Ho Myeong Kim

Chonnam National University, Gwangju, Gwangju, South Korea

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Publications (7)22.01 Total impact

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    ABSTRACT: The microalga Chlorella vulgaris is a potential feedstock for bioenergy due to its rapid growth, carbon dioxide fixation efficiency, and high accumulation of lipids and carbohydrates. In particular, the carbohydrates in microalgae make them a candidate for bioethanol feedstock. In this study, nutrient stress cultivation was employed to enhance the carbohydrate content of C. vulgaris. Nitrogen limitation increased the carbohydrate content to 22.4% from the normal content of 16.0% on dry weight basis. In addition, several pretreatment methods and enzymes were investigated to increase saccharification yields. Bead-beating pretreatment increased hydrolysis by 25% compared with the processes lacking pretreatment. In the enzymatic hydrolysis process, the pectinase enzyme group was superior for releasing fermentable sugars from carbohydrates in microalgae. In particular, pectinase from Aspergillus aculeatus displayed a 79% saccharification yield after 72h at 50°C. Using continuous immobilized yeast fermentation, microalgal hydrolysate was converted into ethanol at a yield of 89%.
    Bioresource Technology 12/2013; 153C:47-54. · 5.04 Impact Factor
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    ABSTRACT: Rice straw has considerable potential as a raw material for bioethanol production. Popping pretreatment of rice straw prior to downstream enzymatic hydrolysis and fermentation was found to increase cellulose to glucose conversion efficiency. The aim of this study was to investigate the influence of popping pretreatment and determine the optimal enzyme loading using a surface response design. The optimal doses of cellulase and xylanase enzymes were 23 FPU and 62 IU/g biomass, respectively. Using the optimized enzyme condition and popping pretreatment of rice straw (15% substrate loading, w/v), a sugar recovery of 0.567 g/g biomass (glucose; 0.394 g/g) was obtained in 48 h, which was significantly higher than that from untreated rice straw (total sugar recovery; 0.270 g/g biomass). Fermentation of the hydrolyzates by Saccharomyces cerevisiae resulted in 0.172 g ethanol/g biomass after 24 h, equivalent to 80.9% of the maximum theoretical yield (based on the amount of glucose in raw material). Changes in the chemical composition and surface area of rice straw were also investigated before and after popping pretreatment. The results showed little or no difference in chemical composition between the pretreated rice straw and the control. However, the surface area of pretreated rice straw increased twofold compared to the control. Popping pretreatment of rice straw can effectively improve downstream saccharification and fermentation, important for bioethanol production.
    Biotechnology for Biofuels 11/2013; 6(1):166. · 5.55 Impact Factor
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    ABSTRACT: The xylanase gene from Gloeophyllum trabeum was cloned and expressed in Pichia pastoris GS115. Xyl10g has a molecular weight of approximately 50 kDa, and exhibits maximum specific activity at 70 °C and a broad range of pH 4.0 to 7.0. Purified recombinant Xyl10g efficiently degraded popping-pretreated corn stover and newspaper waste at 50 °C and pH 4.0 after 24 h, and showed synergistic effects with Cel5B (endoglucanase) and BglB (β-glucosidase) to increase reduced sugar levels by about 1.71- to 1.88-fold and 2.26- to 2.48-fold, respectively. Although Xyl10g has low specific activity for beechwood xylan, as compared to XynA, Xyl10g more efficiently degraded corn stover than did XynA. According to immunogold labeling analysis, Xyl10g can attack highly substituted, unsubstituted, and low-substituted xylans, whereas XynA cannot efficiently attack highly substituted xylans, which is important for lignocellulose degradation. These results suggest that GH10 Xyl10g can be used for lignocellulose degradation.
    Journal of Biotechnology 01/2013; · 3.18 Impact Factor
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    ABSTRACT: The gene of endo-beta-1-4 xylanase, xynT, was cloned from Bacillus alcalophilus AX2000 and expressed in Escherichia coli. This XynT, which belongs to glycoside hydrolase (GH) family 10, was found to have a molecular weight of approximately 37 kDa and exhibit optimal activity at pH 7-9 and 50 °C. It exhibits a high activity towards birchwood xylan and has the ability to bind avicel. Under optimal conditions, XynT hydrolyzes all xylooligomers into xylobiose as an end product with a preference for cleavage sites at the second or third glycosidic bond from the reducing end. XynT has a different substrate affinity on xylooligomers at pH 5.0, which contributes to its low activity toward xylotriose and its derived intermediate products. This low activity may be due to an unstable interaction with the amino acids that constitute subsites of the active site. Interestingly, the addition of Co(2+) and Mn(2+) led to a significant increase in activity by up to 40 and 50 %, respectively. XynT possesses a high binding affinity and hydrolytic activity toward the insoluble xylan, for which it exhibits high activity at pH 7-9, giving rise to its efficient biobleaching effect on Pinus densiflora kraft pulp.
    Journal of Industrial Microbiology 07/2012; 39(10):1465-75. · 1.80 Impact Factor
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    ABSTRACT: Contrary to extensive researches on the roles of metallothioneins (MTs) in metal tolerance of animals, the roles of plant MTs in metal tolerance are largely under investigation. In this study, we evaluated the functional role of type 2 MT from Colocasia esculenta (CeMT2b) in Zn tolerance of tobacco and E. coli cells. Under Zn-stress conditions, transgenic tobacco overexpressing CeMT2b displayed much better seedling growth, a significant decrease in the levels of H(2)O(2) and an increase in Zn accumulation compared with the wild type. Overexpression of CeMT2b in E. coli greatly enhanced Zn tolerance and Zn accumulation under Zn stresses compared with control cells. CeMT2b bound 5.38 ± 0.29 atoms of Zn per protein. To identify a structural domain of CeMT2b for Zn binding, we investigated the growth of E. coli expressing each of the N-terminal, C-terminal, and central linker domains or a CNC motif deletion from the C-terminus of full-length CeMT2b. The results showed that the CNC motif is required for Zn tolerance, and the N-terminal domain is more effective in Zn tolerance than the C-terminal domain. Taken together, our results provide direct evidence for functional contributions of CeMT2b in Zn tolerance of tobacco and E. coli cells.
    Journal of Plant Research 05/2012; · 2.06 Impact Factor
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    ABSTRACT: Mutation in active site would either completely eliminate enzyme activity or may result in an active site with altered substrate-binding properties. The enzyme xylose isomerase (XI) is sterospecific for the α-pyranose and α-fructofuranose anomers and metal ions (M1 and M2) play a pivotal role in the catalytic action of this enzyme. Mutations were created at the M2 site of XI of Thermus thermophilus by replacing D254 and D256 with arginine. Mutants D254R and a double mutant (D254R/D256R) showed complete loss of activity while D256R showed an increase in the specificity on D-lyxose, L-arabinose and D-mannose which are non-preferential substrates for XI. Both wild type (WT) and D256R showed higher activity at pH 7.0 and 85°C with an increase in metal requirement. The catalytic efficiency Kcat/Km (S(-1) mM(-1)) of D256R for D-lyxose, L-arabinose and D-mannose were 0.17, 0.09 and 0.15 which are higher than WT XI of T.thermophilus. The altered catalytic activity for D256R could be explained by the possible role of arginine in catalytic reaction or the changes in a substrate orientation site. However, both the theories are only assumptions and have to be addressed with crystal study of D256R.
    Protein Engineering Design and Selection 05/2012; 25(7):331-6. · 2.59 Impact Factor
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    ABSTRACT: The endoglucanase (Cel5B) from the filamentous fungus Gloeophyllum trabeum was cloned and expressed without a signal peptide, and alanine residue 22 converted to glutamine in Pichia pastoris GS115. The DNA sequence of Cel5B had an open reading frame of 1,077 bp, encoding a protein of 359 amino acid residues with a molecular weight of 47 kDa. On the basis of sequence similarity, Cel5B displayed active site residues at Glu-175 and Glu-287. Both residues lost full hydrolytic activity when replaced with alanine through point mutation. The purified recombinant Cel5B showed very high specific activity, about 80- to 1,000-fold and 13- to 70-fold in comparison with other endoglucanases and cellobiohydrolase, on carboxymethylcellulose and filter paper, respectively, at pH 3.5 and 55°C. Cel5B displayed bifunctional characteristics under acidic conditions. The kinetic properties of the enzyme determined using a Lineweaver-Burk plot indicated that Cel5B is a catalytically efficient cellulolytic enzyme. These results suggest that Cel5B has high bifunctional endo- and exoglucanase activity under acidic conditions and is a good candidate for bioconversion of lignocellulose.
    Journal of Industrial Microbiology 03/2012; 39(7):1081-9. · 1.80 Impact Factor

Publication Stats

4 Citations
22.01 Total Impact Points

Institutions

  • 2012–2013
    • Chonnam National University
      • Department of Plant Biotechnology
      Gwangju, Gwangju, South Korea
    • Charotar University of Science and Technology
      Aimand, Gujarāt, India