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Journal articles on the topic 'Cephalosporin C'

Author: Grafiati

Published: 4 June 2021

Last updated: 8 February 2022

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1

Hardianto, Dudi, Bima Wedana Isdiyono, and Fransiskus Xaverius Ivan. "BIOKONVERSI SEFALOSPORIN C MENJADI ASAM 7-AMINOSEFALOSPORANAT DENGAN SEFALOSPORIN ASILASE." Jurnal Bioteknologi & Biosains Indonesia (JBBI) 3, no. 2 (December 13, 2016): 89. http://dx.doi.org/10.29122/jbbi.v3i2.139.

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Cephalosporins are the most widely used class of β-lactam antibiotic in the world and clinically active against gram positive and gram negative bacteria. Cephalosporin C (CPC) is naturally produced by fungus Cephalosporiun acremonium. CPC has moderate antibacterial activity with minimum inhibitory concentration values of 25-100 µg/mL and 12-25 µg/mL for gram-positive and for gram-negative bacteria, respectively. CPC can be converted into 7-aminocephalosporonic acid (7-ACA) as intermediate compound for cephalosporin derivatives by two-steps or one-step enzymatic method. Two-step enzymatic method uses D-amino acid oxidase (DAAO) to produce glutaryl-7-amino cephalosporanic acid (GL 7-ACA) for the first step and GL-7-ACA acylase to produce 7-ACA for the second step. One-step enzymatic method uses CPC acylase to convert CPC into 7-ACA directly. Some microorganisms produce CPC acylase, such as Pseudomonas sp., Bacillus megaterium, Aeromonas sp., dan Arthrobacler. A natural CPC acylase has low activity and genetic engineering was used to increase its activity.Keywords: Cephalosporin, cephalosporin acylase, 7-ACA, genetic engineering, mutation ABSTRAKSefalosporin merupakan antibiotik golongan β-laktam yang paling banyak digunakan di dunia dan secara klinis aktif terhadap bakteri gram positif dan gram negatif. Sefalosporin C merupakan sefalosporin alami yang dihasilkan oleh kapang Cephalosporium acremonium. Sefalosporin C mempunyai aktivitas antibakteri moderat dengan nilai konsentrasi hambat minimum 25-100 µg/mL untuk bakteri gram positif dan 12-25 µg/mL untuk bakteri gram negatif. Sefalosporin C dapat diubah menjadi asam 7-aminosefalosporanat (7-ACA) sebagai senyawa antara untuk pembuatan turunan sefalosporin dengan metode enzimatik secara dua atau satu tahap. Produksi 7-ACA secara enzimatik dapat menggunakan metode dua tahap dan satu tahap enzimatik. Metode enzimatik secara dua tahap menggunakan enzim asam D-amino oksidase (DAAO) untuk menghasilkan asam glutaril-7-aminosefalosporinat (GL-7-ACA) pada tahap pertama dan menggunakan asam glutaril-7-aminosefalosporinat asilase untuk menghasilkan 7-ACA pada tahap kedua. Metode enzimatik secara satu tahap menggunakan sefalosporin asilase untuk mengubah CPC menjadi 7-ACA secara langsung. Beberapa mikroorganisme penghasil sefalosporin asilase yaitu Pseudomonas sp., Bacillus megaterium, Aeromonas sp., dan Arthrobacter. Aktivitas CPC asilase alami sangat rendah dan rekayasa genetik digunakan untuk meningkatkan aktivitasnya.Kata kunci : Sefalosporin, sefalosporin asilase, 7-ACA, rekayasa genetik, mutasi

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2

Xiao, X., S. Wolfe, and A. L. Demain. "Purification and characterization of cephalosporin 7α-hydroxylase from Streptomyces clavuligerus." Biochemical Journal 280, no. 2 (December 1, 1991): 471–74. http://dx.doi.org/10.1042/bj2800471.

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Cephalosporin 7 alpha-hydroxylase, which catalyses the conversion of cephalosporins into their 7 alpha-hydroxy derivatives, was purified nearly 390-fold from Streptomyces clavuligerus through ion-exchange chromatography, (NH4)2SO4 fractionation, gel filtration and dye chromatography, with the use of h.p.l.c. to monitor enzyme activity. The nearly pure enzyme migrates as a single major band, with an Mr of 32,000 in SDS/PAGE. Its optimum pH is in the range 7.3-7.7. Under our conditions the reaction was fastest at temperatures in the range 20-30 degrees C. The Km for cephalosporin C is 0.72 mM, and the Vmax. is 15.4 mumol of cephalosporin C hydroxylated/min per mg. Cephalosporin 7 alpha-hydroxylase did not show any deacetoxycephalosporin C synthase or deacetoxycephalosporin C hydroxylase activity.

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3

Balakrishnan, Nataraj, Sadhasivam Ganesan, Padma Rajasekaran, Lingeshwaran Rajendran, Sivaprasad Teddu, and Micheal Durairaaj. "Modified Deacetylcephalosporin C Synthase for the Biotransformation of Semisynthetic Cephalosporins." Applied and Environmental Microbiology 82, no. 13 (April 15, 2016): 3711–20. http://dx.doi.org/10.1128/aem.00174-16.

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ABSTRACTDeacetylcephalosporin C synthase (DACS), a 2-oxoglutarate-dependent oxygenase synthesized byStreptomyces clavuligerus, transforms an inert methyl group of deacetoxycephalosporin C (DAOC) into an active hydroxyl group of deacetylcephalosporin C (DAC) during the biosynthesis of cephalosporin. It is a step which is chemically difficult to accomplish, but its development by use of an enzymatic method with DACS can facilitate a cost-effective technology for the manufacture of semisynthetic cephalosporin intermediates such as 7-amino-cephalosporanic acid (7ACA) and hydroxymethyl-7-amino-cephalosporanic acid (HACA) from cephalosporin G. As the native enzyme showed negligible activity toward cephalosporin G, an unnatural and less expensive substrate analogue, directed-evolution strategies such as random, semirational, rational, and computational methods were used for systematic engineering of DACS for improved activity. In comparison to the native enzyme, several variants with improved catalytic efficiency were found. The enzyme was stable for several days and is expressed in soluble form at high levels with significantly higherkcat/Kmvalues. The efficacy and industrial scalability of one of the selected variants, CefFGOS, were demonstrated in a process showing complete bioconversion of 18 g/liter of cephalosporin G into deacetylcephalosporin G (DAG) in about 80 min and showed reproducible results at higher substrate concentrations as well. DAG could be converted completely into HACA in about 30 min by a subsequent reaction, thus facilitating scalability toward commercialization. The experimental findings with several mutants were also used to rationalize the functional conformation deduced from homology modeling, and this led to the disclosure of critical regions involved in the catalysis of DACS.IMPORTANCE7ACA and HACA serve as core intermediates for the manufacture of several semisynthetic cephalosporins. As they are expensive, a cost-effective enzyme technology for the manufacture of these intermediates is required. Deacetylcephalosporin C synthase (DACS) was identified as a candidate enzyme for the development of technology from cephalosporin G in this study. Directed-evolution strategies were employed to enhance the catalytic efficiency of deacetylcephalosporin C synthase. One of the selected mutants of deacetylcephalosporin C synthase could convert high concentrations of cephalosporin G into DAG, which subsequently could be converted into HACA completely. As cephalosporin G is inexpensive and readily available, the technology would lead to a substantial reduction in the cost for these intermediates upon commercialization.

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4

Botnarciuc, Mihaela, Irina Stan, and Sorina Ispas. "Cephalosporin resistant bacterial strains isolated from respiratory infections." ARS Medica Tomitana 21, no. 1 (February 1, 2015): 7–11. http://dx.doi.org/10.1515/arsm-2015-0012.

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Abstract Objectives: The objective of the study is the evaluation of the actual resistance to second, third, and fourth generation cephalosporins over bacterial strains isolated from respiratory infections. The main causes for cephalosporin resistance of pathogenic and conditioned pathogen bacteria are: widespread usage, and impair immune response. Materials and methods: The analyzed specimens were throat swabs and sputum, from adult patients. The tests were performed using disk diffusion technique. We tested the following cephalosporin: From second generation: cefuroxime axetil; from third generation: cefotaxime, ceftazidime, cefpodoxime; Combinations of cephalosporins and beta-lactamase inhibitors: cefotaxime + clavulanic acid; ceftazidim + clavulanic acid; From fourth generation: cefepime; and association cefepime and clavulanic acid. Results: The following bacterial strains were isolated: Staphylococcus aureus, Streptococcus pneumoniae, Group C β-hemolytic Streptococcus, E. coli, Klebsiella pneumoniae and Proteus sp. The Group A. β-hemolytic Streptococcus isolated strains were not tested. For Staphylococcus aureus, E. coli, K. pneumoniae and Proteus, we found a high frequency resistance tocefuroxim, approximately 47%. Highest resistance to third generation cephalosporin was identified to E.coli and Klebsiella pneumoniae, especially resistant to cefotaxime, cefotaxime + clavulanic acid and ceftazidime. Conclusions: Cefpodoxime can be considered as a first election antibiotic in treating upper and lower respiratory tract infections, due to the lowest level of bacterial strain resistance, approximately 10% of the third generation cephalosporines tested. Also, cefepime may be proper in treating severe respiratory tract infections, with resistant broad-spectrum antibiotics bacterial strains. In our trial, resistance to cefepime was to a minimum low, approximately 4%, represented by the E.coli strains.

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5

Baldwin, Jack E., Robert M. Adlington, Nicholas P. Crouch, and Christopher J. Schofield. "The enzymatic conversion of exomethylene cephalosporin c into deacetyl cephalosporin c and the role of molecular oxygen in cephalosporin c biosynthesis." Tetrahedron 44, no. 2 (January 1988): 643–50. http://dx.doi.org/10.1016/s0040-4020(01)85852-x.

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6

Braña, Alfredo F., Saul Wolfe, and Arnold L. Demain. "Ammonium repression of cephalosporin production by Streptomyces clavuligerus." Canadian Journal of Microbiology 31, no. 8 (August 1, 1985): 736–43. http://dx.doi.org/10.1139/m85-138.

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Production of β-lactam antibiotics took place during growth of Streptomyces clavuligerus in chemically defined medium. The specific activities of isopenicillin N synthetase ("cyclase"), isopenicillin N epimerase, and deacetoxycephalosporin C synthetase ("expandase") increased during the exponential phase of growth. Specific cephalosporin productivity during fermentation followed a similar pattern, reaching a maximum near the end of the growth phase and decaying rapidly in the stationary phase. Ammonium chloride depressed cephalosporin production, presumably as a result of repression of cyclase and expandase formation, but not of epimerase. No inhibitory effects on enzyme activity by ammonium were found. Addition of tribasic magnesium phosphate [Mg3(PO4)2∙8H2O] prevented the repression of cyclase and markedly stimulated cephalosporin production. Cephamycin C and, in smaller amounts, O-carbamoyldeacetylcephalosporin C were the only cephalosporins detected. Growth with ammonium resulted in lower titers of both compounds, and did not change the relative proportion of each. The correlation found between cephalosporin productivity and cyclase specific activity in different media suggests that formation of this enzyme may be the rate-limiting step in the pathway.

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7

Hano, Tadashi, Michiaki Matsumoto, Takaaki Ohtake, and Fumiaki Hori. "Reactive extraction of cephalosporin C." JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 25, no. 3 (1992): 293–97. http://dx.doi.org/10.1252/jcej.25.293.

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8

Usher, John J., MaryAnn Lewis, Doris W. Hughes, and Bruce J. Compton. "Development of the cephalosporin C fermentation taking into account the instability of cephalosporin C." Biotechnology Letters 10, no. 8 (August 1988): 543–48. http://dx.doi.org/10.1007/bf01027126.

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9

Mustika, Indria Puti, and Ahmad Wibisana. "PERAN MUTASI GEN ACY II TERHADAP PRODUKSI ANTIBIOTIK SEFALOSPORIN." Jurnal Bioteknologi & Biosains Indonesia (JBBI) 4, no. 2 (December 30, 2017): 96. http://dx.doi.org/10.29122/jbbi.v4i2.2272.

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The Roles of AcyII Gene Mutations for Production of Antibiotics Derived From CephalosporinSemisynthetic antibiotics cephalosporins are widely used to treat infectious diseases, especially those caused by gram-negative bacteria. Various types of semisynthetic antibiotics could be synthesized using 7-aminocephalosporanic acid (7-ACA) as the main raw material. 7-ACA is obtained by conversion of cephalosporin C, either chemically or enzymatically. Converting cephalosporin C to 7-ACA enzymatically in one step involves the cephalosporin acylase enzyme. Currently, all of cefalosporin acylase enzymes produced by wild-type microbes have only high activity on glutaryl-7-ACA as the main substrate. Genetic engineering of the encoding gene of cefalosporin acylase is required to obtain recombinant enzyme having high activity on cephalosporin C. In this paper, the engineering attempts made on acyII gene from Pseudomonas SE83 using directed mutagenesis, error prone PCR, and structural modeling are described. Keywords: AcyII gene, cephalosporin, cephalosporin C acylase, enzyme activity, mutation ABSTRAKAntibiotik sefalosporin semisintetik banyak digunakan untuk mengatasi penyakit infeksi, khususnya yang ditimbulkan oleh bakteri gram negatif. Berbagai jenis antibiotik semisintetk dapat disintesis menggunakan senyawa asam 7-aminosefalosporanat (7-ACA) sebagai bahan baku utamanya. Senyawa 7-ACA diperoleh melalui konversi sefalosporin C, baik yang dilakukan secara kimiawi maupun enzimatis. Konversi sefalosporin C menjadi 7-ACA secara enzimatis dalam satu langkah melibatkan enzim sefalosporin asilase. Hingga saat ini, seluruh enzim sefalosporin asilase yang dihasilkan oleh mikroba wild type hanya mempunyai aktifitas yang tinggi terhadap glutaryl-7-ACA. Rekayasa genetik terhadap gen pengkode enzim sefalosporin asilase diperlukan untuk memperoleh enzim rekombinan yang mempunyai aktifitas tinggi terhadap substrat sefalosporin C. Dalam ulasan ini diuraikan upaya-upaya rekayasa yang telah dilakukan terhadap gen acyII dari Pseudomonas SE83 menggunakan teknik mutasi terarah, error prone PCR, dan pemodelan struktur.Kata kunci: Aktivitas enzim, gen acyII, mutasi, sefalosporin, sefalosporin C asilase Received: 14September 2017 Accepted: 19 December 2017 Published: 30 December 2017 Received: 14September 2017 Accepted: 19 December 2017 Published: 30 December 2017

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10

Atroshenko, Denis L., Mikhail D. Shelomov, Sophia A. Zarubina, Nikita Y. Negru, Igor V. Golubev, Svyatoslav S. Savin, and Vladimir I. Tishkov. "Multipoint TvDAAO Mutants for Cephalosporin C Bioconversion." International Journal of Molecular Sciences 20, no. 18 (September 7, 2019): 4412. http://dx.doi.org/10.3390/ijms20184412.

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d-amino acid oxidase (DAAO, EC 1.4.3.3) is used in many biotechnological processes. The main industrial application of DAAO is biocatalytic production of 7-aminocephalosporanic acid from cephalosporin C with a two enzymes system. DAAO from the yeast Trigonopsis variabilis (TvDAAO) shows the best catalytic parameters with cephalosporin C among all known DAAOs. We prepared and characterized multipoint TvDAAO mutants to improve their activity towards cephalosporin C and increase stability. All TvDAAO mutants showed better properties in comparison with the wild-type enzyme. The best mutant was TvDAAO with amino acid changes E32R/F33D/F54S/C108F/M156L/C298N. Compared to wild-type TvDAAO, the mutant enzyme exhibits a 4 times higher catalytic constant for cephalosporin C oxidation and 8- and 20-fold better stability against hydrogen peroxide inactivation and thermal denaturation, respectively. This makes this mutant promising for use in biotechnology. The paper also presents the comparison of TvDAAO catalytic properties with cephalosporin C reported by others.

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11

Tong, Shuangming, Linlin Zhu, Xiaona Wang, Xi LI, Yanhong Chang, and Hui Luo. "Optimization of Cephalosporin C Acylase Immobilization." E3S Web of Conferences 78 (2019): 02003. http://dx.doi.org/10.1051/e3sconf/20197802003.

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Cephalosporin C Acylase (CCA), the key biocatalyst in one-step enzymatic production of 7- amino cephalosporanic acid (7-ACA), was immobilized by amino-activated carrier (LX-1000HA) and epoxy-activated carriers (ES-103B, LX-1000EPC), and the activity was assayed. ES-103B carriers showed an advantage than the others. The amount of free enzyme and salt concentration were tested, and the optimum conditions were 1400U/g and 0.9M. In addition, two different methods (by shaker and packed column) were used in CCA immobilization, and the results demonstrated that the former obtained a higher immobilized CCA activity.

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12

Hicketier, M., and K. Buchholz. "Fluidized bed adsorption of Cephalosporin C." Journal of Biotechnology 93, no. 3 (February 2002): 253–68. http://dx.doi.org/10.1016/s0168-1656(01)00408-4.

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13

Despande, Bhagwant S., Sudha S. Ambedkar, and Jaiprakash G. Shewale. "Monitoring of cephalosporin C during bioconversion." Applied Biochemistry and Biotechnology 60, no. 3 (September 1996): 245–50. http://dx.doi.org/10.1007/bf02783587.

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14

Babu, Setty Mallikarjuna, and Subramania Ranganathan. "The total synthesis of Cephalosporin C." Resonance 19, no. 7 (July 2014): 649–53. http://dx.doi.org/10.1007/s12045-014-0067-1.

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15

Ullán, Ricardo V., Fernando Teijeira, Susana M. Guerra, Inmaculada Vaca, and Juan F. Martín. "Characterization of a novel peroxisome membrane protein essential for conversion of isopenicillin N into cephalosporin C." Biochemical Journal 432, no. 2 (November 12, 2010): 227–36. http://dx.doi.org/10.1042/bj20100827.

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The mechanisms of compartmentalization of intermediates and secretion of penicillins and cephalosporins in β-lactam antibiotic-producing fungi are of great interest. In Acremonium chrysogenum, there is a compartmentalization of the central steps of the CPC (cephalosporin C) biosynthetic pathway. In the present study, we found in the ‘early’ CPC cluster a new gene named cefP encoding a putative transmembrane protein containing 11 transmembrane spanner. Targeted inactivation of cefP by gene replacement showed that it is essential for CPC biosynthesis. The disrupted mutant is unable to synthesize cephalosporins and secretes a significant amount of IPN (isopenicillin N), indicating that the mutant is blocked in the conversion of IPN into PenN (penicillin N). The production of cephalosporin in the disrupted mutant was restored by transformation with both cefP and cefR (a regulatory gene located upstream of cefP), but not with cefP alone. Fluorescence microscopy studies with an EGFP (enhanced green fluorescent protein)–SKL (Ser-Lys-Leu) protein (a peroxisomal-targeted marker) as a control showed that the red-fluorescence-labelled CefP protein co-localized in the peroxisomes with the control peroxisomal protein. In summary, CefP is a peroxisomal membrane protein probably involved in the import of IPN into the peroxisomes where it is converted into PenN by the two-component CefD1/CefD2 protein system.

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16

Sohn, Young-Sun, Keun-Cheol Lee, Young-Hwan Koh, and Gwang-Hoon Gil. "Changes in Cellular Fatty Acid Composition of Cephalosporium acremonium during Cephalosporin C Production." Applied and Environmental Microbiology 60, no. 3 (1994): 947–52. http://dx.doi.org/10.1128/aem.60.3.947-952.1994.

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17

Skatrud, Paul L., Anthony J. Tietz, Thomas D. Ingolia, Cathleen A. Cantwell, Deborah L. Fisher, Jerry L. Chapman, and Stephen W. Queener. "Use of Recombinant DNA to Improve Production of Cephalosporin C By Cephalosporium acremonium." Nature Biotechnology 7, no. 5 (May 1989): 477–85. http://dx.doi.org/10.1038/nbt0589-477.

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18

Park, Hong-Je, and Yong-Ho Khang. "Production of cephalosporin C by immobilized Cephalosporium acremonium in polyethyleneimine-modified barium alginate." Enzyme and Microbial Technology 17, no. 5 (May 1995): 408–12. http://dx.doi.org/10.1016/0141-0229(94)00076-4.

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19

Ren, Yu, Yulin Lei, and Yushan Zhu. "Site-Directed Mutagenesis of Cephalosporin C Acylase and Enzymatic Conversion of Cephalosporin C to 7-Aminocephalosporanic Acid." Turkish Journal of Biochemistry 39, no. 1 (2014): 51–56. http://dx.doi.org/10.5505/tjb.2014.48569.

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20

Hardianto, Dudi, Juwartina Royani, and Anna Safarrida. "Cephalosporin C Acylase from Microbes for One-step Enzymatic Transformation of Cephalosporin C to 7-Aminocephalosporanic Acid." Journal of Pure and Applied Microbiology 10, no. 4 (December 31, 2016): 2495–99. http://dx.doi.org/10.22207/jpam.10.4.03.

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21

Mazzella, L. J., and R. F. Pratt. "Effect of the 3′-leaving group on turnover of cephem antibiotics by a class C β-lactamase." Biochemical Journal 259, no. 1 (April 1, 1989): 255–60. http://dx.doi.org/10.1042/bj2590255.

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It has been previously demonstrated for class A beta-lactamases and the DD-peptidase of Streptomyces R61 that the presence of a leaving group at the 3′-position of a cephalosporin can lead to the generation of more-inert acyl-enzyme intermediates than from cephalosporins lacking such a leaving group, and thus to beta-lactamase inhibitors and potentially better antibiotics. In the present work we extend this result to a class C beta-lactamase, that of Enterobacter cloacae P99. The effect is not seen with first-generation cephalosporins, since here deacylation generally seems faster than elimination of the leaving group, but it does clearly appear with cephamycins and third-generation cephalosporins. The structural and/or mechanistic features of the active site giving rise to this phenomenon may thus be common to all serine beta-lactamases and transpeptidases.

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22

Cummings, Maxwell D., David P. Czajkowski, John Brunstein, Narender A. V. Reddy, Oludotun A. Phillips, Charles Fiakpui, Paul Spevak, Ronald G. Micetich, and Samarendra N. Maiti. "2α-Alkoxymethyl Cephalosporins: Reactions of exo-2-Methylene Cephalosporin Sulfones with Alcohols." Collection of Czechoslovak Chemical Communications 59, no. 10 (1994): 2282–92. http://dx.doi.org/10.1135/cccc19942282.

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A series of 2α-alkoxymethyl cephem sulfones were prepared by nucleophilic addition of a variety of alcohols to exo-2-methylene cephem sulfones. The 2α-alkoxymethyl group was introduced with the aim of improving the inhibitory activity against human leukocyte elastase (HLE) over the unsubstituted compounds. However, against HLE the in vitro activity was still inferior to that shown by the C-2 unsubstituted cephem sulfones.

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23

Zafira, Indira Zahra, and Jobrun Nandong. "Optimal feeding strategy of Cephalosporin C fermentation." IOP Conference Series: Materials Science and Engineering 495 (June 7, 2019): 012107. http://dx.doi.org/10.1088/1757-899x/495/1/012107.

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24

YAMADA, HISASHI, YOSHINORI ISHII, YUJI NOGUCHI, TOSHIKO MIURA, THORU MORI, and YOSHIMASA SAITO. "Protein Engineering of a Cephalosporin C Acylase." Annals of the New York Academy of Sciences 799, no. 1 Enzyme Engine (October 1996): 74–81. http://dx.doi.org/10.1111/j.1749-6632.1996.tb33181.x.

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25

Pollegioni, Loredano, Elena Rosini, and Gianluca Molla. "Cephalosporin C acylase: dream and(/or) reality." Applied Microbiology and Biotechnology 97, no. 6 (February 16, 2013): 2341–55. http://dx.doi.org/10.1007/s00253-013-4741-0.

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26

Yang, Wu-Yung, Chun-Der Lin, I.-Ming Chu, and Chau-Jen Lee. "Extraction of cephalosporin C from whole broth and separation of desacetyl cephalosporin C by aqueous two-phase partition." Biotechnology and Bioengineering 43, no. 6 (March 15, 1994): 439–45. http://dx.doi.org/10.1002/bit.260430602.

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27

Preston, Sandra L., and Laurie L. Briceland. "Intrathecal Administration of Amikacin for Treatment of Meningitis Secondary to Cephalosporin-Resistant Escherichia Coli." Annals of Pharmacotherapy 27, no. 7-8 (July 1993): 870–73. http://dx.doi.org/10.1177/106002809302700709.

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OBJECTIVE: To report a case of gram-negative bacillary meningitis (GNBM) secondary to cephalosporin-resistant Escherichia coli that was treated with intrathecal and intravenous amikacin and intravenous imipenem/cilastatin (I/C). CASE SUMMARY: A patient who had undergone two recent neurosurgical procedures developed GNBM and bacteremia. He was treated empirically with ceftazidime. Both bloodstream and cerebrospinal fluid isolates were identified as E. coli, resistant to third-generation cephalosporins, penicillins, tobramycin, and gentamicin. The patient was subsequently treated with intravenous and intrathecal amikacin plus intravenous I/C He experienced subjective and objective improvement on days 2–4 of antimicrobial therapy; two generalized tonic-clonic seizures occurred on days 7 and 12. Intrathecal amikacin was discontinued after 6 days, and intravenous amikacin and I/C were discontinued after 23 and 27 days, respectively. The patient's mental status did not completely return to premeningitis baseline. DISCUSSION: Third-generation cephalosporins are the treatment of choice for GNBM. In the case reported herein, bacterial resistance to these agents prompted the use of a therapy that has not been well studied and is also considered to be less safe and perhaps less efficacious. Treatment of GNBM with an intrathecally administered aminoglycoside or with intravenous I/C plus an aminoglycoside is reviewed. CONCLUSIONS: Patients with GNBM secondary to third-generation cephalosporin-resistant organisms may require therapies that may be less effective and more toxic. Further study of alternative agents is warranted.

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28

Zhang, Jinyou, Saul Wolfe, and Arnold L. Demain. "Ammonium ions repress δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine synthetase in Streptomyces clavuligerus NRRL 3585." Canadian Journal of Microbiology 35, no. 3 (March 1, 1989): 399–402. http://dx.doi.org/10.1139/m89-061.

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Production of cephems (predominantly cephamycin C) by Streptomyces clavuligerus grown in chemically defined medium supplemented with 120 mM NH4Cl was sharply reduced. This concentration of ammonium ions in the medium repressed δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (ACV) synthetase formation by about 75%. Of the other cephalosporin synthases, cyclase was repressed by 70%, expandase by 50%, and epimerase only to a very small extent. Inhibition of the action of ACV synthetase was only slight in the presence of 100 mM NH4Cl. Repression of ACV synthetase, cyclase, and expandase appears to be the major factors contributing to the negative effect of ammonium on S. clavuligerus NRRL 3585. ACV synthetase is probably the rate-limiting step of cephalosporin biosynthesis in this strain.Key words: β-lactam biosynthesis, antibiotic biosynthesis, cephalosporins, Streptomyces clavuligerus, ACV synthetase.

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29

Teijeira, Fernando, Ricardo V. Ullán, Susana M. Guerra, Carlos García-Estrada, Inmaculada Vaca, and Juan F. Martín. "The transporter CefM involved in translocation of biosynthetic intermediates is essential for cephalosporin production." Biochemical Journal 418, no. 1 (January 28, 2009): 113–24. http://dx.doi.org/10.1042/bj20081180.

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The cluster of early cephalosporin biosynthesis genes (pcbAB, pcbC, cefD1, cefD2 and cefT of Acremonium chrysogenum) contains all of the genes required for the biosynthesis of the cephalosporin biosynthetic pathway intermediate penicillin N. Downstream of the cefD1 gene, there is an unassigned open reading frame named cefM encoding a protein of the MFS (major facilitator superfamily) with 12 transmembrane domains, different from the previously reported cefT. Targeted inactivation of cefM by gene replacement showed that it is essential for cephalosporin biosynthesis. The disrupted mutant accumulates a significant amount of penicillin N, is unable to synthesize deacetoxy-, deacetyl-cephalosporin C and cephalosporin C and shows impaired differentiation into arthrospores. Complementation of the disrupted mutant with the cefM gene restored the intracellular penicillin N concentration to normal levels and allowed synthesis and secretion of the cephalosporin intermediates and cephalosporin C. A fused cefM-gfp gene complemented the cefM-disrupted mutant, and the CefM–GFP (green fluorescent protein) fusion was targeted to intracellular microbodies that were abundant after 72 h of culture in the differentiating hyphae and in the arthrospore chains, coinciding with the phase of intense cephalosporin biosynthesis. Since the dual-component enzyme system CefD1–CefD2 that converts isopenicillin N into penicillin N contains peroxisomal targeting sequences, it is probable that the epimerization step takes place in the peroxisome matrix. The CefM protein seems to be involved in the translocation of penicillin N from the peroxisome (or peroxisome-like microbodies) lumen to the cytosol, where it is converted into cephalosporin C.

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Li, Ruichao, Dachuan Lin, Kaichao Chen, Marcus Ho Yin Wong, and Sheng Chen. "First Detection of AmpC β-LactamaseblaCMY-2on a Conjugative IncA/C Plasmid in a Vibrio parahaemolyticus Isolate of Food Origin." Antimicrobial Agents and Chemotherapy 59, no. 7 (April 27, 2015): 4106–11. http://dx.doi.org/10.1128/aac.05008-14.

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ABSTRACTVibrio parahaemolyticusis an important causative agent of gastroenteritis, with the consumption of contaminated seafood being the major transmission route. Resistance to penicillin is common amongV. parahaemolyticusstrains, whereas cephalosporin resistance remains rare. In an attempt to assess the current prevalence and characteristics of antibiotic resistance of this pathogen in common food samples, a total of 54 (17% of the total samples)V. parahaemolyticusstrains were isolated from 318 meat and seafood samples purchased from supermarkets and wet markets in Shenzhen, China, in 2013. These isolates exhibited high-level resistance to ampicillin, yet they were mostly susceptible to other antimicrobials, except for two that were resistant to extended-spectrum cephalosporins. The β-lactamase geneblaPER-1was detectable in one strain,V. parahaemolyticusV43, which was resistant to both third- and fourth-generation cephalosporins. Compared to otherblaPER-1-positiveV. parahaemolyticusstrains reported in our previous studies, strain V43 was found to harbor an ∼200-kb conjugative plasmid carrying genes that were different from the antimicrobial resistance genes reported from the previous studies. The β-lactamase geneblaCMY-2was detectable for the first time in anotherV. parahaemolyticusisolate, V4, which was resistant to third-generation cephalosporins. ThisblaCMY-2gene was shown to be located in an ∼150-kb IncA/C-type conjugative plasmid with a genetic structure consisting oftraB-traV-traA-ISEcp1-blaCMY-2-blc-sugE-encR-orf1-orf2-orf3-orf4-dsbC-traC, which is identical to that of other IncA/C conjugative plasmids inEnterobacteriaceae, albeit with a different size. These findings indicate that the transmission of extended-spectrum-β-lactamase (ESBL) and AmpC β-lactamase genes via conjugative plasmids can mediate the development of extended-spectrum cephalosporin resistance inV. parahaemolyticus, thereby posing a potential threat to public health.

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Lin, Po-Chun, and I.-Ming Chu. "Separation of cephalosporin C and desacetyl cephalosporin C by high speed counter-current chromatography in aqueous two-phase systems." Biotechnology Techniques 9, no. 8 (August 1995): 549–52. http://dx.doi.org/10.1007/bf00152441.

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Ma, Xiaoqiang, Senwen Deng, Erzheng Su, and Dongzhi Wei. "One-pot enzymatic production of deacetyl-7-aminocephalosporanic acid from cephalosporin C via immobilized cephalosporin C acylase and deacetylase." Biochemical Engineering Journal 95 (March 2015): 1–8. http://dx.doi.org/10.1016/j.bej.2014.11.015.

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33

Felici, A., M. Perilli, N. Franceschini, G. M. Rossolini, M. Galleni, J. M. Frere, A. Oratore, and G. Amicosante. "Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases." Antimicrobial Agents and Chemotherapy 41, no. 4 (April 1997): 866–68. http://dx.doi.org/10.1128/aac.41.4.866.

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Ceftriaxone and ceftriaxone S-oxide behaved as inactivators against the metallo-beta-lactamase of Aeromonas hydrophila AE036 and as substrates for the zinc beta-lactamase produced by Bacillus cereus (569/H/9) and Stenotrophomonas maltophilia ULA 511. Moreover, RO 09-1428, a catechol-cephalosporin, was not recognized by the A. hydrophila enzyme. Panipenem, cephalosporin C, cephalosporin C-gamma-lactone, and loracarbef were substrates for the three studied beta-lactamases.

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34

Prabandari, Erwahyuni, Dyah Noor Hidayati, Diana Dewi, Eni Dwi Islamiati, and Khaswar Syamsu. "PENINGKATAN PRODUKSI SEFALOSPORIN C DARI Acremonium chrysogenum CB2/11/1.10.6 DENGAN OPTIMASI MEDIA MENGGUNAKAN METODE RESPON PERMUKAAN." Jurnal Bioteknologi & Biosains Indonesia (JBBI) 4, no. 1 (June 8, 2017): 10. http://dx.doi.org/10.29122/jbbi.v4i1.1808.

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Cephalosporin is a β-lactam antibiotic produced by Acremonium chrysogenum using submerged fermentation. Carbon and nitrogen are the most influential medium ingredients for cephalosporin formation. The purpose of this study was to obtain the best composition of media for cephalosporin C production. Response surface methodology was used for production optimization. The results showed that molasses of 70 g/Lwas the best carbon source, while the best nitrogen source was the combination of corn steep liquor, urea and ammonium sulphate. DL-methionine, carbon, and nitrogen source significantly affected the production of cephalosporin C. The mathematically modelled optimization showed that the highest production of cephalosporin C (3876 mg/L) was obtained using medium composition of 68.28 g/L molasses, 71.61 g/L nitrogen, and 0.4 g/L DL-methionine. Laboratory verification using the same medium composition produced 3696 mg/L of cephalosporin C, being 4.65% different from the mathematically optimized results. Medium optimization increased the cephalosprin C production which was 1.48 times higher than that using the previous medium, where the maximum production was only 2487 mg / L.Keywords: Carbon, cephalosporin C, cultivation medium, nitrogen, A. chrysogenum ABSTRAKSefalosporin C adalah golongan antibiotik β-lactam yang dihasilkan Acremonium chrysogenum melalui fermentasi cair. Komponen yang sangat berpengaruh terhadap produksi sefalosporin C adalah sumber karbon dan nitrogen. Penelitian ini bertujuan mendapatkan komposisi media terbaik untuk produksi sefalosporin C. Optimasi dilakukan menggunakan metode respon permukaan. Hasil menunjukkan bahwa molases 70 g/L adalah sumber karbon terbaik dan kombinasi corn steep liquor, urea dan ammonium sulfat adalah sumber nitrogen terbaik. DL-methionin, sumber karbon, dan nitrogen berpengaruh nyata terhadap produksi sefalosporin C. Optimasi menggunakan model matematika menunjukkan produksi sefalosporin C tertinggi (3876 mg/L) yang diperoleh dengan komposisi media 68,28 g/L molases, 71,61 g/L nitrogen, dan 0,4 g/L DL-methionin. Verfikasi di laboratorium menggunakan komposisi media yang sama menghasilkan sefalosporin C sebesar 3696 mg/L, berbeda 4,65% dibanding dengan hasil optimasi matematis. Optimasi media mampu meningkatkan produksi sefalosprin C sebesar 1,48 kali dibanding media yang digunakan sebelumnya, dimana maksimal hanya menghasilkan 2487 mg/L.Kata kunci: Karbon, sefalosporin C, media kultivasi, nitrogen, A. chrysogenum

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Demain, Arnold L., and Jinyou Zhang. "Cephalosporin C Production byCephalosporium acremonium: The Methionine Story." Critical Reviews in Biotechnology 18, no. 4 (January 1998): 283–94. http://dx.doi.org/10.1080/0738-859891224176.

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REYES, F., M. J. MARTINEZ, and J. SOLIVERI. "Determination of cephalosporin-C amidohydrolase activity with fluorescamine." Journal of Pharmacy and Pharmacology 41, no. 2 (February 1989): 136–37. http://dx.doi.org/10.1111/j.2042-7158.1989.tb06412.x.

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37

Han, Kai Hua, Hui Luo, Yao Zhen Xie, Shun Yao, Yan Hong Chang, Hui Min Yu, Qiang Li, and Zhong Yao Shen. "Immobilization and Thermostability Characterization of Cephalosporin C Acylase." Advanced Materials Research 634-638 (January 2013): 682–88. http://dx.doi.org/10.4028/www.scientific.net/amr.634-638.682.

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Some kinds of epoxy supports, LX1000-EP(C), LX1000-EP(D), LKZ-116, LKZ-118 and LKZ-126 were utilized to covalently immobilize cephalosporin C (CPC) acylase, the key enzyme in the one-step enzymatic process of 7-aminocephalosporanic acid (7-ACA) production. After preliminary carrier screening, the immobilized CPC acylase with LKZ-118 as the support shows the highest activity (115 U/g) suggesting its potential application in industrial 7-ACA production. The conditions of CPC acylase immobilized on LKZ-118 to achieve higher activity and thermostability of the immobilized enzyme were optimized by adjusting pH value, buffer concentration, enzyme dosage and immobilized time. The activity of immobilized enzyme was found to be optimal at pH 8.5, in 0.85 M sodium phosphate buffer when the enzyme dosage was 500 U/g and immobilization time was 28 h.

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Rhee, J. I., G. Seidel, and K. Schügerl. "Modellierung der Biosynthese von Cephalosporin C durchAcremonium chrysogenum." Chemie Ingenieur Technik 74, no. 8 (August 15, 2002): 1171–74. http://dx.doi.org/10.1002/1522-2640(20020815)74:8<1171::aid-cite1171>3.0.co;2-t.

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39

Pollegioni, Loredano, Simona Lorenzi, Elena Rosini, Giorgia Letizia Marcone, Gianluca Molla, Roberto Verga, Walter Cabri, and Mirella S. Pilone. "Evolution of an acylase active on cephalosporin C." Protein Science 14, no. 12 (December 2005): 3064–76. http://dx.doi.org/10.1110/ps.051671705.

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40

Herold, T., T. Bayer, and K. Schügerl. "Cephalosporin C production in a stirred tank reactor." Applied Microbiology and Biotechnology 29, no. 2-3 (September 1988): 168–73. http://dx.doi.org/10.1007/bf00939302.

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Herold, T., T. Bayer, and K. Sch�gerl. "Cephalosporin C production in a stirred tank reactor." Applied Microbiology and Biotechnology 29, no. 2-3 (September 1988): 168–73. http://dx.doi.org/10.1007/bf00251697.

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42

Ghosh, A. C., S. Borthakur, M. K. Roy, and N. N. Dutta. "Extraction of cephalosporin C using supported liquid membrane." Separations Technology 5, no. 2 (May 1995): 121–26. http://dx.doi.org/10.1016/0956-9618(95)00114-l.

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43

Weil, Joseph, Joseph Miramonti, and Michael R. Ladisch. "Cephalosporin C: Mode of action and biosynthetic pathway." Enzyme and Microbial Technology 17, no. 1 (January 1995): 85–87. http://dx.doi.org/10.1016/0141-0229(94)00083-4.

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Weil, Joseph, Joseph Miramonti, and Michael R. Ladisch. "Biosynthesis of cephalosporin C: Regulation and recombinant technology." Enzyme and Microbial Technology 17, no. 1 (January 1995): 88–90. http://dx.doi.org/10.1016/0141-0229(94)00084-5.

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45

Hicketier, M., and K. Buchholz. "Investigations on cephalosporin C adsorption kinetics and equilibria." Applied Microbiology and Biotechnology 32, no. 6 (March 1990): 680–85. http://dx.doi.org/10.1007/bf00164739.

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46

Bautista, L. Fernando, José L. Casillas, Mercedes Martínez, and José Aracil. "Functionalized Adsorbents for the Purification of Cephalosporin C and Deacetylcephalosporin C." Industrial & Engineering Chemistry Research 45, no. 9 (April 2006): 3230–36. http://dx.doi.org/10.1021/ie051221m.

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47

Bent, Zachary W., and Glenn M. Young. "Contribution of BlaA and BlaB β-Lactamases to Antibiotic Susceptibility of Yersinia enterocolitica Biovar 1B." Antimicrobial Agents and Chemotherapy 54, no. 9 (June 4, 2010): 4000–4002. http://dx.doi.org/10.1128/aac.01754-09.

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ABSTRACT Highly pathogenic Yersinia enterocolitica biovar 1B produces two distinct β-lactamases, BlaA and BlaB. Mutants of a representative biovar 1B isolate were constructed and evaluated to determine the extent of limitation of susceptibility to broad-spectrum β-lactam antibiotics by BlaA and BlaB. The results demonstrated that BlaA, a class A enzyme, plays a significant role in limiting susceptibility to penicillins and cephalosporins. The contribution of BlaB, a class C enzyme, was less profound and was limited primarily to cephalosporin susceptibility.

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48

Zhu, Xiangwei, Hui Luo, Yanhong Chang, Houbo Su, Qiang Li, Huimin Yu, and Zhongyao Shen. "Characteristic of immobilized cephalosporin C acylase and its application in one-step enzymatic conversion of cephalosporin C to 7-aminocephalosporanic acid." World Journal of Microbiology and Biotechnology 27, no. 4 (August 10, 2010): 823–29. http://dx.doi.org/10.1007/s11274-010-0523-3.

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49

Hermas, Abou-Elhagag A., Abobakr Mohamed Elnady, and Reham M. Ali. "Corrosion inhibition of stainless steel in sulfuric acid solution containing sulfide ions." Anti-Corrosion Methods and Materials 66, no. 3 (May 7, 2019): 360–68. http://dx.doi.org/10.1108/acmm-10-2018-2016.

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Purpose Although stainless steel (SS) has good corrosion resistance in most aqueous solutions, it suffers corrosion in some solutions which contain aggressive ions such as sulfide ions. This study aims to use some cephalosporins (cefotaxime, cephapirin and cefazolin) as corrosion inhibitors of commercial SS in 0.5 M H2SO4 solution containing sulfide ions at 30°C. Design/methodology/approach The study was carried out using weight loss method, potential-time, linear polarization, potentiodynamic polarization, electrochemical impedance measurements, scanning electron microscopy, Fourier transform infrared and energy dispersive X-ray analysis. Findings The presence of the cephalosporin compound in the corrosive medium shifted the corrosion potential of SS to much positive side, which enhances self-passivation of SS, and the shifting increased with increasing inhibitor concentration. The cephalosporin compounds worked as effective inhibitors with mainly anodic and the efficiency increase as cefotaxime < cephapirin < cefazolin. The inhibitors form a protective adsorbed layer, which enriches the surface content of Ni and Cr and thus assists the SS to be passive. Originality/value The antibiotics cephalosporins could be used as effective corrosion inhibitors for SS in acidic solutions containing sulfide ions. The inhibitors enhances the the passive oxide film of SS even in presence of aggressive ions such as sulfide ions.

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Basak, Subir, Ajoy Velayudhan, and Michael R. Ladisch. "Simulation of diauxic production of cephalosporin C by Cephalosporium acremonium: lag model for fed-batch fermentation." Biotechnology Progress 11, no. 6 (November 1995): 626–31. http://dx.doi.org/10.1021/bp00036a004.

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