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Acaconin, a chitinase-like antifungal protein with cytotoxic and anti-HIV-1 reverse transcriptase activities from Acacia confusa seeds

100%

Lam S. K., Ng T. B.

Acta Biochimica Polonica

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2010

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tom 57

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nr 3

From the seeds of Acacia confusa, a chitinase-like antifungal protein designated as acaconin that demonstrated antifungal activity toward Rhizoctonia solani with an IC50 of 30 ± 4 μM was isolated. Acaconin demonstrated an N-terminal sequence with pronounced similarity to chitinases and a molecular mass of 32 kDa. It was isolated by chromatography on Q-Sepharose, SP-Sepharose and Superdex 75 and was not bound by either ion exchanger. Acaconin was devoid of chitinase activity. The antifungal activity against Rhizoctonia solani was completely preserved from pH 4 to 10 and from 0ºC to 70ºC. Congo Red staining at the tips of R. solani hyphae indicated inhibition of fungal growth. However, there was no antifungal activity toward Mycosphaerella arachidicola, Fusarium oxysporum, Helminthosporium maydis, and Valsa mali. Acaconin inhibited proliferation of breast cancer MCF-7 cells with an IC50 of 128 ± 9 μM but did not affect hepatoma HepG2 cells. Its IC50 value toward HIV-1 reverse transcriptase was 10 ± 2.3 μM. The unique features of acaconin include relatively high stability when exposed to changes in ambient pH and temperature, specific antifungal and antitumor actions, potent HIV-reverse transcriptase inhibitory activity, and lack of binding by strongly cationic and anionic exchangers.

2

Novel galactonic acid-binding hexameric lectin from Hibiscus mutabilis seeds with antiproliferative and potent HIV-1 reverse transcriptase inhibitory activities

100%

Lam S. K., Ng T. B.

Acta Biochimica Polonica

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2009

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tom 56

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nr 4

649-654

A hexameric 150-kDa lectin was isolated from dried Hibiscus mutabilis seeds using a chromatographic protocol that involved ion exchange chromatography on SP-Sepharose, and gel filtration on Superdex 75 and Superdex 200. The lectin was not adsorbed on SP-Sepharose and was eluted from the Superdex 75 column in the void volume. It was eluted in the first peak from Superdex 200. It was strongly adsorbed on DEAE-cellulose and Q-Sepharose and could not be easily desorbed. The hemagglutinating activity of the lectin, which was stable at pH 4-7 and up to 50oC, could be inhibited by 25 mM galactonic acid. This is the first report of a galactonic acid-binding lectin. It potently inhibited HIV-1 reverse transcriptase with an IC50 of 0.2 µM. It exhibited weak antiproliferative activity towards both hepatoma HepG2 cells (40% inhibition) and breast cancer MCF-7 cells (50% inhibition) at 100 µM concentration of the lectin. It did not inhibit mycelial growth of a number of fungi tested.

3

A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa

81%

Zhang G. Q., Sun J., Wang H. X., Ng T. B.

Acta Biochimica Polonica

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2009

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tom 56

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nr 3

415-421

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 50oC, 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.

4

Purification and characterization of a novel laccase from the mushroom Pleurotus nebrodensis

81%

Tian G.-T., Zhang G.-Q., Wang H.-X., Ng T. B.

Acta Biochimica Polonica

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2012

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tom 59

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nr 3

A novel laccase with a molecular mass of 64 kDa and the N-terminal sequence AIGPDDTINF was isolated from fresh fruiting bodies of the mushroom Pleurotus nebrodensis. The purification protocol comprised ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration on Superdex 75. The laccase was adsorbed on DEAE-cellulose and Q-Sepharose, but not on CM-cellulose. It demonstrated an optimal temperature of 70°C. The enzyme activity increased steadily over the temperature range 20°C-70°C. There was only a slight reduction in activity at 80°C. However, all activity disappeared following exposure to 100°C for 10 minutes. The enzyme activity changed only slightly over the pH range 3-5, with the optimum at pH 5, but underwent a precipitous decline when the pH was elevated to 6, and was undetectable at pH 8 and pH 9.

5

A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa

71%

Sun J., Zhao Y., Chai H., Wang H., Ng T. B.

Acta Biochimica Polonica

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2011

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tom 58

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nr 4

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.

6

Purification and characterization of an antibacterial protein from dried fruiting bodies of the wild mushroom Clitocybe synopica

71%

Zheng S., Liu Q., Zhang G., Wang H., Ng T. B.

Acta Biochimica Polonica

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2010

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tom 57

|

nr 1

43-48

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 1 h.

7

Purification and characterization of a novel metalloprotease from fruiting bodies of Oudemansiella radicata

61%

Geng X., Te R., Tian G., Zhao Y., Zhao L., Wang X., Ng T. B.

Acta Biochimica Polonica

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2017

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tom 64

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nr 3

8

Characterization of an acidic Alpha-galactosidase from hemp (Cannabis sativa L.) seeds and its application in removal of raffinose family oligosaccharides (RFOs)

61%

Zhang W., Du F., Tian G., Zhao Y., Wang X., Ng T. B.

Acta Biochimica Polonica

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2018

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tom 65

|

nr 3

Ograniczanie wyników

8 Acta Biochimica Polonica

8 Ng T. B.

3 Zhao Y.

2 Lam S. K.

2 Sun J.

2 Tian G.

2 Wang H.

2 Wang X.

1 Chai H.

1 Du F.

1 Geng X.

1 Liu Q.

1 Te R.

1 Tian G.-T.

1 Wang H. X.

1 Wang H.-X.

1 Zhang G.

1 Zhang G. Q.

1 Zhang G.-Q.

1 Zhang W.

1 Zhao L.

1 Zheng S.

1 2018

1 2017

1 2012

1 2011

2 2010

2 2009

Acaconin, a chitinase-like antifungal protein with cytotoxic and anti-HIV-1 reverse transcriptase activities from Acacia confusa seeds

Novel galactonic acid-binding hexameric lectin from Hibiscus mutabilis seeds with antiproliferative and potent HIV-1 reverse transcriptase inhibitory activities

A novel lectin with antiproliferative activity from the medicinal mushroom Pholiota adiposa

Purification and characterization of a novel laccase from the mushroom Pleurotus nebrodensis

A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa

Purification and characterization of an antibacterial protein from dried fruiting bodies of the wild mushroom Clitocybe synopica

Purification and characterization of a novel metalloprotease from fruiting bodies of Oudemansiella radicata

Characterization of an acidic Alpha-galactosidase from hemp (Cannabis sativa L.) seeds and its application in removal of raffinose family oligosaccharides (RFOs)