Isolation and characterization of the Omp-PA porin from Porphyromonas asaccharolytica, determination of the omp-PA gene sequence and prediction of Omp-PA protein structure

Anaerobe ◽  
2007 ◽  
Vol 13 (2) ◽  
pp. 74-82 ◽  
Author(s):  
Lana Magalashvili ◽  
Izabella Pechatnikov ◽  
Hannah M. Wexler ◽  
Yeshayahu Nitzan
2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Celosia Lukman ◽  
Christopher Yonathan ◽  
Stella Magdalena ◽  
Diana Elizabeth Waturangi

Abstract Objective This study was conducted to isolate and characterize lytic bacteriophages for pathogenic Escherichia coli from chicken and beef offal, and analyze their capability as biocontrol for several foodborne pathogens. Methods done in this research are bacteriophage isolation, purification, titer determination, application, determination of host range and minimum multiplicity of infection (miMOI), and bacteriophage morphology. Results Six bacteriophages successfully isolated from chicken and beef offal using EPEC and EHEC as host strain. Bacteriophage titers observed between 109 and 1010 PFU mL−1. CS EPEC and BL EHEC bacteriophage showed high efficiency in reduction of EPEC or EHEC contamination in meat about 99.20% and 99.04%. The lowest miMOI was 0.01 showed by CS EPEC bacteriophage. CI EPEC and BL EPEC bacteriophage suspected as Myoviridae family based on its micrograph from Transmission Electron Microscopy (TEM). Refers to their activity, bacteriophages isolated in this study have a great potential to be used as biocontrol against several foodborne pathogens.


1980 ◽  
Vol 35 (3-4) ◽  
pp. 209-212 ◽  
Author(s):  
B. Schöbel ◽  
W. Pollmann

Abstract The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 °C respectively. Divalent cations were not required for the enzyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. The Km-value is 0.70 mᴍ chlorogenic acid, the molecular weight 240000. The described enzyme is specific for chlorogenic acid. On the other hand a typical unspecific esterase like the pig liver esterases does not split chloro­genic acid. The isoelectric focusing reveals several isoenzymes of chlorogenase within a pI-range of 4.0-4.5.


1971 ◽  
Vol 24 (1) ◽  
pp. 179 ◽  
Author(s):  
IJ O'donnell

Proteins extracted from reduced and carboxymethylated feather keratins (SCM-keratins) have been studied by Harrap and Woods (1964a, 1964b, 1967). They have demonstrated the presence of electrophoretic heterogeneity amongst the proteins and have obtained a molecular weight of approximately 11,000 in agreement with earlier work of Woodin (1954). There was no indication of marked heterogeneity with respect to size. Using acid hydrolysis and determination of acetic acid produced they found an acetyl content of 1 �30 molesj104 g in the rachis off owl feathers. These were thought to be attached to primary amino groups since there were no O-acetyl groups. In the present paper the isolation and characterization of the predominant, and probably sole, amino-terminal tripeptide from goose feather calamus is described. Goose feather calamus was chosen because its extracted proteins had one of the simplest electrophoretic patterns of proteins from the feathers of a number of species (Harrap and Woods 1967).


1986 ◽  
Vol 28 (11) ◽  
pp. 1753-1760 ◽  
Author(s):  
Bruce E. Rittmann ◽  
LouAnn Crawford ◽  
Cynthia K. Tuck ◽  
Eun Namkung

1991 ◽  
Vol 57 (2) ◽  
pp. 147-152 ◽  
Author(s):  
Keith Dudley ◽  
Francis Shanahan ◽  
M. Burtenshaw ◽  
E. P. Evans ◽  
S. Ruddy ◽  
...  

SummaryThe mouse t complex on chromosome 17 is known to harbour many genes which have an important role in spermatogenesis. One of these, Tcp-1 has been cloned and shown to code for a protein probably essential for acrosome formation. During the isolation of a cDNA for Tcp-1 two other homologous sequences were recognized and described as Tcp-1x and Tcp-1y. In this paper we describe the isolation of a cDNA which has been shown by in situ hybridization to correspond to the Tcp-1x gene. Sequence analysis has confirmed that a 140 bp region of homology between Tcp-1 and Tcp-1x lies in the 3′ portion of both genes. Northern blotting has revealed that the Tcp-1x gene is expressed abundantly in liver where two transcripts are detectable and hybrid selection shows that the gene codes for a 37 kDa protein. A search of the DNA databases has failed to find any significant homology between Tcp-1x and any other sequences apart from Tcp-1.


2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Anna Krasowska ◽  
Anna Biegalska ◽  
Daria Augustyniak ◽  
Marcin Łoś ◽  
Malwina Richert ◽  
...  

Bacteriophages have been suggested as an alternative approach to reduce the amount of pathogens in various applications. Bacteriophages of various specificity and virulence were isolated as a means of controlling food-borne pathogens. We studied the interaction of bacteriophages withBacillusspecies, which are very often persistent in industrial applications such as food production due to their antibiotic resistance and spore formation. A comparative study using electron microscopy, PFGE, and SDS-PAGE as well as determination of host range, pH and temperature resistance, adsorption rate, latent time, and phage burst size was performed on three phages of theMyoviridaefamily and one phage of theSiphoviridaefamily which infectedBacillus subtilisstrains. The phages are morphologically different and characterized by icosahedral heads and contractile (SIOΦ, SUBω, and SPOσphages) or noncontractile (ARπphage) tails. The genomes of SIOΦ and SUBωare composed of 154 kb. The capsid of SIOΦ is composed of four proteins. Bacteriophages SPOσand ARπhave genome sizes of 25 kbp and 40 kbp, respectively. Both phages as well as SUBωphage have 14 proteins in their capsids. Phages SIOΦ and SPOσare resistant to high temperatures and to the acid (4.0) and alkaline (9.0 and 10.0) pH.


Author(s):  
O. G. Dawodu ◽  
O. R. Agbeni ◽  
V. Iwu

This study reports a modified SDS extraction technique for isolation of DNA from root tubers namely Dioscorea (yam), Manihot esculenta (cassava) and Colocasia esculenta (cocoyam). DNA extraction in many plants is very difficult because of secondary metabolites that interfere with DNA isolation procedure. Young fresh leaves were collected from the selected tubers and DNA extracted using SDS-extraction protocol, the DNA isolated from the extracted leaves was subjected to gel electrophoresis for determining their purity and concentration and PCR amplification was carried out on the extracted DNA, afterwards gel-electrophoresis was performed for molecular weight determination of the samples. DNA sequencing were performed on both reverse and forward using Sanger sequencing method which gave the nucleotide bases of the samples. DNA isolated by modified SDS protocol method was pure and highest level of purity was obtained from Manihot esculenta, Colocasia esculenta and Dioscorea which are 1.77, 1.72 and 1.20 with concentration of 537.7 ng/µl, 992.4 ng/µl and 149.8 ng/µl respectively. The DNA isolated from root tubers was pure and of good quality, and the isolated DNA was characterized by sequencing. The isolated DNA was successfully sequenced which coded for marker genes of the respective root tubers.


2011 ◽  
Vol 61 (9) ◽  
pp. 2151-2154 ◽  
Author(s):  
Isabelle Pagnier ◽  
Didier Raoult ◽  
Bernard La Scola

The analysis of three water samples from two cooling towers and one river allowed us to isolate three strains of a novel species of the class Alphaproteobacteria which is phylogenetically related to uncultured alphaproteobacteria. Based upon 16S rRNA gene sequence analysis and phenotypic characterization, we propose to name this novel species Reyranella massiliensis gen. nov., sp. nov., type strain 521T ( = CSUR P115T  = DSM 23428T). The most closely related cultivable micro-organism to this novel bacterium is a member of the genus Magnetospirillum.


2021 ◽  
Vol 2021 ◽  
pp. 1-11
Author(s):  
Eshetu Mekonnen ◽  
Ameha Kebede ◽  
Asefa Nigussie ◽  
Gessese Kebede ◽  
Mesfin Tafesse

Urease is an enzyme produced by ureolytic microorganisms which hydrolyzes urea into ammonia and carbon dioxide. Microbial urease has wide applications in biotechnology, agriculture, medicine, construction, and geotechnical engineering. Urease-producing microbes can be isolated from different ecosystems such as soil, oceans, and various geological formations. The aim of this study was to isolate and characterize rapid urease-producing bacteria from Ethiopian soils. Using qualitative urease activity assay, twenty urease-producing bacterial isolates were screened and selected. Among these, three expressed urease at high rates as determined by a conductivity assay. The isolates were further characterized with respect to their biochemical, morphological, molecular, and exoenzyme profile characteristics. The active urease-producing bacterial isolates were found to be nonhalophilic to slightly halophilic neutrophiles and aerobic mesophiles with a range of tolerance towards pH (4.0–10.0), NaCl (0.25—5%), and temperature (20–40°C). According to the API ZYM assays, all three isolates were positive for alkaline phosphatase, leucine aryl amidase, acid phosphatase, and naphthol_AS_BI_phosphohydrolase. The closest described relatives of the selected three isolates (Isolate_3, Isolate_7, and Isolate_11) were Bacillus paramycoides, Citrobacter sedlakii, and Enterobacter bugandensis with 16S rRNA gene sequence identity of 99.0, 99.2, and 98.9%, respectively. From the study, it was concluded that the three strains appear to have a relatively higher potential for urease production and be able to grow under a wider range of growth conditions.


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