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Jatuporn Phaopongthai,Suthep Wiyakrutta,Duangdeun Meksuriyen,Nongluksna Sriubolmas,Khanit Suwanborirux 한국미생물학회 2013 The journal of microbiology Vol.51 No.6
In this study, a tropical endophytic fungus, Alternaria alternata Tche-153 was isolated from a Thai medicinal plant Terminalia chebula Rezt. The ethyl acetate extract prepared from the fermentation broth exhibited significant ketoconazole-synergistic activity against Candida albicans. Bioassaydirected fractionation of the ethyl acetate extract led to the isolation of altenusin (1), isoochracinic acid (2), and altenuic acid (3) together with 2,5-dimethyl-7-hydroxychromone (4). Using the disc diffusion method and the microdilution chequerboard technique, only altenusin (1) in combination with each of three azole drugs, ketoconazole, fluconazole or itraconazole at their low sub-inhibitory concentrations exhibited potent synergistic activity against C. albicans with the fractional inhibitory concentration index range of 0.078 to 0.188. This first discovery of altenusin (1) as a new azole-synergistic prototype possessing a biphenyl structure is of significance for further development of new azole-synergists to treat invasive candidiasis.
Maneekarn Chinworrungsee,Suthep Wiyakrutta,Nongluksna Sriubolmas,Phitaya Chuailua,Apichart Suksamrarn 대한약학회 2008 Archives of Pharmacal Research Vol.31 No.5
Bioassay-guided fractionation of the extract of the endophytic fungus KLAR 5 belonging to order Hypocreales, which was isolated from the twig of Knema laurina (Blume) Warb., resulted in the isolation of brefeldin A (1), 8-deoxy-trichothecin (2), trichothecolone (3), 7α-hydroxytrichodermol (4), and 7α-hydroxyscirpene (5). Compound 5 was isolated from natural source for the first time. Compound 1 was very highly active against human epidermoid carcinoma of the mouth, human breast cancer (BC-1), and human small cell lung cancer (NCI-H187) cells whereas compounds 2 and 4 were selectively active against BC-1 and NCI-H187 cells. Compounds 3 and 5 were moderately active against these three cancer cell lines.
Pijug Summpunn,Suttidarak Chaijan,Duangnate Isarangkul,Suthep Wiyakrutta,Vithaya Meevootisom 한국미생물학회 2011 The journal of microbiology Vol.49 No.1
Bacillus subtilis BCC41051 producing a thermostable β-mannanase was isolated from soybean meal-enriched soil and was unexpectedly found to be thermophilic in nature. The extracellular β-mannanase (ManA) produced was hydrophilic, as it was not precipitated even with ammonium sulfate at 80% saturation. The estimated molecular weight of ManA was 38.0 kDa by SDS-PAGE with a pI value of 5.3. Optimal pH and temperature for mannan-hydrolyzing activity was 7.0 and 60°C, respectively. The enzyme was stable over a pH range of 5.0-11.5, and at temperatures of up to 60°C for 30 min, with more than 80% of its activity retained. ManA was strongly inhibited by Hg^(2+) (1 mM), but was sensitive to other divalent ions to a lesser degree. The gene of ManA encoded a protein of 362 amino acid residues, with the first 26 residues identified as a signal peptide. High expression of recombinant ManA was achieved in both Escherichia coli BL21 (DE3)(415.18 U/ml) and B. megaterium UNcat (359 U/ml).
Effect of the Derivatives of Andrographolide on the Morphology of Bacillus subtilis
Chantana Aromdee,Nongluksna Sriubolmas,Suthep Wiyakrutta,Supawadee Suebsasna,Watcharee Khunkitti 대한약학회 2011 Archives of Pharmacal Research Vol.34 No.1
Andrographis paniculata has been reported to have antiviral, antipyretic and anticancer activities. Andrographolide, an ent-labdane diterpene, is an active constituent in this plant. In this study, andrographolide (1) and its natural derivative 14-deoxy-11,12-didehydroandrographolide (2) and 5 other semisynthetic derivatives were tested for their activity against Grampositive and Gram-negative bacteria and Candida albicans. Only derivatives bearing a 14-acetyl group showed activity, and this activity was only against Gram-positive bacteria. 14-Acetylandrographolide showed the highest potency against Bacillus subtilis; the other 14-acetylandrographolides with additional substitution at the 3- and 19-hydroxyl groups showed lower activity against Gram-positive bacteria. The morphology of B. subtilis after being treated with 14-acetylandrographolide was investigated with TEM. This is the first report on 14-acetylandrographolide’s quantified antibacterial activity, and the crucial functional group of this ent-labdane that plays an important role in perturbing the morphogenesis of B. subtilis leading to cell death.
A Thermostable Phytase from Neosartorya spinosa BCC 41923 and Its Expression in Pichia pastoris
Patcharaporn Pandee,Pijug Summpunn,Suthep Wiyakrutta,Duangnate Isarangkul,Vithaya Meevootisom 한국미생물학회 2011 The journal of microbiology Vol.49 No.2
A phytase gene was cloned from Neosartorya spinosa BCC 41923. The gene was 1,455 bp in size, and the mature protein contained a polypeptide of 439 amino acids. The deduced amino acid sequence contains the consensus motif (RHGXRXP) which is conserved among phytases and acid phosphatases. Five possible disulfide bonds and seven potential N-glycosylation sites have been predicted. The gene was expressed in Pichia pastoris KM71 as an extracellular enzyme. The purified enzyme had specific activity of 30.95 U/mg at 37°C and 38.62 U/mg at 42°C. Molecular weight of the deglycosylated recombinant phytase, determined by SDS-PAGE, was approximately 52 kDa. The optimum pH and temperature for activity were pH 5.5and 50°C. The residual phytase activity remained over 80% of initial activity after the enzyme was stored in pH 3.0 to 7.0 for 1 h, and at 60% of initial activity after heating at 90°C for 20 min. The enzyme exhibited broad substrate specificity, with phytic acid as the most preferred substrate. Its Km and Vmax for sodium phytate were 1.39 mM and 434.78 U/mg, respectively. The enzyme was highly resistant to most metal ions tested, including Fe^(2+), Fe^(3+), and Al^(3+). When incubated with pepsin at a pepsin/phytase ratio of 0.02 (U/U) at 37°C for 2 h, 92% of its initial activity was retained. However, the enzyme was very sensitive to trypsin, as 5% of its initial activity was recovered after treating with trypsin at a trypsin/phytase ratio of 0.01 (U/U).
( Hossein Javid ),( Juntratip Jomrit ),( Aiya Chantarasiri ),( Duangnate Isarangkul ),( Vithaya Meevootisom ),( Suthep Wiyakrutta ) 한국미생물 · 생명공학회 2014 Journal of microbiology and biotechnology Vol.24 No.5
D-Phenylglycine aminotransferase (D-PhgAT) from Pseudomonas stutzeri ST-201 is useful for enzymatic synthesis of enantiomerically pure D-phenylglycine. However, its low protein solubility prevents its application at high substrate concentration. With an aim to increase the protein solubility, the N-terminus of D-PhgAT was genetically fused with short peptides (A1 α-helix, A2 α-helix, and ALAL, which is a hybrid of A1 and A2) from a ferredoxin enzyme of a halophilic archaeon, Halobacterium salinarum. The fused enzymes A1-D-PhgAT, A2-D-PhgAT, and ALAL-D-PhgAT displayed a reduced pI and increased in solubility by 6.1-, 5.3-, and 8.1- fold in TEMP (pH 7.6) storage, respectively, and 5-, 4.5-, and 5.9-fold in CAPSO (pH 9.5) reaction buffers, respectively, compared with the wild-type enzyme (WT-D-PhgAT). In addition, all the fused D-PhgAT displayed higher enzymatic reaction rates than the WT-DPhgAT at all concentrations of L-glutamate monosodium salt used. The highest rate, 23.82 ± 1.47 mM/h, was that obtained from having ALAL-D-PhgAT reacted with 1,500 mM of the substrate. Moreover, the halophilic fusion significantly increased the tolerance of D-PhgAT in the presence of NaCl and KCl, being slightly in favor of KCl, where under the same condition at 3.5 M NaCl or KCl all halophilic-fused variants showed higher activity than WT-D-PhgAT.