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  1. AU="Jin Cheol Yoo"
  2. AU="Wu, S F"
  3. AU="Onyango, Reagan"
  4. AU="Greene, Joseph Scott"
  5. AU="Kapur, Ibani"
  6. AU="Yunyuan Li"
  7. AU="Li, Qingtian"
  8. AU="Song, An"
  9. AU="Ersin Akinci"
  10. AU="Lale Say"
  11. AU="Nada, Khaled M"
  12. AU="Letesson, Gaetan"
  13. AU="Łukasik, Sylwia"
  14. AU="Van Der Meer, Peter J."
  15. AU="Jojoa Jojoa, Ruby Isabel"
  16. AU="Tan, Qingshan" AU="Tan, Qingshan"
  17. AU="Pennington, R Toby"
  18. AU="Bou Sanayeh, Elie"
  19. AU="Yun, Hwa Young"
  20. AU="C. Maridith Arthur"
  21. AU="Kunze, Ursula"
  22. AU="Adam Bienenstock"
  23. AU="Laviolette, M"
  24. AU="Mama, Khursheed R"
  25. AU="Sachse, Katharina" AU="Sachse, Katharina"
  26. AU="Skrlin, Branimir"
  27. AU="Mathais, Quentin"
  28. AU=Armstrong Ehrin J
  29. AU="Bahadi, Abdelaali"
  30. AU="Qin, Shuhui"
  31. AU="Huaraca-Quispe, Lidia P"
  32. AU=Petrovan Vlad AU=Petrovan Vlad AU=Petrovan Vlad
  33. AU="Elaina M Blair"
  34. AU="Hui Ram Kim"
  35. AU="Litvak, Yael"
  36. AU="Chen, Xiang-Yan"
  37. AU="Honorio Coronado, Eurídice N."
  38. AU="Garny, Hella"
  39. AU="Idris, Zamzuri"
  40. AU="Gao, Xinyu"
  41. AU="Tewari, Srishti"
  42. AU="Behrendt, Ulrike" AU="Behrendt, Ulrike"
  43. AU="Margenthaler, Julie A"
  44. AU="Si, Lian-Jing"
  45. AU="Strand, Torbjørn"
  46. AU=Abdoli Amir

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  1. Artikel ; Online: Biochemical Characterization and Application of a Detergent Stable, Antimicrobial and Antibiofilm Potential Protease from Bacillus siamensis

    Hasan Tarek / Kyung Bin Nam / Young Kyun Kim / Suzia Aktar Suchi / Jin Cheol Yoo

    International Journal of Molecular Sciences, Vol 24, Iss 5774, p

    2023  Band 5774

    Abstract: Proteases are important enzymes that are engaged in a variety of essential physiological functions and have a significant possible use in industrial applications. In this work, we reported the purification and biochemical characterization of a detergent ... ...

    Abstract Proteases are important enzymes that are engaged in a variety of essential physiological functions and have a significant possible use in industrial applications. In this work, we reported the purification and biochemical characterization of a detergent stable, antimicrobial, and antibiofilm potential protease (SH21) produced by Bacillus siamensis CSB55 isolated from Korean fermented vegetable kimchi. SH21 was purified to obtain homogeneity via ammonium sulfate precipitation (40–80%), Sepharose CL-6B, and Sephadex G-75 column. By analyzing the SDS-PAGE and zymogram, it was determined that the molecular weight was around 25 kDa. The enzyme activity was almost completely inhibited in the presence of PMSF and DFP, which indicated that it was a member of the serine protease family. SH21 showed excellent activity with a broad range of pH and temperature, with its maximum pH of 9.0 and temperature of 55 °C. The enzyme had estimated K m and V max values of 0.197 mg/mL and 1.22 × 10 3 U/mg, respectively. In addition, it preserved good activity in the presence of different organic solvents, surfactants, and other reagents. This enzyme showed good antimicrobial activity that was evaluated by MIC against several pathogenic bacteria. Furthermore, it exhibited strong antibiofilm activity as determined by MBIC and MBEC assay and degraded the biofilms, which were analyzed by confocal microscopic study. These properties established that SH21 is a potent alkaline protease that can be used in industrial and therapeutic applications.
    Schlagwörter biochemical characterization ; antimicrobial protease ; antibiofilm ; Bacillus ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Thema/Rubrik (Code) 572
    Sprache Englisch
    Erscheinungsdatum 2023-03-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
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  2. Artikel ; Online: Activation of Nrf2/HO-1 by Peptide YD1 Attenuates Inflammatory Symptoms through Suppression of TLR4/MYyD88/NF-κB Signaling Cascade

    Md Saifur Rahman / Md Badrul Alam / Young Kyun Kim / Mst Hur Madina / Ismail Fliss / Sang Han Lee / Jin Cheol Yoo

    International Journal of Molecular Sciences, Vol 22, Iss 5161, p

    2021  Band 5161

    Abstract: In this study, we investigate the immunomodulatory effects of a novel antimicrobial peptide, YD1, isolated from Kimchi, in both in vitro and in vivo models. We establish that YD1 exerts its anti-inflammatory effects via up-regulation of the Nrf2 pathway, ...

    Abstract In this study, we investigate the immunomodulatory effects of a novel antimicrobial peptide, YD1, isolated from Kimchi, in both in vitro and in vivo models. We establish that YD1 exerts its anti-inflammatory effects via up-regulation of the Nrf2 pathway, resulting in the production of HO-1, which suppresses activation of the NF-κB pathway, including the subsequent proinflammatory cytokines IL-1β, IL-6, and TNF-α. We also found that YD1 robustly suppresses nitric oxide (NO) and prostaglandin E2 (PGE 2 ) production by down-regulating the expression of the upstream genes, iNOS and COX-2, acting as a strong antioxidant. Collectively, YD1 exhibits vigorous anti-inflammatory and antioxidant activity, presenting it as an interesting potential therapeutic agent.
    Schlagwörter anti-inflammation ; YD1 ; peptide drug ; NF-κB ; RAW 264.7 ; TLR-4 ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Sprache Englisch
    Erscheinungsdatum 2021-05-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  3. Artikel: Immobilization of an alkaline endopolygalacturonase purified from Bacillus paralicheniformis exhibits bioscouring of cotton fabrics

    Khan, Md. Maruf / Jin Cheol Yoo / Yoon Seok Choi / Young Kyun Kim

    Bioprocess and biosystems engineering. 2018 Oct., v. 41, no. 10

    2018  

    Abstract: Pectin degrading enzyme has been increasing interest in an industrial application as biocatalysts, such as juice, textile, and wine industry. Bacillus paralicheniformis CBS3, isolated from popular traditional Korean food (kimchi), produced a novel ... ...

    Abstract Pectin degrading enzyme has been increasing interest in an industrial application as biocatalysts, such as juice, textile, and wine industry. Bacillus paralicheniformis CBS3, isolated from popular traditional Korean food (kimchi), produced a novel extracellular thermostable alkaline endopolygalacturonase (BPN3). In this study, BPN3 was purified to 22.04-fold with a recovery yield of 18.93% and specific activity of 2216.41 U/mg by gel filtration and anion exchange column chromatography. The molecular mass of BPN3 was approximately 53 kDa as analyzed by SDS-PAGE and pectic zymography. The N-terminal sequence of BPN3 was AIPVILAX. BPN3 was stable over a broad pH range (8.14–11.47), was thermally stable at 50–60 °C, and functioned optimally in pH 9.1 at 60 °C. BPN3 had Km and Vmax values of 0.039 mg/mL and 747.9 ± 1.2 U mg− 1, respectively, whereas pectin from apple as substrate. BPN3 activity was remarkably affected by metal ions, modulators, and detergents. Digalacturonic acid (GA2) was the major oligosaccharide produced by hydrolysis of BPN3. Immobilized BPN3 was active over a pH range (8.1–11.5), temperature (50–60)°C, and remained stable with 63.34 and 43.41% of its relative activity during second and third cycle, respectively. Desized cotton exhibited highest reducing sugar liberation through optimized conditions of bioscouring. Bioscouring effectiveness of BPN3 was characterized by the comparison of weight loss for purified BPN3 with commercial pectinase and comparison of BPN3 with grey fabric. BPN3 was simple to purify, had high thermal stability, and was stable over a broad pH range that suggests its suitability for bioscouring application as an industrial catalyst.
    Schlagwörter anion exchange ; apples ; Bacillus (bacteria) ; biocatalysts ; bioscouring ; cotton ; cotton fabric ; detergents ; gel chromatography ; hydrolysis ; industrial applications ; kimchi ; metal ions ; molecular weight ; oligosaccharides ; pectins ; pH ; polyacrylamide gel electrophoresis ; polygalacturonase ; reducing sugars ; temperature ; thermal stability
    Sprache Englisch
    Erscheinungsverlauf 2018-10
    Umfang p. 1425-1436.
    Erscheinungsort Springer Berlin Heidelberg
    Dokumenttyp Artikel
    ZDB-ID 1476357-6
    ISSN 1432-0797 ; 1615-7605 ; 1615-7591
    ISSN (online) 1432-0797 ; 1615-7605
    ISSN 1615-7591
    DOI 10.1007/s00449-018-1971-7
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  4. Artikel: Antimicrobial peptide isolated from Bacillus amyloliquefaciens K14 revitalizes its use in combinatorial drug therapy

    Regmi, Sudip / Yun Hee Choi / Yoon Seok Choi / Mi Ri Kim / Jin Cheol Yoo

    Folia microbiologica. 2017 Mar., v. 62, no. 2

    2017  

    Abstract: The present study was performed to evaluate the antibacterial activities of an antimicrobial peptide (CSpK14) and the synergies thereof with β-lactams against vancomycin-resistant Staphylococcus aureus (VRSA) and Enterococci (VRE). Our strain was ... ...

    Abstract The present study was performed to evaluate the antibacterial activities of an antimicrobial peptide (CSpK14) and the synergies thereof with β-lactams against vancomycin-resistant Staphylococcus aureus (VRSA) and Enterococci (VRE). Our strain was isolated from fermented food (kimchi), which is 99.79 % homologous with Bacillus amyloliquefaciens subsp. plantarum FZB42(T). CSpK14 was purified to homogeneity by diammonium sulfate precipitation, concentration, dialysis, and followed by two-stage chromatographic separation, i.e., Sepharose Cl-6B and Sephadex G-25 chromatography, and had a molar mass of ~4.6 kDa via Tricine SDS-PAGE and in situ examination. It was stable at pH 6.0–11.5 and temperature up to 80 °C. In addition, it was also stable with various metal ions, solvents, and proteases. The N-terminal amino acid sequence was H-Y-D-P-G-D-D-S-G-N-T-G and did not show any significant homology with reported peptides. However, it shows some degrees of identity with alpha-2-macroglobulin and ligand-gated channel protein from different microorganisms. CSpK14 significantly reduced the minimum inhibitory concentrations (MICs) of β-lactams and had no effect on non-β-lactams against VRSA and VRE. MICs of CSpK14/oxacillin and CSpK14/ampicillin were reduced by 8- to 64-fold and 2- to 16-fold, respectively. The time killing assay between CSpK14/oxacillin (2.29–2.37 Δlog₁₀CFU/mL at 24 h) and CSpK14/ampicillin (2.30–2.38 Δlog₁₀CFU/mL at 24 h) being >2-fold and fractional inhibitory concentration index ˂0.5 revealed synergy. Furthermore, the biofilms formed by VRSA and VRE were reduced completely. CSpK14 was simple to purify, had low molecular mass, was stable over a wide pH range or tested chemicals, had broad inhibitory spectrum, and possessed potent synergistic antimicrobial-antibiofilm properties. CSpK14 synergistically enhanced the efficacy of β-lactams and is therefore suitable for combination therapy.
    Schlagwörter Bacillus amyloliquefaciens ; Enterococcus ; Staphylococcus aureus ; agarose ; amino acid sequences ; antibacterial properties ; antimicrobial peptides ; beta-lactams ; biofilm ; chromatography ; dialysis ; drug therapy ; kimchi ; metal ions ; microorganisms ; minimum inhibitory concentration ; molecular weight ; pH ; polyacrylamide gel electrophoresis ; proteinases ; solvents ; sulfates ; temperature
    Sprache Englisch
    Erscheinungsverlauf 2017-03
    Umfang p. 127-138.
    Erscheinungsort Springer Netherlands
    Dokumenttyp Artikel
    ZDB-ID 240503-9
    ISSN 1874-9356 ; 0015-5632
    ISSN (online) 1874-9356
    ISSN 0015-5632
    DOI 10.1007/s12223-016-0479-2
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  5. Artikel ; Online: Response Surface Optimization of Culture Conditions for Cyclic Lipopeptide MS07 from Bacillus siamensis Reveals Diverse Insights Targeting Antimicrobial and Antibiofilm Activity

    Md Maruf Khan / Young Kyun Kim / SeungSik Cho / Ying-Yu Jin / Joo-Won Suh / Dae Young Lee / Jin Cheol Yoo

    Processes, Vol 8, Iss 744, p

    2020  Band 744

    Abstract: Efforts to isolate a broad-spectrum antimicrobial peptide (AMP) from microbial sources have been on the rise recently. Here, we report the identification, the optimization of the culture conditions, and the characterization of an efficient AMP from the ... ...

    Abstract Efforts to isolate a broad-spectrum antimicrobial peptide (AMP) from microbial sources have been on the rise recently. Here, we report the identification, the optimization of the culture conditions, and the characterization of an efficient AMP from the Bacillus strain designated MS07 that exhibits antimicrobial and antibiofilm activity. The production of MS07 was maximized by evaluating the culture conditions by the response surface methodology to obtain optimum media compositions. The biochemical integrity of MS07 was assessed by a bioassay indicating inhibition at ~6 kDa, like tricine-SDS-PAGE. MALDI-TOF confirmed the molecular weight and purity, showing a molecular mass of 6.099 kDa. Peptide MS07 exhibited antimicrobial activity against both Gram-positive and Gram-negative bacteria. The MIC of MS07 for Escherichia coli , Alcaligenes faecalis , MRSA , and Pseudomonas aeruginosa ranged from 16–32 µg/mL, demonstrating superior potency. The biomass was diminished by about 15% and 11%, with rising concentrations up to 8 × MIC, for P. aeruginosa and E. coli biofilm, respectively. MS07 exhibited an 8 µM and 6 µM minimum bactericidal concentration against the biofilm of the Gram-negative strains P. aeruginosa and E. coli , respectively . Peptide MS07 reduced and interrupted the biofilm development in a concentration-dependent manner, as determined by BacLight live/dead staining using confocal microscopy.
    Schlagwörter antimicrobial peptide ; cyclic lipopeptide ; antibiofilm ; killing kinetics ; response surface methodology ; Chemical technology ; TP1-1185 ; Chemistry ; QD1-999
    Thema/Rubrik (Code) 571
    Sprache Englisch
    Erscheinungsdatum 2020-06-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  6. Artikel: Selective determination of dopamine with an amperometric biosensor using electrochemically pretreated and activated carbon/tyrosinase/Nafion®-modified glassy carbon electrode

    Rahman, Siti Fauziyah / Kyoungseon Min / Seok-Hwan Park / Jae-Hee Park / Jin Cheol Yoo / Don-Hee Park

    Biotechnology and bioprocess engineering. 2016 Sept., v. 21, no. 5

    2016  

    Abstract: Dopamine, the most important neurotransmitter in the human brain, controls various functions. Dopamine deficiency causes fatal neurological disorders such as Parkinson’s disease. Even though various types of electrochemical sensors have been studied to ...

    Abstract Dopamine, the most important neurotransmitter in the human brain, controls various functions. Dopamine deficiency causes fatal neurological disorders such as Parkinson’s disease. Even though various types of electrochemical sensors have been studied to measure dopamine levels, they often have poor selectivity for dopamine due to co-existence of interfering substances (e.g. ascorbic acid). Herein, we aimed to develop a highly sensitive dopamine detection method in the co-existence of ascorbic acid, a major interfering substance in real sample by designing an electrochemically pretreated and activated carbon/tyrosinase/Nafion®-modified GCE as an amperometric dopamine biosensor. To maximize the biosensor performance, pH, volume of Nafion®, and scan rate were optimized. This electrochemically pretreated and activated carbon/tyrosinase/ Nafion®-modified GCE could detect as low as 50 μM of dopamine with a wide linear range (50 ~ 1,000 μM) within a few seconds. In addition, it had a sensitivity of 103mAM/cm², which was higher than all previously reported tyrosinasebased dopamine biosensors. In addition, interference effect caused by 4 mM of ascorbic acid was negligible in the co-existence of 1 mM of dopamine. Consequently, this electrochemically pretreated and activated carbon/tyrosinase/ Nafion®-modified GCE might be applicable as amperometric biosensor for selective detection of dopamine in real samples with interfering substances.
    Schlagwörter Parkinson disease ; activated carbon ; ascorbic acid ; biosensors ; brain ; dopamine ; electrochemistry ; glassy carbon electrode ; humans ; neurotransmitters ; pH
    Sprache Englisch
    Erscheinungsverlauf 2016-09
    Umfang p. 627-633.
    Erscheinungsort The Korean Society for Biotechnology and Bioengineering
    Dokumenttyp Artikel
    ZDB-ID 2125481-3
    ISSN 1976-3816 ; 1226-8372
    ISSN (online) 1976-3816
    ISSN 1226-8372
    DOI 10.1007/s12257-016-0382-3
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  7. Artikel: A novel antioxidant peptide, purified from Bacillus amyloliquefaciens, showed strong antioxidant potential via Nrf-2 mediated heme oxygenase-1 expression

    Saifur Rahman, Md / Jin Cheol Yoo / Md. Badrul Alam / Sang Han Lee / Yoon Seok Choi / Yun Hee Choi

    Food chemistry. 2017,

    2017  

    Abstract: A novel antioxidant peptide YD1 (∼1.0 kDa), purified from the strain Bacillus amyloliquefaciens CBSYD1, displayed activity in several in vitro assays and was also efficient against Gram-positive, Gram-negative as well as multidrug-resistant (MDR) ... ...

    Abstract A novel antioxidant peptide YD1 (∼1.0 kDa), purified from the strain Bacillus amyloliquefaciens CBSYD1, displayed activity in several in vitro assays and was also efficient against Gram-positive, Gram-negative as well as multidrug-resistant (MDR) bacteria. Strain growth was adapted to bile-salt conditions where a clear halos-zone was observed in a bile-salt plate assay and was viable in different digestive track conditions. YD1 treatment on RAW 264.7 cells increased the transcriptional and translational activities of NF-E2-related factor-2 (Nrf-2) through the enhanced levels of heme oxygenase-1 (HO-1). Furthermore, the YD1-treated group showed higher levels of antioxidant enzymes compared to the oxidative stress group. YD1 demonstrated a strong antioxidant activity by decreasing nitric oxide (NO) and reactive oxygen species (ROS) in RAW 264.7 cells. This study suggests that YD1 and the strain could be a natural antioxidant and a probiotic candidate respectively.
    Schlagwörter antioxidant activity ; Bacillus amyloliquefaciens ; bacteria ; heme oxygenase (biliverdin-producing) ; in vitro studies ; multiple drug resistance ; nitric oxide ; oxidative stress ; probiotics ; reactive oxygen species ; transcription (genetics) ; translation (genetics)
    Sprache Englisch
    Umfang p. .
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    Anmerkung Pre-press version
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2017.06.106
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  8. Artikel ; Online: Anti-inflammatory effect of Allium hookeri on carrageenan-induced air pouch mouse model.

    Jung-Eun Kim / Kyung-Mok Park / Soon-Young Lee / Ji-Hye Seo / In-Soo Yoon / Chun-Sik Bae / Jin-Cheol Yoo / Mi-Ae Bang / Seung-Sik Cho / Dae-Hun Park

    PLoS ONE, Vol 12, Iss 12, p e

    2017  Band 0190305

    Abstract: Inflammation is a commonly observed immune reaction, and rheumatoid arthritis is a particularly severe inflammatory disease. In this study, we used an air pouch mouse model to evaluate the anti-inflammatory potential of Allium hookeri, which has both ... ...

    Abstract Inflammation is a commonly observed immune reaction, and rheumatoid arthritis is a particularly severe inflammatory disease. In this study, we used an air pouch mouse model to evaluate the anti-inflammatory potential of Allium hookeri, which has both been used as a culinary material and a traditional medicine in south-eastern Asia for many years. Allium hookeri suppressed typical symptoms of inflammation, such as condensation of the air pouch membrane, and inhibited the expression of several inducible proinflammatory cytokines such as IL-1β, IL-6, IL-13, and TNF-α. In order to determine the molecules modulating the inflammatory effect of carrageenan treatment, the components in Allium hookeri were analyzed by GC-MS, and linoleic acid, which have anti-inflammatory effect, was detected. From the results, we concluded that the anti-inflammatory effect of Allium hookeri might be attributed to linoleic acid, which could be promising candidates for anti-inflammatory drugs that have no adverse effects.
    Schlagwörter Medicine ; R ; Science ; Q
    Thema/Rubrik (Code) 616
    Sprache Englisch
    Erscheinungsdatum 2017-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
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  9. Artikel ; Online: A novel multifunctional peptide oligomer of bacitracin with possible bioindustrial and therapeutic applications from a Korean food-source Bacillus strain.

    Yun Hee Choi / Seung Sik Cho / Jaya Ram Simkhada / Md Saifur Rahman / Yoon Seok Choi / Chun Sung Kim / Jin Cheol Yoo

    PLoS ONE, Vol 12, Iss 5, p e

    2017  Band 0176971

    Abstract: CSP32 has stable characteristics and may find bio-industrial and therapeutic applications. ...

    Abstract CSP32 has stable characteristics and may find bio-industrial and therapeutic applications.
    Schlagwörter Medicine ; R ; Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2017-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
    Dokumenttyp Artikel ; Online
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  10. Artikel: Purification and characterization of chitinase showing antifungal and biodegradation properties obtained from Streptomyces anulatus CS242

    Mander, Poonam / Seung Sik Cho / Yun Hee Choi / Sandesh Panthi / Yoon Seok Choi / Hwan Mook Kim / Jin Cheol Yoo

    Archives of pharmacal research. 2016 July, v. 39, no. 7

    2016  

    Abstract: In an effort to identify a microbial enzyme that can be useful as a fungicide and biodegradation agent of chitinous wastes, a chitinase (Chi242) was purified from the culture supernatant of Streptomyces anulatus CS242 utilizing powder of shrimp shell ... ...

    Abstract In an effort to identify a microbial enzyme that can be useful as a fungicide and biodegradation agent of chitinous wastes, a chitinase (Chi242) was purified from the culture supernatant of Streptomyces anulatus CS242 utilizing powder of shrimp shell wastes as a sole carbon source. It was purified employing ammonium sulfate precipitation and gel permeation chromatography techniques. The molecular weight of the purified chitinase was
    Schlagwörter Streptomyces anulatus ; amino acid sequences ; ammonium sulfate ; antifungal properties ; biodegradation ; biological control agents ; biotransformation ; carbon ; chitin ; chitinase ; fungi ; fungicides ; gel chromatography ; glucosamine ; molecular weight ; pH ; pathogens ; polyacrylamide gel electrophoresis ; scanning electron microscopy ; shrimp ; thermal stability ; wastes
    Sprache Englisch
    Erscheinungsverlauf 2016-07
    Umfang p. 878-886.
    Erscheinungsort Pharmaceutical Society of Korea
    Dokumenttyp Artikel
    ZDB-ID 447623-2
    ISSN 1976-3786 ; 0253-6269
    ISSN (online) 1976-3786
    ISSN 0253-6269
    DOI 10.1007/s12272-016-0747-3
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