• Microbiology and Biotechnology Letters
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• v.10 no.4
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• pp.237-243
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• 1982

A microorganism, YS-40 strain which powerfully produced penicillinase was isolated from soil. The morphological and cultural characteristics of the strain ; spore chain, spore surface, aerial mass color, melanoid pigment, reverse side pigment, other soluble pigment, and physiological properties were investigated. As the results of various examinations, the strain YS-40 was identified to be similar to Streptemyces bobili except the spore chain and the utilization of L-rhamnose among the various carbon sources.

• Korean Journal of Veterinary Research
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• v.24 no.2
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• pp.163-168
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• 1984

The in vitro activity of penicillins(penicillin G, ampicillin, carbenicillin, methicillin and cloxacillin) and gentamicin to Staphylococcus aureus and coagulase-negative staphylococci isolated from bovine mastitic milk samples was determined. The growth of all isolates of staphylococci tested was inhibited by cloxacillin and methicillin at a concentration of $0.78{\mu}g/ml$ and by gentamicin at a minimum inhibitory concentration (MIC) of $1.56{\mu}g/ml$. Of the 140 strains of Staphylococcus aureus isolated 99(70.7%) gave positive reactions for penicillinase on the starch-iodine test. Of 121 isolates of coagulase-negative staphylococci, 58(47.9%) showed penicillinase production, but all the Staph. xylosus lacked the ability to produce penicillinase. MIC of penicillin G of the penicillinase-positive strains was $0.2{\mu}g/ml$ or more. The combination of cloxacillin with gentamicin showed a synergistic effect by inhibiting regrowth of the tested organism.

• Microbiology and Biotechnology Letters
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• v.10 no.3
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• pp.185-190
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• 1982

A strain of Streptomyces sp. (YS-40) which was able to produce penicillinase, was isolated from soil and the enzymatic characteristics of this enzyme were investigated. The crude enzyme was obtained with the fractionation by 80 % cold acetone. The optimal temperature and pH of this enzyme was 45$^{\circ}C$ and 5.0 respectively. The stable pH range of the enzyme was between pH 5.5 and 8.0 at 37$^{\circ}C$. By heat treatment at 6$0^{\circ}C$ and 8$0^{\circ}C$ for 10 min, the remained relative activities were about 50%, 30% respectively. The activity of the enzyme was inhibited by Cu$^{＋＋}$, $_Mn^{＋＋}$, Zn$^{＋＋}$ but Co$^{＋＋}$, Li$^{＋＋}$, $Ca^{＋＋}$, $Mg^{＋＋}$ $Ba^{＋＋}$ did not affect. Among 11 chemical reagents, ethylenedi aminetetra-acetic acid disodium salt (EDTA-2Na), sodium dodecyl sulfate (SDS) and sodium fluoride inhibited the enzyme activity.

• Microbiology and Biotechnology Letters
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• v.10 no.3
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• pp.177-184
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• 1982

Studies were carried out to investigate the optimal culture conditions for the production of penicillinase using a strain of Streptomyces sp. isolated from soil, YS-40. Among the carbon and nitrogen sources, glucose and L-asparagine increased the peniciilinase production. The addition of M $n^{＋＋}$, $Ca^{＋＋}$ and L $i^{＋}$ increased the enzyme production, but depressed by F $e^{＋＋＋}$, F $e^{＋＋}$, $Mg^{＋＋}$, Z $n^{＋＋}$, A $g^{＋＋}$, $Ba^{＋＋}$ and S $n^{＋＋}$. L-Leucine slightly increased the enzyme production but L-histidine, L-methionine depressed. Among the vitamins riboflavine, i-inositol, hesperidine, niacin-amide, biotin, folic acid, DL-$\alpha$-lipoic acid increased the enzyme formation. The addition of cephradine, cephalexin, ampicillin, cloxacillin more increased the enzyme formation than that of other$\beta$-lactam antibiotics and antibiotics. Optimal pH and temperature on the enzyme formation was pH 7.0 and 28$^{\circ}C$ respectively Amount of the enzyme production reached at maximum with incubation for 3 days on the optimal condition.

• Archives of Pharmacal Research
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• v.20 no.1
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• pp.68-71
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• 1997

Penicillin sensor was prepared by immobilizing penicillinase (Pcase) on $H^{+}$-selective carboxylated poly (vinyl chloride) (PVC-COOH) membrane or cellulose filter membrane. The immobilization techniques are as follows. Pcase was immobilized with GTH on $H^{+}$-selective PVC-COOH membrane or some amount of BSA was dropped on that membrane. Another method to make immobilization is to mix type I Pcase with GTH and drop on a cellulose filter membrane. According to immobilization techniques, there were some differences in response properties of enzyme electrodes, however, all electrodes responded to Pcase-resistant penicillin derivatives. Pcase immobilized on cellulose filter membrane with $H^{+}$-selective PVC membrane eletrode was more stable and more sensitive to penicillinase-resistant penicillin derivatives than any other immobilization techniques.

• YAKHAK HOEJI
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• v.28 no.2
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• pp.89-95
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• 1984

Microorganisms having beta-latamase inhibitory activity were selected from soil samples collected from 63 spots throughout the country. Screening procedures consist of two steps. Those are growth inhibition test of penicillinase-producing Staphylococcus aureus by double-layered agar plate containing penicillin G as a substrate, and that of penicillin sensitive Staphylococcus aureus ATCC 6538 in the similiar condition including penicillinase. Finally, a strain was selected from a soil sample of Pa-ju, Kyeong-gi Do. This strain was classified as a Streptomyces sp. by ISP(International Streptomycete Project) and Bergey's manual.

• Microbiology and Biotechnology Letters
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• v.7 no.3
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• pp.135-140
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• 1979

A Streptomyces sp. strain AS-727 which was capable of producing penicillinase, was isolated from soil. The enzyme production was affected by the carbon and nitrogen sources added. Among them so far tested, glucose (or maltose) and sodium nitrate increased the enzyme production. And the amount of enzyme prodced reached maximum in 4 days cultivation. The optimla pH and temperature of the penicillinase was between pH 6.0 to 8.0 and 4$0^{\circ}C$ respectively. The stabel pH range of the enzyme was stable at 4$0^{\circ}C$, but it lost about 30％ and 40％ of the the activity respectively when it was treated at 6$0^{\circ}C$ and 8$0^{\circ}C$ for 60 minutes. The activity of the enzyme was inhibited by Z $n^{++}$, but A $g^{+}$, $Co^{++}$, $_Mn^{++}$, $Ca^{++}$, P $b^{++}$ did not affected enzyme activity. Peculiarly, the enzyme protein precipitated by freezing or addition of ammonium sulfate, urea, sodium chloride and some organic solvents as etanol, methanol, acetone was not dissolved in deionized water or any buffer solution.n.n.ion.n.n.

• Maxillofacial Plastic and Reconstructive Surgery
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• v.23 no.2
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• pp.180-184
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• 2001

MRSI is the staphylococcal infection having resistance to the methicillin which is semisynthetic penicillinase-resistant agents against penicillinase. These infections are very difficult to treat because they have resistance to almost every antibiotics except for vancomycin. We experienced MRSE(methicilline-resistant staphylococcal epidermis) infected 56 years old man who developed 2 months after arthroplasty for TMJ ankylosis and MRSA(methicilline-resistant staphylococcal aureus) infected 59 years old man who was performed arthroplasty far traumatic TMJ disc displacement.

• Journal of Microbiology and Biotechnology
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• v.14 no.4
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• pp.698-706
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• 2004

$\beta$-Lactam antibiotics such as penicillin G, amoxicillin, and ampicillin were determined by a potentiometric biosensor system which exploited penicillinase immobilized on Immobilon cellulose nitrate membrane and a flat-bottomed pH electrode-as the biological component and transducer. The optimum reaction buffer for maximum sensitivity was found as 2 mM of sodium phosphate buffer (pH 7.2). The detection limit of the biosensor could be extended to 1 $\mu{M}$ of the analytes by increasing the enzyme loading for immobilization to 100 units/$m\ell$. The model samples spiked with each of the standard penicillins were measured for their biosensor responses and HPLC peak area, resulting in the relative responses of 82.1-103.5% and 79.5-106.1% for the biosensor method along with HPLC analysis, respectively. This result showed a good precision of the current biosensor method for screening the penicillin compounds.

• YAKHAK HOEJI
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• v.40 no.1
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• pp.72-77
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• 1996

Penicillin sensor was manufactured by immobillizing penicillinase with glutaraldehyde on the $H^+$-selective membrane based on PVC-COOH-TDDA. This membrane was not inter fered by $K^+$ ion in Pc-G potassium salt. When enzyme was immobilized with glutaraldehyde, the PVC-COOH matrix was more effective than PVC matrix. Calibration curve calculated from Nernst equation was not linear. But potential was relative to concentration of Pc-G. And maximal potentiometric velocity was also relative to concentration of Pc-G. Therefore, it may be applied to Michaelis-Menten equation. The penicillin sensor was useful for determination of Pc-G at concentration of 0.1~10mM level.