ISSN 2736-1756
Research Article
Advanced Journal of Microbiology Research Vol. 2010
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2010 International Scholars Journals
Full Length Research Paper
Production cellulase by different co-culture of Aspergillus niger and Tricoderma viride from waste paper
Ali A. Juwaied, Suhad Adnan and Ahmed Abdulamier Hussain Hussain Al-Amiery*
Department of Applied Science, Biochemical Division, University of Technology, Baghdad, Iraq.
Accepted 16 April, 2010
Abstract
In Iraq, there is attempts to transfer the various industrial carbon waste to veterinary proteins depend on microorganisms by using of chemical process. Five different co-culture combinations (1:1 ratio, 1 × 106 conidia)of Aspergillus niger and Trichoderma viride, mixing of A. niger and T. viride, in 24 and 48 h old monocultures of Aspergillus similar mixing of A. in 24 and 48 h old monoculture of Trichoderma and the monocultures of both were evaluated for their potential performance of cellulases production. The study indicates that the cellulases obtained from compatible mixed cultures simultaneous mixing of both fungi have more enzyme activity as compared to their pure cultures and other combinations. The fermentation experiments were performed in solid stat fermentation (SSF). Incubation time, carbon sources and initial pH of fermentation medium was optimized with simultaneous mixed culture. It was revealed that the newspaper at pH = 5 and 40°C was the best source of carbon for the enhanced production of cellulase in the compatible mixed culture experiments after 8 days of incubation with 5.70 U/ml. Based on the reported results, it may be concluded that industrial carbon waste can be a potential substrate for production of cellulase, incorporation of co-culturing A. niger and T. viride. The aim of this work is to produce of Cellulase from waste paper and reduce the pollution.
Key words: Aspergillus niger, Tricoderma viride, cellulase, culture.
Suhad Adnan and Ahmed Abdulamier Hussain Hussain Al-Amiery*, Ali A. Juwaied
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2010
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2010 International Scholars Journals
Full Length Research Paper
A specific inhibitory protein to a restriction enzyme from Saccharomyces cerevisiae
Mukaram Shikara*
Biotechnology Division, Department of Applied Sciences, University of Technology, Baghdad, Iraq. E-mail: [email protected].
Accepted 22 May, 2010
Abstract
A specific protein inhibitor for the restriction enzyme (SacC1) has been purified from Saccharomyces cerevisiae approximately 21,000 fold and its inhibitory properties have been characterized. The isoelectric points (pI) of SacCI and its inhibitor are 9.0 and 5.22, respectively. The molecular weight of SacC1, the inhibitor and SacC1-inhibitor complex were estimated by gel filtration on a Sephadex G-100 column to be 64,000, 32,000 and 85,000, respectively. The inhibitor protein inhibits SacC1 catalytic activities efficiently, but has no effect on other restriction enzymes tested. Inhibition does not occur unless SacC1 enzyme is exposed to the inhibitor protein prior to the reaction of the enzyme with DNA. The inhibitory activity is independent of temperature. The inhibition increased linearly with the addition of inhibitor to various amounts of SacC1, up to 85% inhibition. The slope of inhibition was constant irrespective of the initial amount of SacC1 and Ki value of 3.45 x 10-12 was obtained. The inhibitor interacts strongly with SacC1 and this interaction could increase the stability of the complex, possibly manifesting itself as SacC1 decreases in the dissociation rate due to the electrostatic attraction between the two groups or the stability may increase by potentially stronger electrostatic interaction. The conformational specificity between SacC1 and its inhibitor seems to be essential for their interaction. The extremely strong affinity of the inhibitor to SacC1 is remarkable and stronger than the affinity of several restriction enzymes.
Key words: Saccharomyces cerevisiae, inhibitor, protein, restriction enzyme, yeast, purification, Ki.
Mukaram Shikara*
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2010
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2010 International Scholars Journals
Full Length Research Paper
Studies on the mycoflora associated with sugarcane factory waste and pollution of River Nile in upper Egypt
A.H.M. El-Said1*, T. H. Sohair1 and A. G. El-Hadi2
1Department of Botany, Faculty of Science, South Valley University, Qena, Egypt.
2Department of Botany, Faculty of Science, Az-Zawiyah University, Libya.
Accepted 24 February, 2010
Abstract
Sixty-nine species and four varieties which belong to twenty eight genera of terrestrial fungi were recovered from polluted and nonpolluted water and mud samples on glucose and cellulose-Czapek's agar at 28˚C. The most common species from the two substrates on the two types of media were Aspergillus flavus, Aspergillus fumigatus, Aspergillus niger, Cladosporium cladosporioides, Fusarium oxysporum, Mycosphaerella tassiana and Penicillium chrysogenum. Twenty-six species belonging to 14 genera were isolated from polluted (26 species and 14 genera) and nonpolluted (17 and 10) mud samples on sabouraud’s dextrose agar at 28°C. The most prevalent species were Acremonium retiulum, Alternaria alternata, A. flavus, Aphanoascus fulvescens, Aspergillus terreus, Aphanoascus sp., Penicillium funiculosum and Stachybotrys chartarum.
Key words: Pollution, River Nile, terrestrial fungi and keratinophilic fungi.
A.H.M. El-Said*, T. H. Sohair and A. G. El-Hadi
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2010
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2010 International Scholars Journals
Full Length Research Paper
Antifungal activity of extracts obtained from actinomycetes
Harpreet Sharma and Leena Parihar*
Department of Biotechnology, Lovely Professional University, Phagwara-144402 Punjab, India.
Accepted 7 January, 2010.
Abstract
In the present investigation an attempt has been done on isolation of actinomycetes from the soil, extracting the antifungal compounds from these isolated actinomycetes and then testing the extract against the growth of Alternaria sps, Aspergillus niger, Aspergillus flavus, Fusarium sps, and Rhizopus stolonifer. During the investigation it was found that nearly all the extracts were effective against the test fungi and the mycelial growth of fungi is inversely proportional to the concentration of extract.
Key words: Antifungal activity, actinomycetes extracts, plant pathogenic fungi.
Harpreet Sharma, Leena Parihar*
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2009
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2009 International Scholars Journals
Full Length Research Paper
A novel antifungal phenolic compound from Parrotia persica
M. Ahanjan1, M. P. Raghavendra 2,3 and K. A. Raveesha2*
1Faculty of Medicine, Mazandaran University of Medical Sciences, Sari, Iran.
2Herbal Drug Technology Laboratory, Department of Studies in Botany, University of Mysore, Manasagangotri, Mysore-570 006, Karnataka, India.
3Maharani’s Science College for Women, Mysore- 570 008, Karanataka.
Accepted 18 May, 2009
Abstract
Aqueous and methanol extracts of Parrotia persica leaves were assayed for antifungal activity against phytopathogenic Fusarium oxysporum and human pathogenic Candida albicans by poisoned food technique. Both the aqueous and methanol extracts demonstrated significant antifungal activity. Further fractionation of methanol extract guided by antifungal activity resulted in the isolation of an active principle and it is identified as phenolic compound. The structure of the active principle was elucidated by mass spectroscopy, 1H NMR and 13C NMR spectroscopy. These results revealed that the compound is 6-(ethoxymethyl)-tetrahydro-2H-pyran-2, 3, 4, 5-tetraol compound with 1- isopropyl-4-methoxybenzene, the compound was found responsible for antifungal activity against both F. oxysporum and C. albicans.
Key words: Parrotia persica, phenolic compound, antifungal activity.
M. Ahanjan, M. P. Raghavendra and K. A. Raveesha*
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2009
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2009 International Scholars Journals
Full Length Research Paper
Recent advances in the characterization of peptidyl transferase center: zero-distance labeling of proteins at or near the catalytic site of human 80S or Escherichia coli 70S ribosomes by means of periodate-oxidized tRNA
Soria Baouz1, Anne Woisard1, Lila Chenoune1, Gustave Aguié1, Gérard Keith1, Jean-Marie Schmitter2, Jean-Pierre Le Caer3 and Codjo Hountondji1*
1UPMC Univ Paris 06, Equipe de Photobiologie Moléculaire, Tour 42 (5ème Etage, couloir 42-32), Case Courrier 60, 2 place Jussieu, F-75251 Paris Cedex 05, France.
2Institut Européen de Chimie et Biologie (CNRS FRE 2247), F-33607, Pessac, France.
3CNRS-UPR 2301, Institut de Chimie des Substances Naturelles (ICSN), Avenue de la Terrasse, F-91198 Gif-Sur-Yvette, France.
Accepted 12 August, 2009
Abstract
Periodate-oxidized tRNA (tRNAox), the 2’,3’-dialdehyde derivative of tRNA, was used as a zero-length active site-directed affinity labeling reagent, to covalently label proteins at the peptidyl transferase center (PTC), the catalytic site of the large ribosomal subunit. When human 80S or Escherichia coli 70S ribosomes were reacted separately with tRNAox positioned at the P-site, in the presence of an appropriate 12 mer mRNA, a set of two tRNAox- labeled ribosomal proteins was observed. These proteins referred to in this work as rPox1 and rPox2 exhibited comparable physico-chemical properties including apparent molecular weights. In the case of human 80S ribosome, the protein present in the major labeled tRNA- rPox1 covalent complex was identified as the 60S ribosomal protein L36a-like (RPL36AL) by mass spectrometry. The molecular weight of the minor labeled tRNA-rPox2 covalent complex was estimated from the data of the 1-D SDS-PAGE, and a deduced molecular weight of 34,000+ 2,000 Da for the ribosomal protein referred to as rPox2 designated protein RPL5 as the candidate minor labeled protein of human 80S ribosome. Search for candidate ribosomal proteins for the tRNAox-labeled proteins rPox1 and rPox2 of 70S ribosome from E. coli designated RPL2 (M.W. 29,860 Da), the largest eubacterial rP as the tRNAox-labeled protein corresponding to the minor labeled human RPL5, and RPL15 (M.W. 14,980 Da) or RPL16 (M.W. 15,281 Da) as corresponding to the major labeled human RPL36AL.
Key words: Human 80S or E. coli 70S ribosomes, peptidyl transferase center, human RPL36AL, RPL5/P-site or A-site tRNA, periodate-oxidized tRNA.
Gustave Aguié, Soria Baouz, Jean-Marie Schmitter, Lila Chenoune, Gérard Keith, Anne Woisard, Jean-Pierre Le Caer3 and Codjo Hountondji*
Page: 1 - 10