic synthesis of glycoside. The latex microspheres were coated with polyethyleneimine to establish structural and functional properties relevant to the covalent Immobilization with a high retention of activity. Polythyleneimine-coated microspheres satisfactorily immobilized the invertase for methyl fructoside synthesis, and model reaction were formed into alginate-enclosed microspheres biocatalyst. Using the alginate-enclosed microspheres biocatalyst, the yield of model glycoside was obtained as high as 52.2% at concentration of aqueous 30%(v/v) methanol and 0.291mo1/1 sucrose solution with 2U/ml of activity. The present study showed that the latex microspheres were successfully applied to enzymatic synthesis of glycoside.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2001.06a
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• pp.97-97
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• 2001

• Journal of the Korean Chemical Society
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• v.51 no.2
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• pp.154-159
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• 2007

Biodegradation of Quinoline by free and immobilized Bacillus brevis has been investigated. The rate of quinoline degradation by immobilized Bacillus brevis on coconut shell carbon is faster than the rate by the microorganism immobilized on foam pieces and free cells. A complete removal of 100 ppm of Quinoline in the sample was achieved at a hydraulic retention time of 20 hours with the biocatalyst prepared by immobilizing Bacillus brevis onto coconut shell carbon. The biocatalyst had a reasonable shelf life and desirable recycle capacity.