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1.
Lett Appl Microbiol ; 75(1): 135-144, 2022 Jul.
Article in English | MEDLINE | ID: mdl-35344598

ABSTRACT

In this study, we aimed to analyse the spoilage potential of the isolated yeast, LAB and AAB species. Thus, 11 strains were inoculated at 0·3% (v/v) into a sterile filtered tchapalo and stored for 3 days at ambient temperature (27-30°C). All the tested strains grew well or remained stable except for Limosilactobacillus fermentum and Pediococcus acidilactici, which decreased throughout the storage time. A significant decrease of total soluble solids was observed only for Saccharomyces cerevisiae (from 7·8 to 5·8 °Brix) and Meyerozyma guilliermondii (from 7·8 to 5·5 °Brix). The tchapalo samples inoculated with the LAB strains Weissella paramesenteroides, P. acidilactici, L. fermentum and the yeast strain Candida tropicalis were judged similar to the control by the panellists. However, the strains of Lacticaseibacillus paracasei and Latilactobacillus curvatus (LAB), S. cerevisiae, M. guilliermondii and Kluyveromyces marxianus (yeasts) and Acetobacter pasteurianus and A. cerevisiae (AAB) induced the spoilage of the tchapalo appearance, smell and/or taste. In the spoiled tchapalo quantitative and qualitative modification of some volatile compounds (VOCs), such as lilac aldehyde, ethyl acetate, ethyl hexanoate, ethyl octanoate and phenethyl acetate, were observed. These results provide information about the microorganisms that need to be removed to extend the shelf life of tchapalo.


Subject(s)
Beer , Sorghum , Bacteria/genetics , Beer/microbiology , Cote d'Ivoire , Fermentation , Food Microbiology , Saccharomyces cerevisiae , Yeasts/genetics
2.
Lett Appl Microbiol ; 56(1): 44-50, 2013 Jan.
Article in English | MEDLINE | ID: mdl-23078634

ABSTRACT

UNLABELLED: The distribution and presence of hygiene indicator and pathogenic micro-organisms in 375 samples of attieke marketed in Côte d'Ivoire, and their roles in the food poisoning were evaluated. Microbiological analyses were carried out, which included the total viable bacteria, coliforms, Escherichia coli, Staphylococcus aureus, Salmonella, Bacillus spores, fungi and Clostridium perfringens. The results revealed that the viable bacteria counts ranged from 2·2 ± 1·2 × 10(5) to 3·4 ± 1·4 × 10(6) CFU g(-1), while the yeasts and the moulds counts ranged, respectively, from 2·4 ± 0·12 × 10(4) to 9·8 ± 0·4 × 10(5) CFU g(-1) and 1·3 ± 0·7 × 10(1) to 1·7 ± 0·7 × 10(2) CFU g(-1). Bacillus subtilis, Bacillus cereus, Staphylococcus aureus, Citrobacter freundi, Enterobacter amnigenus, Citrobacter youngae, Enterobacter aerogenes, Klebsiella pneumoniae, Serratia marcescens, Enterobacter agglomerans and Klebsiella oxytoca were the bacteria isolated, and Rhizopus spp., Mucor spp., Thamnidium spp., Fusarium spp., Moniliella spp. the fungi. Escherichia coli, Clostridium perfringens and Salmonella spp. were not found. The occurrence of some bacteria and fungi illustrate that attieke collected in Côte d'Ivoire markets may act as a reservoir of pathogenic micro-organisms for human. SIGNIFICANCE AND IMPACT OF STUDY: This study demonstrates the great need to carry out microbiological tests frequently on attieke and even more the need to apply correct HACCP system during the production. Attieke is especially a well-known product in West Africa; hence, it is extremely important to ensure an adequate microbiological quality to guarantee consumers health. Overall, the study highlighted the need for effective communication on microbiological food risks, proper instruction and supervision in food-handling procedures, greater education on food safety risks.


Subject(s)
Bacteria/isolation & purification , Food Microbiology , Fungi/isolation & purification , Manihot/microbiology , Bacteria/classification , Colony Count, Microbial , Cote d'Ivoire , Fermentation , Food Handling , Fungi/classification
3.
Mol Cell Probes ; 9(6): 391-7, 1995 Dec.
Article in English | MEDLINE | ID: mdl-8808309

ABSTRACT

The antifols, inhibitors of the dihydrofolate reductase (DHFR), such as pyrimethamine and proguanil, have been used against Plasmodium falciparum in the areas where chloroquine resistance is widespread. This use has selected resistant strains in Southeast Asia and South America. The resistance is correlated with point mutations in precise positions of the DHFR gene. A reliable semi-nested PCR diagnosis test was established and used to determine the genotypic features of 29 isolates of P. falciparum originating from Africa. The results obtained by the PCR technique were compared with those of the in vitro drug sensitivity test. Some isolates were found to be polyclonal. Among the mutations tested, only mutations on codon 108 which generate an asparagine induce a decrease in sensitivity to pyrimethamine and cycloguanil, whereas mutation on codon 59 strengthens resistance to both antifols. No mutation on codon 16 or codon 164 was found.


Subject(s)
Antimalarials/pharmacology , Folic Acid Antagonists/pharmacology , Plasmodium falciparum/drug effects , Polymerase Chain Reaction/methods , Proguanil/pharmacology , Protozoan Proteins/genetics , Pyrimethamine/pharmacology , Tetrahydrofolate Dehydrogenase/genetics , Animals , Base Sequence , Codon/genetics , DNA Mutational Analysis , DNA, Protozoan/genetics , Drug Resistance/genetics , Molecular Sequence Data , Plasmodium falciparum/enzymology , Plasmodium falciparum/genetics , Point Mutation , Protozoan Proteins/antagonists & inhibitors , Sensitivity and Specificity
4.
Exp Parasitol ; 80(3): 483-7, 1995 May.
Article in English | MEDLINE | ID: mdl-7729483

ABSTRACT

We describe here a rapid procedure to predict the resistance of Plasmodium falciparum to pyrimethamine or cycloguanil. The method consists of amplification by PCR of the DHFR gene followed by restriction enzyme digestion of codons 16 and 108. Three different enzymes are used to cut the wild-type, 108-threonine mutant, and 108-asparagine mutant gene. Since every natural antifolate-resistant isolate identified until now carries a mutation in codon 108, determination of the nature of this codon can predict the sensitivity of any P. falciparum isolate.


Subject(s)
Plasmodium falciparum/drug effects , Point Mutation , Pyrimethamine/pharmacology , Tetrahydrofolate Dehydrogenase/genetics , Triazines/pharmacology , Animals , Base Sequence , Codon/chemistry , Codon/genetics , DNA Primers/chemistry , Drug Resistance/genetics , Genes, Protozoan , Humans , Molecular Sequence Data , Plasmodium falciparum/genetics , Polymerase Chain Reaction , Proguanil , Restriction Mapping
5.
Nucleic Acids Res ; 18(12): 3489-93, 1990 Jun 25.
Article in English | MEDLINE | ID: mdl-2362804

ABSTRACT

We have cloned cDNAs encoding two variants of the elongation factor for protein synthesis in Xenopus laevis, called EF-1 alpha. One of these (42Sp50) is expressed exclusively in immature oocytes. It is one of two protein components of a 42S RNP particle that is very abundant in previtellogenic oocytes. The 42S RNP particle consists of various tRNAs, 5S RNA, 42Sp50 and a 5S RNA binding protein (42Sp43). A major function served by 42Sp50 appears to be the storage of tRNAs for later use in oogenesis and early embryogenesis. The second EF-1 alpha variant (EF-1 alpha O) is expressed mainly in oocytes but transiently in early embryogenesis as well. Its mRNA cannot be detected after neurulation in somatic cells. EF-1 alpha O is closely related to a third EF-1 alpha (EF-1 alpha S), discovered originally by Krieg et al. (1). EF-1 alpha S is expressed at low levels in oocytes but actively in somatic cells. The latter two proteins are very similar to known eukaryotic EF-1 alpha from other organisms and presumably function in their respective cell types to support protein synthesis.


Subject(s)
Gene Expression Regulation , Oocytes/metabolism , Peptide Elongation Factors/genetics , Ribonucleoproteins/genetics , Amino Acid Sequence , Animals , Base Sequence , Blotting, Northern , Cloning, Molecular , Genes , Liver/metabolism , Molecular Sequence Data , Peptide Elongation Factor 1 , Peptide Elongation Factors/biosynthesis , Sequence Homology, Nucleic Acid , Xenopus laevis
6.
FEBS Lett ; 223(2): 232-6, 1987 Nov 02.
Article in English | MEDLINE | ID: mdl-3666148

ABSTRACT

We have purified in SDS X.laevis thesaurin a (Mr 50,000) which is part of the 42 S storage particles. Its N-terminal amino acid is blocked and several peptides obtained by V8 protease treatment were purified and sequenced. As expected from one of the functional roles of the 42 S particles (tRNA binding, protection against deacylation and exchange with the ribosome), the amino acid sequence of thesaurin a was found to be closely related to that of the elongation factor EF-1 alpha. We suggest that all three proteins involved in 5 S RNA and tRNA storage in previtellogenic oocytes, TFIIIA, thesaurin a and thesaurin b, have a dual function: storage and a role in transcription or in protein synthesis.


Subject(s)
Oocytes/metabolism , Peptide Elongation Factors , Ribonucleoproteins/analysis , Xenopus laevis/physiology , Amino Acid Sequence , Animals , Molecular Sequence Data , Oogenesis , Peptide Elongation Factor 1 , Peptide Elongation Factors/metabolism , Ribonucleoproteins/metabolism
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