Current Issue : July - September Volume : 2014 Issue Number : 3 Articles : 6 Articles
Bacillus coagulans, a revolutionary new friendly bacteria naturally occurring in the intestine. It is a spore-forming bacteria that make it the choice of probiotic with enormous clinical applications. B. coagulans is a notable exemption which, due to its sporulated form, lives without special handling and proliferates in the gastrointestinal environment rapidly. Due to its spore forming environment, B. coagulans is unaffected to most chemical and physical conditions e.g. Temperature, harsh and persists manufacturing, transport and storage with no loss of viable count. It does not require refrigeration condition and is stable at room temperature. B. coagulans has gained wide application as a biotherapeutic agent in treatment of various chronic diseases including gastrointestinal (GI) to non-GI tract infections. Through the keen references, on B. coagulans we have focused on safety, microbiological background, pharmacokinetics and clinical indications of B. coagulans....
The present study was conducted to test antimicrobial, in-vivo brine shrimp lethality and hemolytic assays of the\r\nhexane, ethyl acetate, chloroform, methanol and ethanolic extracts of Kalinga ornata. The antimicrobial effect of different extract\r\nof Kalinga ornata determined against ten pathogenic bacteria and fungi. All the extracts showed minimum zone of inhibition\r\nagainst Escherichia coli, Klebsiella pneumonia, Proteus mirabilis, Pseusdomonas aeruginosa, Salmonella typhi, Salmonella\r\nparatyphi, Staphyloccus aureus, Aspergillus flavus, A. niger, Candida albicans and Pencillium Sp. According to brine shrimp\r\nlethality test ten nauplii were added into three replicates of each concentration of the Kalinga ornata extract. After 24 hours the\r\nsurviving brine shrimp larvae were counted and LC50 was assessed. Results showed that the extract of Kalinga ornata was\r\npotent against the brine shrimp with LC50 values of 40, 80 and 100 ppm (?g/ml), respectively. The hemolytic activity was also\r\nestimated as 128 HU/mg chicken blood erythrocytes. This study indicated that bioactive components are present in the Kalinga\r\nornata and the results support new marine source for drug development....
Zinc finger nucleases (ZFNs) are associated with cell death and apoptosis by binding at countless undesired locations. This\ncytotoxicity is associated with the binding ability of engineered zinc finger domains to bind dissimilar DNA sequences with high\naffinity. In general, binding preferences of transcription factors are associated with significant degenerated diversity and complexity\nwhich convolutes the design and engineering of preciseDNA binding domains. Evolutionary success of natural zinc finger proteins,\nhowever, evinces that nature created specific evolutionary traits and strategies, such as modularity and rank-specific recognition to\ncope with binding complexity that are critical for creating clinical viable tools to preciselymodify the human genome. Our findings\nindicate preservation of general modularity and significant alteration of the rank-specific binding preferences of the three-finger\nbinding domain of transcription factor SP1 when exchanging amino acids in the 2nd finger....
Increased frequency of methicillin-resistant Staphylococcus aureus (MRSA) in hospitalized patients requires rapid and reliable\ncharacterization of isolates for control of MRSA spread in hospitals. This study evaluated polymerase chain reaction-restriction\nfragment length polymorphism (PCR-RFLP) as a molecular typing technique for MRSA strains on the basis of protein A (spa)\nand coagulase (coa) gene polymorphisms to verify their ability in assessing the relatedness of isolates. Seventy-five MRSA isolates,\nfrom different ICUs of Alexandria University Main Hospital, were characterized using antibiotyping and PCR-RFLP analysis of\ncoa and spa genes. Thirty-two antibiotypes were identified. coa gene PCR generated 3 types and 10 subtypes of band patterns.\nHaeIII restriction digestion of amplified coa gene products produced 5 major banding patterns and 12 subtypes. spa gene PCR\nproducts generated 4 major and 11 minor types, and their HaeII restriction digestion showed 5 major and 12 minor banding\npatterns. The combined coa and spa RFLP patterns generated 22 combined R types. Typing using coa PCR and PCR-RFLP had\nthe same discriminatory index (DI) value (0.64), which was comparable to that of both spa PCR and PCR-RFLP techniques (0.68).\nThe combined grouping increased the DI value to 0.836.The current study revealed that testing for multiple gene polymorphisms\nis more useful for local epidemiologic purposes....
Klebsiella pneumoniae ML2011, amultiresistant isolate,was isolated fromtheMilitaryHospital ofTunis (Tunisia).Thedetermination\nof the minimal inhibitory concentrations exhibited by K. pneumoniae ML2011 was performed by Etest. The crude extract of the\nisolates contains four different �Ÿ-lactamases with pI 5.5, 7.3, 7.6, and 8.6. Only the �Ÿ-lactamases with pI 7.3 and pI 8.6were transferred\nby transformation and conjugation experiment.Molecular characterization of these genes was performed by PCR and sequencing.\nThe chromosomal �Ÿ-lactamases are TEM (pI 5.5) and SHV-1 (7.6). CTX-M-28 (pI 8.6) and the novel variant of SHV named SHV-\n104 (pI 7.3) were encoded by bla gene located on a 50 kb highly conjugative plasmid. The SHV-104 �Ÿ-lactamase was produced\nin E. coli and purified. Its profile of activity was determined. Compared to SHV-1, SHV-104 contains one mutation, R202S. Their\nkinetic parameters were similar except for cefotaxime.The analysis of the predicted structure of SHV-104 indicated that the R202S\nmutation suppresses a salt bridge present in SHV-1. Therefore, the overall flexibility of the protein increased and might improve the\nhydrolysis of cefotaxime. We can conclude that the multiresistant phenotype of K. pneumoniae ML2011 strain is mainly linked to\nthe production of CTX-M-28 since SHV-104 possesses a narrow spectrum of activity....
Chrysosporium sp. strain isolated from soil using hair baiting technique was tested for its abilities to hydrolyze the hair keratin. It was able to produce highest keratinase i.e. 336 U/ml after 9 days of incubation with a total protein content of 1.19 mg/ml and 16.7 mg/ml of cystein. The enzyme was partially purified by ammonium sulphate fractionation and DEAE-cellulose column chromatography. A purification fold about 7.13 with a recovery of 14.92% was obtained. Specific activity of this partially purified enzyme was 1415.73 U/ml. The optimal pH and temperature for keratinolytic activity was approximately 9 and 50°C respectively. This keratinase was inhibited by addition of PMSF whereas the enzyme activity was enhanced in presence of EDTA and 1,10 phenanthroline at a concentration of 5 mM and 1 mM concentration. Strain Chrysosporium sp., therefore, shows great promise of finding potential applications in keratin hydrolysis and keratinase production....
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