Characterization of a micrococcus which enhances the cellulolytic activity of Trichurus cylindricus

1971 ◽  
Vol 17 (1) ◽  
pp. 31-37 ◽  
Author(s):  
R. E. Smith ◽  
T. S. Neudoerffer

A bacterial contaminant from a cellulase-producing culture of Trichurus cylindricus was subjected to physiological and biochemical tests, and identified as a member of the genus Micrococcus, subgroup 6 (Baird-Parker). It appeared either to stimulate cellulase production by the fungus, or to increase cellulase activity. The amino acid and protein content of the Micrococcus suggested that it might be useful as a feed supplement. In a preliminary trial, rats accepted freeze-dried cells as a partial source of energy, and grew at a normal rate. No toxic effects of the diet were noted.

1978 ◽  
Vol 56 (18) ◽  
pp. 2309-2311 ◽  
Author(s):  
B. N. Dhanvantari

Isolations made from 68 naturally infected peach, plum, and sweet cherry nursery stock from the Niagara Peninsula and southwestern Ontario yielded 30 pathogenic isolates of Agrobacterium. These isolates were separated into two groups by 17 physiological and biochemical tests. The predominant group, consisting of 27 isolates, was 3-ketolactose negative and corresponded to biotype 2, and the other, consisting of only three isolates, corresponded to biotype 1 of Agrobacterium radiobacter var. tumefaciens sensu Keane, Kerr, and New (1970). Among the pathogenic isolates, 25 were sensitive and 5 were resistant to the bacteriocin produced by strain 84 of A. radiobacter var. radiobacter sensu Keane. Kerr, and New (1970).


2005 ◽  
Vol 55 (1) ◽  
pp. 433-436 ◽  
Author(s):  
Hideki Yamamura ◽  
Masayuki Hayakawa ◽  
Youji Nakagawa ◽  
Tomohiko Tamura ◽  
Tetsuro Kohno ◽  
...  

Chemotaxonomic and morphological characterization of two actinomycete strains, MS1-3T and AS4-2, respectively isolated from moat sediment and scumming activated sludge, was carried out. This characterization clearly demonstrated that strains MS1-3T and AS4-2 belong to the genus Nocardia. 16S rRNA gene sequencing studies showed that these isolates are most closely related to Nocardia beijingensis (98·1–98·3 % similarity), Nocardia brasiliensis (97·9–98·0 %) and Nocardia tenerifensis (97·8–97·9 %). However, the results of DNA–DNA hybridizations and physiological and biochemical tests showed that strains MS1-3T and AS4-2 could be differentiated from their closest phylogenetic relatives both genotypically and phenotypically. It is proposed that the two isolates be classified as representatives of a novel species of Nocardia, Nocardia takedensis sp. nov. The type strain is MS1-3T (=NBRC 100417T=DSM 44801T); AS4-2 (=NBRC 100418=DSM 44802) is a reference strain.


2005 ◽  
Vol 51 (9) ◽  
pp. 773-776 ◽  
Author(s):  
T Kudanga ◽  
E Mwenje

Cellulase production by Aureobasidium pullulans from the temperate regions has remained speculative, with most studies reporting no activity at all. In the current study, tropical isolates from diverse sources were screened for cellulase production. Isolates were grown on a synthetic medium containing cell walls of Msasa tree (Brachystegia sp.) as the sole carbon source, and their cellulolytic activities were measured using carboxymethyl cellulose and α-cellulose as substrates. All isolates studied produced carboxymethyl cellulase (endoglucanase) and alpha-cellulase (exoglucanase) activity. Endoglucanase-specific activities of ten selected isolates ranged from 2.375 to 12.884 µmol glucose·(mg protein)–1·h–1, while activities on α-cellulose (exoglucanase activity) ranged from 0.293 to 22.442 µmol glucose·(mg protein)–1·day–1. Carboxymethyl cellulose induced the highest cellulase activity in the selected isolates, while the isolates showed variable responses to nitrogen sources. The current study indicates that some isolates of A. pullulans of tropical origin produce significant extracellular cellulolytic activity and that crude cell walls may be good inducers of cellulolytic activity in A. pullulans.Key words: Aureobasidium pullulans, plant cell wall, cellulases, endoglucanase, exoglucanase.


Author(s):  
A. U. Hassan ◽  
R. Jafaru ◽  
I. B. Mato ◽  
E. Kereakede ◽  
A. H. Galadanci ◽  
...  

Cellulase is one of the most economically important enzyme, which aids in catalyzing cellulolysis, the decomposition of cellulose and other related polysaccharides. So the demand/importance of this enzyme in both domestic and commercial sectors cannot be over emphasized. In this research cellulase-producing bacteria were isolated from soil around sugarcane waste dumping area, which was identified to be P. fulorescens after numerous biochemical and microbiological analysis. The bacteria were then grown and used to ferment certain biomass, with the aim of using the organisms to produce the cellulase enzyme. The total protein/cellulase enzyme activity of the medium was ascertained. Optimization/characterization for maximum cellulase activity was done by varying the temperature, pH, enzyme concentration and substrate concentration, in which the optimum condition for cellulase production was ascertain to be at a temperature and pH of 40˚C and pH 7 respectively. SDS-PAGE electrophoresis was carried out to determine and reconfirm the presence and molecular weight of the isolated enzyme. The estimated extrapolated molecular weight of the enzyme was found to be 13.5KDa.


1969 ◽  
Vol 63 (2) ◽  
pp. 189-194
Author(s):  
D. R. Hale ◽  
T. R. Tosteson

Twenty bacterial isolates from selected marine communities were obtained employing solid, modified sea water media contain ing slops. Thirteen basic morphological, cytological, physiological and biochemical tests were conducted to characterize six of the strains that grew most successfully on the slops media. The ability to hydrolyze high molecular weight sugars and proteins appears to be a necessary condition for the successful growth of some of these isolates on slops media. Tentative identifications of these bacterial strains were made.


2011 ◽  
Vol 183-185 ◽  
pp. 773-777 ◽  
Author(s):  
Jun Bo Pan ◽  
Min Zhao ◽  
Lei Lu ◽  
Mei Hui Du ◽  
Guo Fu Li ◽  
...  

Bacterial strains exhibiting laccase activity were isolated from the forest soil. A strain LC02 with syringaldazine oxidation ability was obtained using enrichment medium supplemented with copper ions. The isolated strain was identified as Bacillus amyloliquefaciens using physiological and biochemical tests as well as 16S rDNA sequence analysis. The characterization of spore laccase activity was investigated. The result showed that the optimum pH and temperature of the enzyme was 6.6 and 70°C, respectively. A great thermostability was observed for the spore laccase at 70°C. Laccase activity was strongly inhibited by 0.1 mmol/L NaN3, dithiothreitol and cysteine.


1985 ◽  
Vol 225 (2) ◽  
pp. 449-454 ◽  
Author(s):  
E H Creaser ◽  
R L Porter ◽  
K A Britt ◽  
J A Pateman ◽  
C H Doy

Aspergillus alcohol dehydrogenase is produced in response to growth in the presence of a wide variety of inducers, of which the most effective are short-chain alcohols and ketones, e.g. butan-2-one and propan-2-ol. The enzyme can be readily extracted from fresh or freeze-dried cells and purified to homogeneity on Blue Sepharose in a single step by using specific elution with NAD+ and pyrazole. The pure enzyme has Mr 290 000 by electrophoresis or gel filtration; it is a homopolymer with subunit Mr 37 500 by electrophoresis in sodium dodecyl sulphate; its amino acid composition corresponds to Mr 37 900, and the native enzyme contains one zinc atom per subunit. The enzyme is NAD-specific and has a wide substrate activity in the forward and reverse reactions; its activity profile is not identical with those of other alcohol dehydrogenases.


2019 ◽  
Vol 47 (3) ◽  
Author(s):  
Gamal El-BAROTY ◽  
Faten ABOU-ELELLA ◽  
Hassan MOAWAD ◽  
Talaat N. El-SEBAI ◽  
Fatma ABDULAZIZ ◽  
...  

Since accumulation of agricultural wastes represents a huge problem, it was important to explore the available methods to help eliminate agricultural wastes safely, and simultaneously produce functional enzyme like cellulase. Six native Egyptian fungal strains were isolated, morphologically identified and screened for cellulose biodegradation potential, which was determined as endoglucanase or as carboximethylcellulase (CMCase). The most promising isolate (Aspergillus terreus) was selected for molecular characterizations based on sequencing of internal transcribed spacer (ITS). Further optimization experiments were accomplished on the selected strain. The strain with cellulolytic activity, 2.26 IU mL-1 was identified using ITS nucleotides (genes) sequences and the result confirmed that the strain is 99.8% homology with A. terreus. Then, it was submitted to GeneBank and given an accession number. Further optimization experiments revealed that 35ºC is the optimum temperature for cellulase production and raised the enzyme activity (EA) up to 3.19 IU mL-1. Out of two organic nitrogen sources; peptone at concentration 6 gL-1 was found to be the optimum nitrogen source for cellulase production with the highest activity 4 IU mL-1. Whereas, the different four carbon sources: microcellulose, corn stalks, wheat straw and rice straw showed significant differences in EA with values 11.07, 9.68, 7.87 and 3.71 IU mL-1, respectively at  pH 3. The maximum EA was recorded to be within 5-7 days of incubation, dependent on type of carbon sources. The optimization of different incubation conditions raised cellulolytic activity from 2.26 IU mL-1 up to 11.18 IU mL-1.   ********* In press - Online First. Article has been peer reviewed, accepted for publication and published online without pagination. It will receive pagination when the issue will be ready for publishing as a complete number (Volume 47, Issue 3, 2019). The article is searchable and citable by Digital Object Identifier (DOI). DOI link will become active after the article will be included in the complete issue. *********


2017 ◽  
Vol 52 (3) ◽  
pp. 209-220
Author(s):  
MM Rahman ◽  
MAA Khan ◽  
IH Mian ◽  
AM Akanda ◽  
MZ Alam

A study was undertaken for characterization and identification of the soft rot causing bacterial pathogens of onion. Bacterial pathogens were isolated from soft rotted stored onions of different varieties and locations of Bangladesh. Altogether 73 bacterial isolates were isolated from soft rotted onions. Among them, twelve soft rot-positive isolates were selected for characterization and identification on the basis of more virulence. Physiological and biochemical tests were performed following standard methods for characterization and identification of selected soft rot bacterial isolates. Seven isolates namely O-03, O-18, O-69, O-72, O-130, O-156 and O-180 were identified as Pectobacterium carotovorum subsp. carotovorum (E. carotovora subsp. carotovora), two isolates O-101 and O-118 were identified as E. chrysanthemi and three isolates O-05, O-14 and O-15 were the members of Burkholderia cepacia.Bangladesh J. Sci. Ind. Res. 52(3), 209-220, 2017


2014 ◽  
Vol 6 (1) ◽  
Author(s):  
Yulia Oktavia ◽  
Aulia Andhikawati ◽  
Tati Nurhayati ◽  
Kustiariyah Tarman

<p>In this study, cellulase was produced by endophytic fungus isolated from seagrass. Substrate used for incubating the fungus was the waste of agar industry. The objectives of this study were to optimize cellulase production and to characterize the highest activity of fungal crude cellulase. In our previous study, the EN isolate (isolated from <span style="text-decoration: underline;">Enhalus</span> <span style="text-decoration: underline;">sp</span>.) showed the highest cellulolytic index. Therefore, in this research we focused on cellulase activity of the isolate. Cellulase activity was determined based on endoglucanase activity, total cellulase activity, and β-glucosidase activity. The highest activity was then used to determine cellulase activity in enzyme characterization. The fungus was cultured in different concentration of agar extraction algal wastes. The fungal culture was incubated for 3-21 days with 120 rpm orbital shaker. The results showed that endoglucanase activity was 0.019-0.031 U/mL, total cellulase activity was 0.007-0.013 U/mL, and β-glucosidase activity was 0.00012-0.00361 U/mL. The highest endoglucanase and total cellulase activity were obtained from the fungal culture after 9 days incubation, β-glucosidase was obtained from the fungal culture after 15 days incubation with 1.5% of algal waste as substrate. The optimum pH and temperature were determined as 4 and 60 <sup>o</sup>C, maximum reaction rate (V<sub>max</sub>) and Michaelis-Menten constant (K<sub>m</sub>) for endoglucanase activity was determined as 0.044 U/mL and 0.103% respectively.</p> <p>Keywords: algal waste, cellulase, endophytes, enzymes, seagrass</p>


Sign in / Sign up

Export Citation Format

Share Document