• 대한수의학회지
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• 제49권2호
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• pp.135-139
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• 2009

Streptomyces (S.) fradiae is a microbe with broad-spectrum antimicrobial activity, isolated from soil. In the present study, antibacterial effects of S. fradiaea against Salmonella (S.) gallinarum was determined. S. fradiae inhibited growing of S. gallinarum in Luria-Bertani media agar. Moreover, ingestion of S. fradiae markedly inhibited mortality of chickens experimentally infected with S. gallinarum. There is no side effect by S. fradiaeon, in safety of chickens and antibiotic material residues in chicken meat. Taken together, S. fradiae have the antibacterial effects against S. gallinarum. Therefore, we concluded that S. fradiae might be a good microbial candidate for treatment or control of fowl typhoid in chickens.

• 미생물학회지
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• 제28권1호
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• pp.65-70
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• 1990

방선균의 세포분화와 관련된 연구의 일환으로 Streptomyces fradiae NRRL2702가 생성하는 단백질분해효소 저해물질을 분리정제하여 그 특성을 분석하였다. 즉 S. fradiaesm s일반 환경 조건하에서 단백질분해효소를 생성하나 특정 조건하에서는 그 단백질의 활성을 저해하는 저해제를 생성함을 알았다. 이 저해제의 분자량은 16,800이며 serine proteinasem이 일부만을 저해하는 특징이 있었다. Pronase E의 활성의 저해양상은 competitive inhibition 이었고 열에 대하여 매우 안정함을 알았다.

• 한국미생물·생명공학회지
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• 제23권6호
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• pp.647-651
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• 1995

A tylosin-hyperproductive mutant of S. fradiae MNU20 was isolated among 3500 strains obtaincd from either MNNG- or UV-treated Streptomyces fradiae NRRL2702. The composition of optimal medium for tylosin production was formulated as followed as: 4 g soluble starch, 1 g glucose, 1 g corn steep liquor, 7.5 ml soy bean oil, 0.2 g KH$_{2}$PO$_{4}$, 1 g Na$_{2}$S$_{2}$O$_{3}$$\cdot $5H$_{2}$O, 2 g CaCO$_{3}$, 2 g NaCl, 0.001 g CoCl$_{2}$$\cdot $6H$_{2}$O in 1 liter of distilled water. With the optimal medium, S. fradiae MNU20 was able to produce 159 mg tylosin (g biomass)$^{-1}$, indicating that tylosin productivity of Streptomyces fradiae NRRL2702 was increased 14 times higher by mutation. When the effect of valine, succinate, and natural zeolite on tylosin production was investigated by using the optimal medium, these substances essentially enhanced tylosin production and their addition time during culture period appeared to be critical for the increase of tylosin production.

• Archives of Pharmacal Research
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• 제15권1호
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• pp.41-47
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• 1992

In order to obtain acetaminophen, a popular analgesic-antipyretic, though microbial p-hydroxylation and N-acetylation of aniline, various Streptomyces strains were screened. Aniline N-acetylation activity was rather ubiquitous but-hydroxylation activity was selective. Microbial conversion pathway of aniline to acetaminophen was considered to be through N-acetylation and p-hydroxylation or vice versa. However, depending on species used, o-hydroxylation and its degradation activity (S. fradiae) and acetaminophen degradation activity (S. coelicolar) were also detected. Among the screened Streptomyces strains, S fradiae NRRL 2702 showed the highest acetanilide p-hydroxylation activity (203% conversion rate). Furthermore, in S. fradiae carbon source and its concentration, phosphate ion concentration and pH of growth medium were found to play the crucial roles in p-hydroxylation activity. Through the proper combination of factors mentioned above, the ten times more activity (26-30% conversion rate) was attained.

• Molecules and Cells
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• 제27권1호
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• pp.83-88
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• 2009

Amino acid homology analysis predicted that rbmD, a putative glycosyltransferase from Streptomyces ribosidificus ATCC 21294, has the highest homology with neoD in neomycin biosynthesis. S. fradiae BS1, in which the production of neomycin was abolished, was generated by disruption of the neoD gene in the neomycin producer S. fradiae. The restoration of neomycin by self complementation suggested that there was no polar effect in the mutant. In addition, S. fradiae BS6 was created with complementation by rbmD in S. fradiae BS1, and secondary metabolite analysis by ESI/MS, LC/MS and MS/MS showed the restoration of neomycin production in S. fradiae BS6. These gene inactivation and complementation studies suggested that, like neoD, rbmD functions as a 2-N-acetlyglucosaminyltransferase and demonstrated the potential for the generation of novel aminoglycoside antibiotics using glycosyltransferases in vivo.

• 미생물학회지
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• 제31권3호
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• pp.237-244
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• 1993

Aspartate aminotransferase (ASAT) (L-aspartate : 2-oxyoglutarate, EC 2.6. 1. 1.) from Streptomyces fradiae NRRL 2702 has been purified by acetone precipitation, DEAE-cellulose, hydroxyapatite, and preparative electrophoresis (Prep cell), of which the last was the most effective step in the purification of ASAT. The molecular mass was estimated to be 54,000 dalton by SDS-PAGE and 120,000 dalton by gel filtration chromatography. Preparative isoelectric focusing of purified ASAT resulted in one polypeptide band with a pI of 4.2, showing homogeneity and indicating that the enzyme is composed of two identical subunits. The enzyme was specific for L-aspartate as an amino donor ; the $K_{m}$ values were determined to be 2.7 mM for L-aspartate, 0.7 mM for 2-oxoglutarate, 12.8 mM for L-glutamate, and 0.15 mM for oxaloacetate. The enzyme was relatively heat-stable, having maximum activity at 55.deg.C, and it had a broad pH optimum ranging from 5.5 to 8.0. The activity of the purified enzyme was not inhibited by ammonium ions. This paper reports the first purification and characterization of the aspartate aminotransferase from a species of Streptomyces.s.

• Journal of Microbiology and Biotechnology
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• 제5권5호
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• pp.305-308
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• 1995

From the plasmid library made from Sstl and San-digested genomic DNA of Streptomyces fradiae NRRL 2702, four positive clones were selected using an oligodeoxynucleotide probe from the N-terminal amino acid sequence of purified threonine dehydratase. The cloned gene for threonine dehydratase was a 2.0 kilo-base pair DNA fragment. The deduced amino acid sequence of PCR product (PCR245) was matched to that of the N-terminal part of threonine dehydratase from S. fradiae and this showed a high similarity to the threonine dehydratases of other organisms. This indicated that amino acid sequences of threonine dehydratases were highly conserved and the polypeptide product of the PCR245 was likely to be involved in the deamination of threonine.

• 미생물학회지
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• 제25권3호
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• pp.189-197
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• 1987

배지성분으로 첨가된 glutamate의 농도가 균의성장고 tylosin 생합성에 미치는 영향을 조사하였다. 그 결과 oxaloacetate를 공동기질로 사용하는 효소의 활성에 의하여 균의 성장과 tylosin의 생합성이 조절됨을 알았다. 즉, citrate synthase와 aspartate aminotransferase의 활성은 균의 성장에 아주 긴요하며 methylmalonyl-CoA carboxytransferase의 활성은 tylosin 생합성에 아주 중요한 효소임을 알았다. Glutamate의 농도는 우의 효소의 활성에 직접적으로 영향을 주고 있음을 알았다.

• 미생물학회지
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• 제28권3호
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• pp.264-267
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• 1990

The objectives of the current studies were to establish the optimal conditions for the production of extracellular protease inhibitor in a strain of Streptomyces fradiae. As results, it was found that cell specific growth rate was very critical for the production of protease inhibitor and the optimum specific growth rate was found to be 0.05 h$^{-1}$ . Dissolved oxygen tension and pH were also important to regulate the inhibitor production. The inhibitory mode of the purified inhibitor to .alpha.-chymotrypsin was found to be competitive (K$_{i}$=5.5*10$^{-7}$ M). One mole of inhibitor could bind two moles of .alpha.-chymotrypsin and the complex has very low dissociation constant.t.

• Journal of Microbiology
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• 제33권2호
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• pp.103-108
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• 1995

Streptomyces fradiae protease inhibitor (SFI) was purified effectively by preparative isoelectric focusing and hydroxyapatite chromatography. The molecular weight of SFI was estimated to be 1.7 kDa by SDS-PAGE and 1.8 kDa by molecular sieving HPLC. One hundred and sixty amino acid residues were determined from which molecular weight of SFI was calculated to be 17.054 Da and carbohydrate residue was not detected. SFI was calculated to be 17,064 Da and carbohydrate residue was not detected. SFI was a monomeric protein with two reactive sits, of which isoelectric point was pH 4.1. N-terminal amino acid sequence of SFI had homology with SSI (Streptomyces subsilisin inhibitor) and other protease inhibitors produced by Streptomyces.