• KSBB Journal
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• v.30 no.4
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• pp.166-174
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• 2015

In this study, an efficient whole cell-based biotransformation for the production of liquiritigenin was developed using Laetiporus sulphureus CS0218 as biocatalyst and aqueous extracts of Glycyrrhiza uralensis as co-substrate, respectively. In order to determine the efficacy of this method, the optimal bioconversion conditions including mycelial growth, three important enzyme activities (${\beta}$-glucosidase, ${\alpha}$-rhamnosidase and ${\beta}$-xylosidase), and apparent viscosity of culture broth were monitored. After optimization, aqueous extracts of G. uralensis were added to the culture medium to directly produce algycone liquiritigenin. By applying this strategy, 67.5% of liquiritin was converted to liquiritigenin at pH 3.0 after 9 days of incubation and finally liquiritigenin was purified from the reaction mixture. And then, their biological activities including anti-oxidant and superoxide dismutase were observed. In fact, purified liquiritigenin was capable of bi-directional functions (i.e., either up-regulation or down-regulation of SIRT1 which is associated with aging). The results indicate that this strategy would be beneficial to produce biologically active liquiritigenin and could be used in pharmaceutical, cosmetic and food applications.

• Journal of Microbiology and Biotechnology
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• v.18 no.5
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• pp.946-951
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• 2008

The opd gene, encoding organophosphorus hydrolase (OPH) from Flavobacterium sp. capable of degrading a wide range of organophosphate pesticides, was surface- and intracellular-expressed in Synechococcus PCC7942, a prime example of photoautotrophic cyanobacteria. OPH was displayed on the cyanobacterial cell surface using the truncated ice nucleation protein as an anchoring motif. A minor fraction of OPH was displayed onto the outermost surface of cyanobacterial cells, as verified by immunostaining visualized under confocal laser scanning microscopy and OPH activity analysis; however, a substantial fraction of OPH was buried in the cell wall, as demonstrated by proteinase K and lysozyme treatments. The cyanobacterial outer membrane acts as a substrate (paraoxon) diffusion barrier affecting whole-cell biodegradation efficiency. After freeze-thaw treatment, permeabilized whole cells with intracellular-expressed OPH exhibited 14-fold higher bioconversion efficiency ($V_{max}/K_m$) than that of cells with surface-expressed OPH. As cyanobacteria have simple growth requirements and are inexpensive to maintain, expression of OPH in cyanobacteria may lead to the development of a low-cost and low-maintenance biocatalyst that is useful for detoxification of organophosphate pesticides.

• Journal of Microbiology and Biotechnology
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• v.25 no.7
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• pp.1108-1113
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• 2015

Cadaverine (1,5-diaminopentane) is an important industrial chemical with a wide range of applications. Although there have been many efforts to produce cadaverine through fermentation, there are not many reports of the direct cadaverine production from lysine using biotransformation. Whole-cell reactions were examined using a recombinant Escherichia coli strain overexpressing the E. coli MG1655 cadA gene, and various parameters were investigated for the whole-cell bioconversion of lysine to cadaverine. A high concentration of lysine resulted in the synthesis of pyridoxal-5'-phosphate (PLP) and it was found to be a critical control factor for the biotransformation of lysine to cadaverine. When 0.025 mM PLP and 1.75 M lysine in 500 mM sodium acetate buffer (pH6) were used, consumption of 91% lysine and conversion of about 80% lysine to cadaverine were successfully achieved.

• Journal of Microbiology and Biotechnology
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• v.27 no.11
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• pp.1952-1960
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• 2017

Recently, soybean isoflavone aglycones (i.e., daidzein and genistein) and ${\gamma}-aminobutyric$ acid (GABA) have begun to receive considerable consumer attention owing to their potential as nutraceuticals. To produce these ingredients, multiple microorganisms and their enzymes are commonly used for catalysis in the nutraceutical industry. In this work, we introduce a novel fermentation process that uses whole-cell biocatalysis to accelerate GABA and isoflavone aglycone production in doenjang (a traditional Korean soybean paste). Microbial enzymes transform soybean isoflavone glycosides (i.e., daidzin and genistin) and monosodium glutamate into soybean isoflavone aglycones and GABA. Lactobacillus brevis GABA 100 and Aspergillus oryzae KACC 40250 significantly reduced the production time with the aid of a protease. The resulting levels of GABA and daidzein were higher, and genistein production resembled the levels in traditional doenjang fermented for over a year. Concentrations of GABA, daidzein, and genistein were measured as 7,162, 60, and $59{\mu}g/g$, respectively on the seventh day of fermentation. Our results demonstrate that the administration of whole-cell L. brevis GABA 100 and A. oryzae KACC 40250 paired with a protease treatment is an effective method to accelerate GABA, daidzein, and genistein production in doenjang.

• Microbiology and Biotechnology Letters
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• v.50 no.3
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• pp.395-403
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• 2022

In this study, we identified that the fermentation of Korean indigenous probiotics and red ginseng produced ginsenoside compound K (CK) from major ginsenosides. Based on whole genome sequencing of 19 probiotics species, β-glucosidase, α-arabinofuranosidase, β-xylosidase, and α-rhamnosidase related to bioconversion of ginsenosides are identified in the genome of 19 species, 3 species, 6 species, and 8 species, respectively. Among the 19 probiotics species, Bifidobacterium longum CBT BG7 converted from ginsenoside Rb1 to CK, and both B. breve CBT BR3 and B. lactis CBT BL3 converted ginsenoside Rb1 to Rd. The final concentration and yield of ginsenoside F2 and CK were higher in the fermentation with the nondisrupted cells than with disrupted cells. The combination of both CBT BG7 and BL3, and CBT BG7 and BR3 showed higher amounts of F2 than CBT BG7 only. CBT BG7 with adding α-amylase increased the amounts of F2. In this study, we identified that the fermentation of both Korean indigenous probiotic bacteria CBT BG7, BR3 and BL3, and red gingseng is able to produce CK, a bioactive compound that promotes health benefits.

• Journal of Microbiology and Biotechnology
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• v.27 no.1
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• pp.92-100
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• 2017

Acetoin (AC) is a volatile platform compound with various potential industrial applications. AC contains two stereoisomeric forms: (3S)-AC and (3R)-AC. Optically pure AC is an important potential intermediate and widely used as a precursor to synthesize novel optically active materials. In this study, chiral (3R)-AC production from meso-2,3-butanediol (meso-2,3-BD) was obtained using recombinant Escherichia coli cells co-expressing meso-2,3-butanediol dehydrogenase (meso-2,3-BDH), NADH oxidase (NOX), and hemoglobin protein (VHB) from Serratia sp. T241, Lactobacillus brevis, and Vitreoscilla, respectively. The new biocatalyst of E. coli/pET-mbdh-nox-vgb was developed and the bioconversion conditions were optimized. Under the optimal conditions, 86.74 g/l of (3R)-AC with the productivity of 3.61 g/l/h and the stereoisomeric purity of 97.89% was achieved from 93.73 g/l meso-2,3-BD using the whole-cell biocatalyst. The yield and productivity were new records for (3R)-AC production. The results exhibit the industrial potential for (3R)-AC production via whole-cell biocatalysis.