Publications by authors named "Joon-Young Oh"

Article Synopsis
  • * This method successfully produced small and large-sized flexible PSC modules, achieving a power conversion efficiency (PCE) of 16.87%, the highest for R2R two-step processed PSCs.
  • * To tackle issues like hysteresis in efficiency measurements, a dual-annealing process was introduced, leading to improved performance and the production of large-scale flexible modules with a PCE of 11.25%.
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Enzyme immobilization provides substantial advantages in terms of improving the efficiency of enzymatic process as well as enhancing the reusability of enzymes. Phasins (PhaPs) are naturally occurring polyhydroxyalkanoate (PHA)-binding proteins, and thus can potentially be used as a fusion partner for oriented immobilization of enzymes onto PHA supports. However, presently available granular PHA supports have low surface-area-to-volume ratio and limited configurational flexibility of enzymatic reactions.

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Article Synopsis
  • The study aimed to compare the loss of abutment teeth between double crown-retained (DC-RPDs) and clasp-retained removable partial dentures (C-RPDs).
  • A meta-analysis of 38 studies involving 3,393 subjects revealed that both types of dentures had similar rates of abutment loss, with C-RPDs showing a loss of 5-8% and DC-RPDs showing a loss of 6-12%, although C-RPDs did not show a statistically significant difference.
  • The analysis highlighted that follow-up time was a significant predictor of abutment loss, suggesting that longer follow-up could influence outcomes in both DC-RPDs and C-RPDs.
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Objective: To analyze the loss of nonvital abutment teeth compared to vital abutment teeth supporting removable partial dentures (RPDs).

Method And Materials: An electronic search was conducted in the Ovid MEDLINE, Embase, and Web of Science databases, and supplemented by a manual search. The search was done to identify clinical studies reporting the loss of nonvital abutment teeth compared to vital abutment teeth for RPDs.

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  • Bacterial phospholipase A1 (PLA1) is valuable in industries for processing phospholipids and refining plant oils, but it can be toxic to bacterial cells when produced internally.
  • This study successfully addressed the toxicity issue by utilizing a secretion-based production method, which involves the ABC transporter complex from SIK-W1 to release the PLA1 protein outside the bacterial cell.
  • A new bacterial strain, ZYAI, was engineered to control PLA1 expression, allowing for high yields of a functional protein that is effective in the oil degumming process, highlighting its industrial application potential.
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Toxoflavin, a 7-azapteridine phytotoxin produced by the bacterial pathogens such as Burkholderia glumae and Burkholderia gladioli, has been known as one of the key virulence factors in crop diseases. Because the toxoflavin had an antibacterial activity, a metagenomic E. coli clone capable of growing well in the presence of toxoflavin (30 μg/ml) was isolated and the first metagenome-derived toxoflavin-degrading enzyme, TxeA of 140 amino acid residues, was identified from the positive E.

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Background: Phospholipase A1 is an enzyme that hydrolyzes phospholipids at the sn-1 position. It has potential applications across diverse fields including food, pharmaceutical, and biofuel industries. Although there has been increasing interest in the use of phospholipase A1 for degumming of plant oils during biodiesel production, production of recombinant phospholipase A1 has been hampered by low efficiency of gene expression and its toxicity to the host cell.

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  • An ABC transporter named TliDEF from Pseudomonas fluorescens SIK W1 is essential for the secretion of a lipase called TliA, and this secretion process is temperature-sensitive, failing above 33°C.
  • Researchers created a mutant version of the TliDEF protein by introducing random mutations into the tliD gene to find one that could function at 35°C.
  • One successful mutant, which had a single amino acid change (Ser287Pro), displayed significant lipase activity and enhanced TliA secretion capability at multiple temperatures, indicating that a small change in the protein structure can impact the transporter's functionality.
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Photobacterium lipolyticum M37 lipase (LipM37) was immobilized on the surface of intracellular polyhydroxybutyrate (PHB) granules in Escherichia coli. LipM37 was genetically fused to Cupriavidus necator PHA synthase (PhaC Cn ), and the engineered PHB operon containing the lip M37 -phaC Cn successfully mediated the accumulation of PHB granules (85 wt.%) inside E.

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Functional screening for lipolytic enzymes at low temperatures resulted in the isolation of the novel cold-active esterases, EstM-N1 and EstM-N2, from a metagenomic DNA library of arctic soil samples. EstM-N1 and EstM-N2 were 395 and 407 amino acids in length, respectively, and showed the highest similarity to class C β-lactamases. However, they shared a relatively low level of sequence similarity (30%) with each other.

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  • Scientists isolated a carboxylesterase gene (bioHs) from the Serratia sp. SES-01 strain by identifying a clear halo on special agar plates, indicating enzyme activity.
  • The BioHs enzyme was found to be very similar (91% similarity) to a related enzyme from Serratia proteamaculans and was compared with another enzyme (BioHe) from E. coli.
  • Both enzymes showed a preference for breaking down carboxylesterase substrates at low temperatures and alkaline pHs, but BioHe was more resilient to changes in temperature and pH, suggesting their potential for various industrial uses.
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The type I secretion system-dependent lipase, TliA, of Pseudomonas fluorescens was successfully produced in quantity in Serratia marcescens by coexpressing its cognate ABC transporter, TliDEF. Compared with P. fluorescens and Escherichia coli, S.

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