Showing papers on "Termitomyces clypeatus published in 2011"

Evaluation of ten wild nigerian mushrooms for amylase and cellulase activities.

Abstract: Amylases and cellulases are important enzymes that can be utilized for various biological activities. Ten different wild Nigerian mushrooms (Agaricus blazei, Agaricus sp., Corilopsis occidentalis, Coriolus versicolor, Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, Podoscypha bolleana, Pogonomyces hydnoides, and Nothopanus hygrophanus) were assayed for production of these secondary metabolites. The results revealed that most of the tested wild fungi demonstrated very good amylase and cellulase activities. With the incorporation of carboxymethyl-cellulose (a carbon source) into the culture medium, Agaricus blazei had the highest amylolytic activity of 0.60 unit/mL (at 25℃, pH 6.8). This was followed in order by P. tuber-regium and Agaricus sp. with 0.42 and 0.39 unit/mL, respectively (p ≤ 0.05). Maltose and sucrose supplementation into the submerged liquid medium made N. hygrophanus and P. hydnoides to exhibit very low amylase activities of 0.09 and 0.11 unit/mL, respectively. Introducing peptone (an organic nitrogen source) into the basal medium enhanced the ability of C. versicolor to produce a cellulase value of 0.74 unit/mL. Other organic nitrogen sources that supported good cellulase activities were yeast extract and urea. Sodium nitrate (inorganic nitrogen source) generally inhibited cellulase production in all mushrooms. The best carbon source was carboxymethyl-cellulose, which promoted very high cellulase activity of 0.67 unit/mL in C. versicolor, which was followed in order by P. tuber-regium, T. chypeatus, and C. occidentalis (p ≤ 0.05). Sucrose was the poorest carbon compound, supporting the lowest values of 0.01, 0.01, and 0.14 unit/mL in P. hydnoides, A. blazei, and Agaricus sp., respectively.

Morphological Characterization and Yield Potential of Termitomyces spp. Mushroom in Gorakhpur forest Division

Abstract: Termitomyces is a wild mushroom growing in the symbiotic association of termite under or aboveground the termatorium, which is extensively used as human food and medicine from the time immortal. It has many more species throughout the country, but the study reveals in the Gorakhpur forest division confined that there are four species of Termitomyces are found. In order to determine the genetic diversity among these four species were studied by using morphological characterization, phenotypical appearance. Four species naming Termitomyces heimii, Termitomyces clypeatus, Termitomyces mammiformis and Termitomyces microcarpus characterized by different morphological traits i.e., shape of perforatorium, stipe length(cm), pileus length, margin of fruit body, colour of fruit body, gills, flesh, annulus, pseudorrhiza and spore print were recorded. Results indicate that all the four species of Termitomyces shows great diversity in their morphological characters.

Collection, morphological characterization and nutrient profile of some wild mushrooms from Akoko, Ondo state, Nigeria.

Abstract: A total number of twenty-six different wild mushrooms namely Agaricus blazei, Agaricus sp, Coprinus africanus, Corilopsis occidentalis, Coriolus vesicolor, Cymatoderma elegans, Daedalea sp, Daldinia concentrica, Filoboletus gracilis, Fomes sp, Fomes noxius, Lactarius hygrophoroides, Panus sp, Marasmius arborescens, Marasmius zenkeri, Panus fulvus, Microporus xanthopus, Nothopanus hygrophanus, Polyporus sp, Polyporus dermoporus, Schizophyllum sp, Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, Pogonomyces hydnoides and Podoscypha bollena were collected fromtypical tropical rain forests in Akoko area of Ondo state, Nigeria Akoko land is an area, located in between 7o00Â’N and 8o00Â’N latitude and 5o30Â’E and 6o15Â’E longitude with a wide range of ecosystems and species diversity The criteria used in the identificationwere habitat,morphological and physical characteristics such as spore morphology, cap type, presence of veil, gills, presence of volva, sizes of mushroom and colour of the sporophores Agaricus sp contained the highest crude protein (3709%) followed in order by Termitomyces globulus (3177%), Termitomyces clypeatus (1982%) and Pleurotus tuberregiun (1214%) Other food materials found in significant quantities in these mushroom are ethanol soluble sugars and mineral elements such as Ca, K, P,Mg and Fe (P<005) The significance of these observations were discussed

Improved production and properties of β-glucosidase influenced by 2-deoxy-d-glucose in the culture medium of Termitomyces clypeatus

Abstract: Increased production, secretion, and activity of β-glucosidase in the filamentous fungus Termitomyces clypeatus was achieved in presence of the glycosylation inhibitor 2-deoxy-d-glucose (0.05%, w/v) during submerged fermentation. Enzyme activity increased to 163 U/mL by adding mannose (2 mg/mL) to the medium. Such a high enzyme activity has not been achieved without mutation or genetic manipulation. The Km and Vmax of the enzyme in culture medium were determined to be 0.092 mM and 35.54 U/mg, respectively, with p-nitrophenyl β-d-glucopyranoside as substrate, confirming its high catalytic activity. The enzyme displayed optimum activity at pH 5.4 and 45°C. The enzyme was fairly stable between acidic to alkaline pH and retained about 75 ∼ 65% residual activities between pH 4 and 10.6 and demonstrated full activity at 45°C for 3 days. The enzyme was also stable in the presence of Zn2+ and Mg2+ and 80% of the residual activity was observed in the presence of Mn2+, Ca2+, K+, Cu2+, EDTA, and sodium azide. Around 70% of the activity was retained in the presence of 2 M guanidium HCl and 3 M urea, whereas the activity was 5 and 2 times higher in the presence of 4 mM beta-mercaptoethanol and 50 mM DTT, respectively. The enzyme obtained from the culture filtrate showed potential cellulose saccharifying ability which increased further when supplemented with commercial cellulase. Thus, this enzyme could be used without any additional downstream processing for commercial cellulase preparation and production of bioethanol or for other biotechnological applications.

Evidence of an alternative route of cellobiase secretion in the presence of brefeldin A in the filamentous fungus Termitomyces clypeatus.

Abstract: Secretion of cellobiase occurred in a brefeldin A (BFA) uninhibited manner in the filamentous fungus Termitomyces clypeatus. Fluorescence confocal microscopy revealed that application of the drug at a concentration of 50 μg/ml caused arrest of Spitzenkorper assembly at the hyphal tip. This resulted in greater than 30% inhibition of total protein secretion in the culture medium. However, the cellobiase titer increased by 17%, and an additional 13% was localized in the vacuolar fraction en route secretion. The secretory vacuoles formed in the presence of the drug were also found to be bigger (68 nm) than those in the control cultures (40 nm). The enzyme secreted in the presence and absence of BFA revealed a single activity band in both cases in native PAGE and had similar molecular masses (approx. 120 kDa) in SDS-PAGE. The BFA enzyme retained 72% of native glycosylation. It also exhibited a higher stability and retained 98% activity at 50oC, 93.3% activity at pH 9, 63.64% activity in the presence of 1M guanidium hydrochloride, and 50% activity at a glucose concentration of 10 mg/ml in comparison to 68% activity, 75% activity, 36% activity, and 19% activity for the control enzyme, respectively. The observations collectively aimed at the operation of an alternative secretory pathway, distinct from the target of brefeldin A, which bypassed the Golgi apparatus, but still was able to deliver the cargo to the vacuoles for secretion. This can be utilized in selectively enhancing the yield and stability of glycosidases for a successful industrial recipe.

Comparative elucidation of properties of sucrase-cellobiase co-aggregate produced in media containing sucrose by Termitomyces clypeatus

Abstract: Production profiles and characterization of the sucrase-cellobiase (S-C) co-aggregates from the filamentous fungus Termitomyces clypeatus were compared in media containing 1% and 5% sucrose to understand the effect of cellular regulation over secretion and aggregation of these two industrially important glycosidases. The enzymes were secreted constitutively but in a high sucrose medium (5%), cellobiase secretion was reduced to a basal level of 0.03 U/mL. In intracellular, cell-bound and extracellular milieus, S/C ratios gradually declined in a predictable trend indicating participation of more cellobiase subunits for secretion. Sucrase was secreted via vacuoles in the fungus, following the same route as that of cellobiase and thus co-aggregates of S-C were present in the vacuolar fraction. The extracellular co-aggregates showed similar molecular sizes (>550 kDa) on zymography; however, SDS-PAGE revealed substantial difference in their subunit assemblies. Sucrase from the 5% medium showed a 2.6 times lower K m than 1% medium. These observations demonstrated the formation of a unique S-C co-assembly, optimally suited to its needs and accommodation of the constituent subunits, to be used for biotechnological applications.

Comparative studies on enzyme activities of bacterium (Bacillus subtilis) and Nigerian edible fungi (Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, and Agaricus sp)

Abstract: Enzyme activities of Termitomyces clypeatus, Termitomyces globulus, Pleurotus tuber-regium, andAgaricus sp (edible Nigerian fungi) were compared with that of Bacillus subtilis (a bacterium) which have been known to be a very good amylase producer. In these studies, Pleurotus tuber-regium and Agaricus sp had amylase activities values of 0.45 and 0.39 U/min respectively. Bacillus subtilis had highest amylase value with yeast extract (0.63U/min) and least valuewithNaNO3 (0.35unit/min). For cellulase activity, Bacillus subtilis had value of 0.4unit/minwith yeast extractwhileCoriolus vesicolor, Pleurotus tuber-regium and Termitomyces clypetus had values of 0.67,0.59 and 0.51 U/min respectively. Temperature and pH also had significant effect on the production of these enzymes.