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Proximate composition, antioxidant activities and fatty acid profiling of selected Mushrooms collected from Azad Jammu and Kashmir

100%
Shahid M., Fatima H., Anjum F., Riaz M.
Acta Poloniae Pharmaceutica - Drug Research
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2020
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vol. 77
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issue 1
145-153
EN
Mushrooms can be used in diet as nutraceutical or functional foods for promoting and maintaining health quality and health longevity. Mushrooms just like medicinal plants can be utilized in the form of powder or extract as curative agents of several diseases and in providing a healthy diet. In current study, ten different mushroom species were collected from Azad Jammu and Kashmir. The selected mushrooms were assessed for their nutritional value, biological activities and fatty acid profiling. Before extraction, proximate analysis of all selected mushrooms was performed. Protein, fat, ash and total carbohydrate contents ranged from 10-30%, 0.43-8.08%, 1.1-9.14%, 12.47-92.52%, respectively. Then mushrooms were extracted with three different solvents n-hexane, ethyl acetate and methanol for the assessment of their antioxidant potentials through different antioxidant assays like total phenolics, total flavonoid contents and DPPH inhibition assay. The order of antioxidant potential in different solvent is methanol>Ethyl acetate>n-hexane. Quantification of fatty acids by GC/MS analysis revealed that stearic acid, palmitic acid, oleic acid, linolenic acid were present in significant quantity in different mushrooms and unsaturated fatty acids were found abundant over saturated fatty acids in all the selected mushrooms. So presence of fatty acids in studied samples is one of the main biologically active ingredients from mushrooms. The study concluded that the selected mushrooms from different regions of Azad Jammu and Kashmir are of nutritional importance having significant antioxidant potential and contains several unsaturated fatty acids which contribute to the nutritional value of mushrooms.
2
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Purification and characterization of an antibacterial protein from dried fruiting bodies of the wild mushroom Clitocybe sinopica

100%
Zheng S., Liu Q., Zhang G., Wang H., Ng T.
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2010
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vol. 57
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issue 1
43-48
EN
A novel antibacterial protein with a molecular mass of 44 kDa has been isolated from dried fruiting bodies of the wild mushroom Clitocybe sinopica. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis showed that the protein was composed of two subunits each with a molecular mass of 22 kDa. Its N-terminal amino-acid sequence, SVQATVNGDKML, has not been reported for other antimicrobial proteins. The purification protocol included ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The antibacterial protein was adsorbed on all three ion exchangers. The antimicrobial activity profile of the protein against tested bacterial and fungal strains disclosed that it possessed potent antibacterial activity against Agrobacterium rhizogenes, A. tumefaciens, A. vitis, Xanthomonas oryzae and X. malvacearum with a minimum inhibitory concentration mostly below 0.6 µM. However, it had no antibacterial activity against Pseudomonas batatae, Erwinia herbicola, Escherichia coli, and Staphylococcus aureus, and no antifungal activity against Setosphaeria turcica, Fusarium oxysporum, Verticillium dahliae, Bipolaris maydis, and B. sativum. The antibacterial antivity against A. tumefaciens was stable after exposure to 20-60°C for 30 min and to pH 4-9 for 1h.
3
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A novel alkaline protease from wild edible mushroom Termitomyces albuminosus

100%
Zheng S., Wang H., Zhang G.
|
2011
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vol. 58
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issue 2
269-274
EN
A protease with a molecular mass of 30 kDa and the N-terminal sequence of GLQTNAPWGLARSS, was isolated from fresh fruiting bodies of the wild edible mushroom Termitomyces albuminosus. The purification protocol included ion exchange chromatography on DEAE-cellulose, Q-Sepharose, SP-Sepharose and FPLC-gel filtration on Superdex 75. The protein was unadsorbed on DEAE-cellulose and Q-Sepharose, but adsorbed on SP-Sepharose. The optimal pH and temperature of the purified enzyme were 10.6 and 60 °C, respectively. The enzyme was stable in the presence of 2 % (v/v) Tween 80 and 4 M urea. More than 80 % of the enzyme activity was retained in 2 % (v/v) Triton X 100, 54 % in 10 mM EDTA and 31 % in 2 % (w/v) SDS. The enzyme was strongly inhibited by phenylmethylsulfonyl fluoride (PMSF), but not inhibited by dithiothreitol (DTT), pepstatin or lima bean trypsin inhibitor suggesting that it was a serine protease but not a trypsin-like one. The protease was inhibited by Hg2+, Cu2+, and Fe3+ ions. The Km and Vmax values of the purified enzyme for casein were 8.26 mg ∙ ml-1 and 0.668 mg ∙ ml-1 ∙ min-1, respectively.
4
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A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa

88%
Zhang G. Q., Sun J., Wang H. X., Ng T. B.
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issue 3
415-421
EN
Little was known about biological activities of compounds from the medicinal mushroom of the genus Pholiota. A lectin from the Pholiota adiposa has now been isolated and its properties tested. The isolation procedure included ion exchange chromatography on DEAE-cellulose and CM-cellulose, and fast protein liquid chromatography-gel filtration (FPLC) on Superdex 75. The lectin was composed of two identical subunits, each with a molecular mass of 16 kDa. Its N-terminal amino-acid sequence showed little similarity to sequences of other Agaricales lectins. The hemagglutinating activity of the lectin was stable at temperatures up to 50°C, and in NaOH and HCl solutions with concentrations less than 25 mM. It was inhibited by inulin (12.5-200 mM), but enhanced by Cu2+ (6.25-25 mM), Fe2+ (12.5-25 mM), and Al3+ (6.25-25 mM) ions. The lectin showed antiproliferative activity toward hepatoma Hep G2 cells and breast cancer MCF7 cells with an IC50 of 2.1 µM and approximately 3.2 µM, respectively. It exhibited HIV-1 reverse transcriptase inhibitory activity with an IC50 of 1.9 µM. When compared with P. aurivella lectin, the only Pholiota lectin published to date, P. adiposa lectin differs in chromatographic behavior, molecular mass, N-terminal sequence, and effect of cations on hemagglutinating activity. In the case of the lectin from P. aurivella, its antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities have not been determined.
5
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Trypsin-specific Inhibitors from the Macrolepiota procera, Armillaria mellea and Amanita phalloides wild mushrooms

75%
Lukanc T., Brzin J., Kos J., Sabotič J.
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2017
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vol. 64
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issue 1
21-24
EN
Wild growing mushrooms are a rich source of novel proteins with unique features. We have isolated and characterized trypsin inhibitors from two edible mushrooms, the honey fungus (Armillaria mellea) and the parasol mushroom (Macrolepiota procera), and from the poisonous death cap (Amanita phalloides). The trypsin inhibitors isolated: armespin, macrospin and amphaspin, have similar molecular masses, acidic isoelectric points and are not N-glycosylated. They are very strong trypsin inhibitors and weak chymotrypsin inhibitors. They are resistant to exposure to high temperatures and withstand extreme pH values. These exceptional characteristics are advantageous for their potential use in biotechnology, agriculture and medicine.
6
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A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa

75%
Sun J., Zhao Y., Chai H., Wang H., Ng T. B.
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2011
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vol. 58
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issue 4
567-572
EN
A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose. It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 °C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC50 of 25 µM. The protease did not have antifungal or ribonuclease activity.
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