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Journal articles on the topic 'Bacitracin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Blackard, W. G., C. Ludeman, and J. Stillman. "Role of hepatocyte plasma membrane in insulin degradation." American Journal of Physiology-Endocrinology and Metabolism 248, no. 2 (1985): E194—E202. http://dx.doi.org/10.1152/ajpendo.1985.248.2.e194.

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An important role of the cell membrane in insulin degradation by cultured rat hepatocytes is supported by studies using the surface-active antibiotic bacitracin. Bacitracin inhibited degradation of cell-associated insulin (both randomly and A14 labeled) by 80–90% at 15 degrees C and by 60% at 37 degrees C. At 37 degrees C, inhibition of degradation was observed only with bacitracin present during dissociation and was accompanied by a compensatory increase in release of trichloroacetic acid (TCA)-precipitable insulin. This profile suggests inhibition of insulin degradation on the membrane after

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2

&NA;. "Bacitracin see Polymixin B + bacitracin." Reactions Weekly &NA;, no. 327 (1990): 4. http://dx.doi.org/10.2165/00128415-199003270-00011.

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3

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 693 (1998): 6. http://dx.doi.org/10.2165/00128415-199806930-00015.

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4

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 723 (1998): 7. http://dx.doi.org/10.2165/00128415-199807230-00020.

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5

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1135 (2007): 9. http://dx.doi.org/10.2165/00128415-200711350-00029.

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6

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1356 (2011): 9–10. http://dx.doi.org/10.2165/00128415-201113560-00026.

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7

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 441 (1993): 6. http://dx.doi.org/10.2165/00128415-199304410-00016.

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8

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 668 (1997): 6. http://dx.doi.org/10.2165/00128415-199706680-00015.

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9

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 828 (2000): 8. http://dx.doi.org/10.2165/00128415-200008280-00011.

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10

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1218 (2008): 7–8. http://dx.doi.org/10.2165/00128415-200812180-00020.

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11

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1223 (2008): 7. http://dx.doi.org/10.2165/00128415-200812230-00022.

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12

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1085 (2006): 9. http://dx.doi.org/10.2165/00128415-200610850-00027.

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13

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 1257 (2009): 10. http://dx.doi.org/10.2165/00128415-200912570-00029.

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14

&NA;. "Bacitracin." Reactions Weekly &NA;, no. 333 (1991): 4. http://dx.doi.org/10.2165/00128415-199103330-00013.

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15

&NA;. "Bacitracin see Neomycin/bacitracin/polymixin B." Reactions Weekly &NA;, no. 335 (1991): 4. http://dx.doi.org/10.2165/00128415-199103350-00011.

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16

Ohki, Reiko, Kozue Tateno, Youji Okada, et al. "A Bacitracin-Resistant Bacillus subtilis Gene Encodes a Homologue of the Membrane-Spanning Subunit of the Bacillus licheniformis ABC Transporter." Journal of Bacteriology 185, no. 1 (2003): 51–59. http://dx.doi.org/10.1128/jb.185.1.51-59.2003.

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ABSTRACT Bacitracin is a peptide antibiotic nonribosomally produced by Bacillus licheniformis. The bcrABC genes which confer bacitracin resistance to the bacitracin producer encode ATP binding cassette (ABC) transporter proteins, which are hypothesized to pump out bacitracin from the cells. Bacillus subtilis 168, which has no bacitracin synthesizing operon, has several genes homologous to bcrABC. It was found that the disruption of ywoA, a gene homologous to bcrC, resulted in hypersensitivity to bacitracin. Resistance to other drugs such as surfactin, iturin A, vancomycin, tunicamycin, gramici

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17

&NA;. "Neomycin/bacitracin." Reactions Weekly &NA;, no. 399 (1992): 10. http://dx.doi.org/10.2165/00128415-199203990-00045.

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18

&NA;. "Bacitracin/colistin." Reactions Weekly &NA;, no. 1081 (2005): 8. http://dx.doi.org/10.2165/00128415-200510810-00023.

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19

&NA;. "Bacitracin/neomycin." Reactions Weekly &NA;, no. 1082 (2005): 8. http://dx.doi.org/10.2165/00128415-200510820-00019.

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20

&NA;. "Bacitracin + clioquinol." Reactions Weekly &NA;, no. 348 (1991): 5. http://dx.doi.org/10.2165/00128415-199103480-00008.

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21

Brod, Bruce A. "Bacitracin Anaphylaxis." American Journal of Contact Dermatitis 7, no. 3 (1996): 193. http://dx.doi.org/10.1097/01634989-199609000-00015.

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22

Brod, Bruce A. "Bacitracin Anaphylaxis." Dermatitis 7, no. 3 (1996): 193. http://dx.doi.org/10.1097/01206501-199609000-00015.

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23

BROD, B. "Bacitracin anaphylaxis." American Journal of Contact Dermatitis 7, no. 3 (1996): 193. http://dx.doi.org/10.1016/s1046-199x(96)90014-7.

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24

Tsuda, Hiromasa, Yoshihisa Yamashita, Yukie Shibata, Yoshio Nakano, and Toshihiko Koga. "Genes Involved in Bacitracin Resistance in Streptococcus mutans." Antimicrobial Agents and Chemotherapy 46, no. 12 (2002): 3756–64. http://dx.doi.org/10.1128/aac.46.12.3756-3764.2002.

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ABSTRACT Streptococcus mutans is resistant to bacitracin, which is a peptide antibiotic produced by certain species of Bacillus. The purpose of this study was to clarify the bacitracin resistance mechanism of S. mutans. We cloned and sequenced two S. mutans loci that are involved in bacitracin resistance. The rgp locus, which is located downstream from rmlD, contains six rgp genes (rgpA to rgpF) that are involved in rhamnose-glucose polysaccharide (RGP) synthesis in S. mutans. The inactivation of RGP synthesis in S. mutans resulted in an approximately fivefold-higher sensitivity to bacitracin

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25

Manson, Janet M., Stefanie Keis, John M. B. Smith, and Gregory M. Cook. "Acquired Bacitracin Resistance in Enterococcus faecalis Is Mediated by an ABC Transporter and a Novel Regulatory Protein, BcrR." Antimicrobial Agents and Chemotherapy 48, no. 10 (2004): 3743–48. http://dx.doi.org/10.1128/aac.48.10.3743-3748.2004.

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ABSTRACT Bacitracin resistance (bacitracin MIC, ≥256 μg ml−1) has been reported in Enterococcus faecalis, and in the present study we report on the genetic basis for this resistance. Mutagenesis was carried out with transposon Tn917 to select for E. faecalis mutants with decreased resistance to bacitracin. Two bacitracin-sensitive mutants (MICs, 32 μg ml−1) were obtained and Tn917 insertions were mapped to genes designated bcrA and bcrB. The amino acid sequences of BcrA (ATP-binding domain) and BrcB (membrane-spanning domain) are predicted to constitute a homodimeric ATP-binding cassette (ABC)

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26

Han, Xiaoyan, Xiang-Dang Du, Luke Southey, et al. "Functional Analysis of a Bacitracin Resistance Determinant Located on ICECp1, a Novel Tn916-Like Element from a Conjugative Plasmid in Clostridium perfringens." Antimicrobial Agents and Chemotherapy 59, no. 11 (2015): 6855–65. http://dx.doi.org/10.1128/aac.01643-15.

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ABSTRACTBacitracins are mixtures of structurally related cyclic polypeptides with antibiotic properties. They act by interfering with the biosynthesis of the bacterial cell wall. In this study, we analyzed an avian necrotic enteritis strain ofClostridium perfringensthat was resistant to bacitracin and produced NetB toxin. We identified a bacitracin resistance locus that resembled a bacitracin resistance determinant fromEnterococcus faecalis. It contained the structural genesbcrABDand a putative regulatory gene,bcrR. Mutagenesis studies provided evidence that bothbcrAandbcrBare essential for ba

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27

Smith, Janet D., and Gordon T. Bolger. "Selective inhibition of [3H]nitrendipine binding to brain and cardiac membranes by bacitracin." Canadian Journal of Physiology and Pharmacology 67, no. 12 (1989): 1591–95. http://dx.doi.org/10.1139/y89-255.

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The effects of bacitracin were investigated on [3H]nitrendipine binding to rat brain and cardiac membranes in a low ionic strength (5 mM Tris–HCl) buffer. Bacitracin inhibited [3H]nitrendipine binding to rat brain and cardiac membranes with IC50 values of 400 ± 100 and 4600 ± 400 μg/mL, respectively. Scatchard analysis in brain membranes revealed that bacitracin inhibited [3H]nitrendipine binding primarily by reducing the Bmax but also by producing a small increase in the Kd. In brain membranes, Na+ (100 mM) and Ca2+ (2 mM) reduced the potency of bacitracin to inhibit [3H]nitrendipine binding

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28

Cao, Min, та John D. Helmann. "Regulation of the Bacillus subtilis bcrC Bacitracin Resistance Gene by Two Extracytoplasmic Function σ Factors". Journal of Bacteriology 184, № 22 (2002): 6123–29. http://dx.doi.org/10.1128/jb.184.22.6123-6129.2002.

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ABSTRACT Bacitracin resistance is normally conferred by either of two major mechanisms, the BcrABC transporter, which pumps out bacitracin, or BacA, an undecaprenol kinase that provides C55-isoprenyl phosphate by de novo synthesis. We demonstrate that the Bacillus subtilis bcrC (ywoA) gene, encoding a putative bacitracin transport permease, is an important bacitracin resistance determinant. A bcrC mutant strain had an eightfold-higher sensitivity to bacitracin. Expression of bcrC initiated from a single promoter site that could be recognized by either of two extracytoplasmic function (ECF) σ f

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29

Beckman, Joshua M., Ernest K. Amankwah, Lisa L. Tetreault, Sharon A. Perlman, and Gerald F. Tuite. "Complications associated with bacitracin powder in surgical wounds." Journal of Neurosurgery: Pediatrics 16, no. 6 (2015): 719–25. http://dx.doi.org/10.3171/2015.4.peds14699.

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OBJECT There has been renewed interest in the application of concentrated antibiotic powder to surgical wounds as a method to decrease infection rates. While there is substantial medical literature describing the effectiveness and complications associated with vancomycin and gentamycin powders, very little has been reported regarding the safety and effectiveness of bacitracin powder in surgical wounds. In this paper the authors report their detailed analysis of potential bacitracin powder-related complications in a population of pediatric patients who underwent shunt surgery. METHODS A detaile

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30

Wang, Xitao, and Mohammad Asghar. "Protein disulfide isomerase regulates renal AT1 receptor function and blood pressure in rats." American Journal of Physiology-Renal Physiology 313, no. 2 (2017): F461—F466. http://dx.doi.org/10.1152/ajprenal.00580.2016.

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The role and mechanism of renal protein disulfide isomerase (PDI) in blood pressure regulation has not been tested before. Here, we test this possibility in Sprague-Dawley rats. Rats were treated with PDI inhibitor bacitracin (100 mg·kg−1 ip·day−1 for 14 days), and then blood pressure and renal angiotensin II type 1 (AT1) receptor function were determined in anesthetized rats. Renal AT1 receptor function was determined as the ability of candesartan (an AT1 receptor blocker) to increase diuresis and natriuresis. A second set of vehicle- and bacitracin-treated rats was used to determine biochemi

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31

HAAVIK, H. I. "Studies on the Formation of Bacitracin by Bacillus licheniformis: Effect of Glucose." Microbiology 81, no. 2 (2000): 383–90. http://dx.doi.org/10.1099/00221287-81-2-383.

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Summary: The production of bacitracin by Bacillus licheniformis closely paralleled growth in a synthetic medium without glucose. Glucose inhibited bacitracin production during the first hours of growth, whereas growth was not affected. Bacitracin was produced mainly during the later stages of growth. Formation of bacitracin was apparently not under catabolite repression control by glucose since the inhibitory effect of glucose upon the early bacitracin production was prevented by neutralizing the culture fluid with CaCO3. The inhibitory effect of glucose may be due to the low pH created by its

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32

Zhu, Ziyu, Leonie Schnell, Bastian Müller, Martin Müller, Panagiotis Papatheodorou, and Holger Barth. "The Antibiotic Bacitracin Protects Human Intestinal Epithelial Cells and Stem Cell-Derived Intestinal Organoids from Clostridium difficile Toxin TcdB." Stem Cells International 2019 (August 5, 2019): 1–8. http://dx.doi.org/10.1155/2019/4149762.

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Bacitracin is an established antibiotic for local application and inhibits the cell wall synthesis of Gram-positive bacteria. Recently, we discovered a completely different mode of action of bacitracin and reported that this drug protects human cells from intoxication by a variety of medically relevant bacterial protein toxins including CDT, the binary actin ADP-ribosylating toxin of Clostridium (C.) difficile. Bacitracin prevents the transport of CDT into the cytosol of target cells, most likely by inhibiting the transport function of the binding subunit of this toxin. Here, we tested the eff

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33

Netland, Peter A., James E. Baumgartner, and Brian T. Andrews. "Intraoperative Anaphylaxis after Irrigation with Bacitracin: Case Report." Neurosurgery 21, no. 6 (1987): 927–28. http://dx.doi.org/10.1227/00006123-198712000-00026.

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Abstract We report a case of anaphylaxis caused by irrigation with a bacitracin solution during lumbar laminectomy. The patient had been exposed to bacitracin during a previous anterior cervical discectomy. We recommend avoiding the use of irrigation solutions containing bacitracin in patients with previous systemic exposure to this antibiotic.

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34

Lin, Kuei-Hung, and Yu-Hsiang Yu. "Evaluation of Bacillus licheniformis-Fermented Feed Additive as an Antibiotic Substitute: Effect on the Growth Performance, Diarrhea Incidence, and Cecal Microbiota in Weaning Piglets." Animals 10, no. 9 (2020): 1649. http://dx.doi.org/10.3390/ani10091649.

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This study investigated the potential of a Bacillus licheniformis-fermented feed additive (BLF) as an antibiotic substitute in weaning piglets. Ninety-six crossbred piglets were randomly allotted into four treatments with three replicate pens per treatment and eight pigs per pen. Piglets were fed diets as follows: a basal diet as control, a basal diet supplemented with bacitracin (30 mg/kg of bacitracin methylene disalicylate), a basal diet supplemented with BLF (1 g/kg of the Bacillus licheniformis-fermented feed additive), and a basal diet supplemented with bacitracin and BLF (15 mg/kg of ba

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35

Harel, Yael Meller, Adriana Bailone, and Eitan Bibi. "Resistance to Bacitracin as Modulated by an Escherichia coli Homologue of the Bacitracin ABC Transporter BcrC Subunit from Bacillus licheniformis." Journal of Bacteriology 181, no. 19 (1999): 6176–78. http://dx.doi.org/10.1128/jb.181.19.6176-6178.1999.

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ABSTRACT A small open reading frame from the Escherichia colichromosome, bcrC EC, encodes a homologue to the BcrC subunit of the bacitracin permease from Bacillus licheniformis. We show that disruption of the chromosomalbcrC EC gene causes bacitracin sensitivity and, conversely, that BcrCEC confers bacitracin resistance when expressed from a multicopy plasmid.

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36

Wang, Lin, Liu Liu, and Xiaotong Zhou. "Bacitracin-Ag Nanoclusters as a Novel Antibacterial Agent Combats Shigella flexneri by Disrupting Cell Membrane and Inhibiting Biofilm Formation." Nanomaterials 11, no. 11 (2021): 2928. http://dx.doi.org/10.3390/nano11112928.

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A novel nanomaterial Bacitracin-Ag Nanoclusters (Bacitracin-AgNCs) was formed to achieve a better antibacterial effect on Shigella flexneri which poses a serious threat to human health. In the current study, X-ray photoelectron spectrometer (XPS), Fourier transform infrared (FTIR), field-emission scanning electron microscopy (FESEM), high resolution transmission electron microscopy (HR-TEM) and thermal gravimetric analysis (TGA) were used to characterize the properties of composited Bacitracin-AgNCs. Furthermore, the inhibitory effects of Bacitracin-AgNCs against S. flexneri were explored, and

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37

Chapnick, Edward K., Jeremy D. Gradon, Barry Kreiswirth, et al. "Comparative Killing Kinetics of Methicillin-Resistant Staphylococcus aureus by Bacitracin or Mupirocin." Infection Control & Hospital Epidemiology 17, no. 3 (1996): 178–80. http://dx.doi.org/10.1017/s0195941700006548.

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AbstractThe in vitro activities of bacitracin and mupirocin were compared for seven different strains of methicillin-resistant Staphylococcus aureus. Six of seven strains showed bacitracin minimum inhibitory concentrations (MICs) of 0.5 to 1.0 units/mL, and all seven had mupirocin MICs of 0.5 to 2 μg/mL. Time-kill studies revealed 2.6- to 4.5-log reduction in 24 hours with strains susceptible to bacitracin (4 units/mL) and 0 to 2.2 reduction with mupirocin (16 μg/mL). Bacitracin should be considered further for in vivo studies because of enhanced bacteriocidal effect and lower cost.

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38

Santativongchai, Pitchaya, Phitsanu Tulayakul, Yinduo Ji, and Byeonghwa Jeon. "Synergistic Potentiation of Antimicrobial and Antibiofilm Activities of Penicillin and Bacitracin by Octyl Gallate, a Food-Grade Antioxidant, in Staphylococcus epidermidis." Antibiotics 11, no. 12 (2022): 1775. http://dx.doi.org/10.3390/antibiotics11121775.

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Staphylococcus epidermidis is a major nosocomial pathogen that frequently forms biofilms on indwelling medical devices. This study aimed to investigate the synergistic antimicrobial and antibiofilm activities of octyl gallate (OG) in combination with penicillin and bacitracin against S. epidermidis. Antimicrobial synergy was assessed by conducting checkerboard titration assays, and antibiofilm activity was determined with biofilm assays and fluorescence microscopy analysis. The presence of 8 µg/mL of OG increased both the bacteriostatic and bactericidal activities of penicillin and bacitracin

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39

&NA;. "Polymixin B + bacitracin." Reactions Weekly &NA;, no. 327 (1990): 8. http://dx.doi.org/10.2165/00128415-199003270-00043.

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40

&NA;. "Bacitracin/corticosteroids/neomycin." Reactions Weekly &NA;, no. 1291 (2010): 10. http://dx.doi.org/10.2165/00128415-201012910-00029.

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41

Podlesek, Z., and A. Comino. "Antagonists of bacitracin." Letters in Applied Microbiology 19, no. 2 (1994): 102–4. http://dx.doi.org/10.1111/j.1472-765x.1994.tb00916.x.

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42

Webster, Gregory K. "Liquid Chromatographic Analysis of Bacitracin Methylene Disalicylate in Feed." Journal of AOAC INTERNATIONAL 80, no. 4 (1997): 732–36. http://dx.doi.org/10.1093/jaoac/80.4.732.

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Abstract Because of its peptide structure, bacitracin is not chemically distinct from many matrixes such as feeds or residue samples. Thus, bacitracin must be isolated from the matrix components or chemically altered to form a distinct component. Because of the complexity of this problem, bacitracin is still analyzed almost exclusively by microbiological methods. However, advances in solid-phase extraction has made sample isolation from the matrix much more practical. In this investigation both strong-cation exchange and C8 columns were used to isolate bacitracin for liquid chromatographic (LC

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43

Aslanli, Aysel, Maksim Domnin, Nikolay Stepanov, and Elena Efremenko. "“Universal” Antimicrobial Combination of Bacitracin and His6-OPH with Lactonase Activity, Acting against Various Bacterial and Yeast Cells." International Journal of Molecular Sciences 23, no. 16 (2022): 9400. http://dx.doi.org/10.3390/ijms23169400.

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The effect of Bacitracin as an antibiotic acting against Gram-positive bacterial cells was evaluated in combination with hexahistidine-containing organophosphate hydrolase (His6-OPH), possessing lactonase activity against various N-acylhomoserine lactones produced by most Gram-negative bacteria as quorum-sensing molecules. The molecular docking technique was used to obtain in silico confirmation of possible interactions between molecules of His6-OPH and Bacitracin as well as the absence of a significant influence of such interactions on the enzymatic catalysis. The in vitro experiments showed

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Andrews, Barry J., Alexandru C. Vasile-Bugarin, Rhodica P. Vasiliu, Gheorge H. Jipa, Dan Panitescu, and Jorgen R. Ronnevig. "Chemotherapy for Giardiasis: Randomized Clinical Trial of Bacitracin, Bacitracin Zinc, and a Combination of Bacitracin Zinc with Neomycin." American Journal of Tropical Medicine and Hygiene 52, no. 4 (1995): 318–21. http://dx.doi.org/10.4269/ajtmh.1995.52.318.

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45

Stanley Chibuzor Ikpa, Precious Chukwuemeka Isima, Chibuzo Nwokafor, et al. "Effects of varied culture conditions on crude bacitracin produced by Bacillus subtilis isolated from the soil." Magna Scientia Advanced Biology and Pharmacy 8, no. 1 (2023): 001–8. http://dx.doi.org/10.30574/msabp.2023.8.1.0095.

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Aim: To determine the effects subjecting Bacillus subtilis to different cultural conditions will have on the crude Bacitracin produced in inhibiting the growth of known susceptible organisms. Method: Bacillus subtilis known to be a bacitracin producer was isolated from the soil and identified. The isolate was used to produce bacitracin under various culture conditions with peptone water serving as a basal fermentation medium. The resultant crude bacitracin produced was checked for its antimicrobial activity against Staphylococcus aureus by using the agar well diffusion method. Culture conditio

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46

Podlesek, Zdravko, Blagajana Herzog, and Aleksandra Comino. "Amplification of bacitracin transporter genes in the bacitracin producing Bacillus licheniformis." FEMS Microbiology Letters 157, no. 1 (2006): 201–5. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12774.x.

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47

Khattak, Rumana Zaib, Asif Nawaz, Maha Abdallah Alnuwaiser, et al. "Formulation, In Vitro Characterization and Antibacterial Activity of Chitosan-Decorated Cream Containing Bacitracin for Topical Delivery." Antibiotics 11, no. 9 (2022): 1151. http://dx.doi.org/10.3390/antibiotics11091151.

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(1) Background: Bacitracin is a broad spectrum antibiotic that is used against various microorganisms. Chitosan is a natural polymer that has been widely investigated as an antimicrobial agent for preventing and treating infections owing to its intrinsic antimicrobial properties, as well as its ability to effectively deliver extrinsic antimicrobial compounds to infected areas. Topical drug delivery offers important benefits for improving the therapeutic effect and reducing systemic side effects of administered compounds/drugs. The topical use of chitosan-decorated bacitracin-loaded cream impro

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48

Soto, Norberto E., Ashok Vaghjimal, Annette Stahl-Avicolli, John R. Protic, Larry I. Lutwick, and Edward K. Chapnick. "Bacitracin Versus Mupirocin for Staphylococcus aureus Nasal Colonization." Infection Control & Hospital Epidemiology 20, no. 05 (1999): 351–53. http://dx.doi.org/10.1086/501633.

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AbstractWe performed a randomized prospective study of 5-day treatment with topical mupirocin or bacitracin for the elimination ofStaphylococcus aureusnasal colonization in healthcare workers (HCWs). Nasal cultures were obtained from 141 HCWs, 37 (26%) of whom showed Saureus.After 72 to 96 hours of treatment, the organism was eradicated in 15 (94%) of 16 by mupirocin and in 8 (44%) of 18 by bacitracin (P=.0031). Similar efficacy was demonstrated at 30 days. Mupirocin may be more effective than bacitracin for eradication of Saureusin healthy HCWs.

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49

Gebhard, Susanne, Chong Fang, Aishath Shaaly, et al. "Identification and Characterization of a Bacitracin Resistance Network in Enterococcus faecalis." Antimicrobial Agents and Chemotherapy 58, no. 3 (2013): 1425–33. http://dx.doi.org/10.1128/aac.02111-13.

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ABSTRACTResistance ofEnterococcus faecalisagainst antimicrobial peptides, both of host origin and produced by other bacteria of the gut microflora, is likely to be an important factor in the bacterium's success as an intestinal commensal. The aim of this study was to identify proteins with a role in resistance against the model antimicrobial peptide bacitracin. Proteome analysis of bacitracin-treated and untreated cells showed that bacitracin stress induced the expression of cell wall-biosynthetic proteins and caused metabolic rearrangements. Among the proteins with increased production, an AT

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50

Shete P.B, Pharne A.G, and Pathade G.R. "Biosynthesis of Bacitracin in Solid-state Fermentation using Different Substrates." Ecology, Environment and Conservation 30, Suppl (2024): 292–95. http://dx.doi.org/10.53550/eec.2024.v30i02s.060.

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A Bacillus isolate was obtained from soil sample. It was then studied for its cultural, morphological and biochemical characteristics. The isolate was tentatively identified as Bacillus subtilis. For solid-state fermentation of bacitracin, the isolate was grown on basal medium. Fermentation was carried out SSF using three different solid substrates, wheat bran, rice husk and defatted cotton seed oil cake. Bacitracin produced was detected by TLC with standard bacitracin. The product formed in wheat bran showed greater inhibitory activity against test organism i.e. Micrococcus luteus with 20mm d

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