• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.593-593
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• 2003

• Biotechnology and Bioprocess Engineering:BBE
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• v.9 no.3
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• pp.223-228
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• 2004

Agricultural waste products, beech wood and walnut shells, were hydrolyzed at 40$^{\circ}C$ using mixed crude enzymes produced by Penicillium sp. AHT-1 and Rhizomucor pusillus HHT-1. D-xylose, 4.1 g and 15.1 g was produced from the hydrolysis of 100 g of beech wood and walnut shells, respectively. For xylitol production, Candida tropicalis IFO0618 and the waste product hydrolyzed solutions were used. The effects on xylitol production, of adding glucose as a NADPH source, D-xylose and yeast extract, were examined. Finally, a 50% yield of xylitol was obtained by using the beech wood hydrolyzed solution with the addition of 1% yeast extract and 1% glucose at an initial concentration.

• Journal of Life Science
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• v.28 no.11
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• pp.1277-1284
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• 2018

In this study, a repeated yeast integrative plasmid (R-YIp) harboring Cre/loxP system was constructed to integrate various gene expression cassettes into the yeast chromosome. The R-YIp system contains a reusable selective marker (CgTRP1), loxP sequence, and target sequence for integration. Therefore, many gene expression cassettes can be integrated into the same position of the same yeast chromosome. In the present study, several model enzymes involving xylan/xylose metabolism were examined, including endoxylanase (XYLP), ${\beta}$-xylosidase (XYLB), xylose reductase (GRE3) and xylitol dehydrogenase (XYL2). Efficient expression of these genes was obtained using two promoters (GAL10p and ADH1p) and various plasmids (pGMF-GENE and pAMF-GENE plasmids) were constructed. The XYLP, XYLB, GRE3, and XYL2 genes were efficiently expressed under the control of the GAL10 promoter. Subsequently, R-YIps containing the GAL10p-GENE-GAL7t cassette were constructed, resulting in pRS-XylP, pRS-XylB, pRS-Gre3, and pRS-Xyl2 plasmids. These plasmids were sequentially integrated into chromosome VII of a Saccharomyces cerevisiae strain by repeated gene integration and selective marker rescue. These genes were integrated by the R-YIp system and were stably expressed in the yeast transformants to produce active recombinant enzymes. Therefore, we expect that the R-YIp system will be able to overcome current limitations of the host cells and allow selective marker selection for the integration of various genes into the yeast chromosome.

• Journal of Microbiology and Biotechnology
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• v.30 no.10
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• pp.1467-1479
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• 2020

Profiling the transcriptome changes involved in xylose metabolism by the fungus Trichoderma reesei allows for the identification of potential targets for ethanol production processing. In the present study, the transcriptome of T. reesei HJ-48 grown on xylose versus glucose was analyzed using next-generation sequencing technology. During xylose fermentation, numerous genes related to central metabolic pathways, including xylose reductase (XR) and xylitol dehydrogenase (XDH), were expressed at higher levels in T. reesei HJ-48. Notably, growth on xylose did not fully repress the genes encoding enzymes of the tricarboxylic acid and respiratory pathways. In addition, increased expression of several sugar transporters was observed during xylose fermentation. This study provides a valuable dataset for further investigation of xylose fermentation and provides a deeper insight into the various genes involved in this process.

• Microbiology and Biotechnology Letters
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• v.45 no.1
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• pp.57-62
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• 2017

Recently, we isolated the mutant Kluyveromyces marxianus 36907-FMEL1, which demonstrated improved xylose reductase activity as compared to the parental strain, K. marxianus ATCC 36907. Effects of agitation conditions on xylitol production were verified using a bioreactor system. Under an agitation speed of 400 rpm, K. marxianus 36907-FMEL1 exhibited the highest xylitol yield (0.57 g/g) and productivity ($0.64g{\cdot}l^{-1}{\cdot}h^{-1}$) at $30^{\circ}C$. When the fermentation temperature was increased to $40^{\circ}C$, interestingly, xylitol yield and productivity were found to be increased to 21% (0.64 g/g) and 58% ($0.90g{\cdot}l^{-1}{\cdot}h^{-1}$), respectively, under the optimized agitation conditions.

• Korean Journal of Microbiology
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• v.48 no.2
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• pp.156-162
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• 2012

A mannitol dehydrogenase (StMDH) gene was cloned from Salmonella typhimurium LT2 (KCTC 2421) and overexpressed in Escherichia coli. It has a 1,467 bp open reading frame encoding 488 amino acids with deduced molecular mass of 54 kDa, which shares approximately 36% of amino acid identity with known long-chain dehydrogenase/reductatse (LDR) family enzymes. The recombinant StMDH showed the highest activity at $30^{\circ}C$, and pH 5.0 and 10.0 for D-fructose reduction and D-mannitol oxidation, respectively. On the contrary, it has no activity on glucose, galactose, xylose, and arabinose. StMDH can catalyze the oxidative/reductive reactions between D-fructose and D-mannitol only in the presence of $NAD^+$/NADH as coenzymes. These results indicate that StMDH is a typical $NAD^+$/NADH-dependent mannitol dehydrogenase (E.C. 1.1.1.67).