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Farjana Nikkon,M. Rowshanul Habib,M. Rezaul Karim,M. Shamim Hossain,M. Ashik Mosaddik,M. Ekramul Haque The Korean Society of Mycology 2008 Mycobiology Vol.36 No.3
The crude ethanol extracts (stem and fruits), their fractions and two triterpenes, β-Amyrin and 12-Oleanene 3β, 21β-diol, isolated as a mixture from the chloroform soluble fraction of an ethanolic extract of Duranta repens stem, were evaluated for antibacterial, antifungal activities by the disc diffusion method and cytotoxicity by brine shrimp lethality bioassay. The structures of the two compounds were confirmed by IR, 1H-NMR, 13C-NMR and LC-MS spectral data. The chloroform soluble fraction of stem and ethanol extract of fruits possess potent antishigellosis activity and also exhibited moderate activity against some pathogenic bacteria and fungi but the isolated compound 1 (mixture of β-Amyrin and 12-Oleanene 3β, 21β-diol) showed mild to moderate inhibitory activity to microbial growth. The minimum inhibitory concentrations (MICs) of the extracts (stem and fruits), their fractions and compound 1 were found to be in the range of 32~128 μg/ml. The chloroform soluble fractions of stem and ethanol extract of fruit showed significant cytotoxicity with LC50 value of 0.94 μg/ml and 0.49 μg/ml, respectively against brine shrimp larvae.
Purification, Characterization, and Biochemical Properties of α-Amylase from Potato
( Goutam Kumar Sarker ),( Sohel Hasan ),( Farjana Nikkon ),( Ashik Mosaddik ),( Niranjan Kumar Sana ),( Habibur Rahman ),( Sang Gyu Park ),( Dong Sun Lee ),( Somi Kim Cho ) 한국응용생명화학회 2010 Applied Biological Chemistry (Appl Biol Chem) Vol.53 No.1
Purification, characterization and biochemical properties of α-amylase from post harvest Bangladeshi Potato (Solanum tuberosum L.) were investigated. The α-amylase was purified by successive chromatography on DEAE and CM-cellulose columns with a yield of 24.24%. SDS-PAGE showed a molecular weight of 44 kDa for the enzyme that contain 2.8% sugar. The enzyme lost total activity in the presence of the chelating agent EDTA, confirming it was an α-type amylase. The enzyme displayed optimum activity at pH 7.2 and 37˚C, with an apparent Km value of 0.26% using starch as its substrate. The enzyme was strongly inhibited by Cu2+, Fe2+ and Zn2+; moderately by Li+, Hg+ and Cd2+; and slightly by Ag+, K+, Mn2+ and Mg2+. Conversely, Fe3+ and Na+ appreciably enhanced activity, while adding calcium ion nearly doubled enzyme activity. In addition, the activity of α-amylase gradually decreased with increasing concentrations of urea. Thus, potato α-amylase is an attractive target for study to better understand the structure-function relationships of α-amylases.
Biochemistry : Purification, Characterization, and Biochemical Properties of α-Amylase from Potato
Goutam Kumar Sarker,Sohel Hasan,Farjana Nikkon,Ashik Mosaddik,Niranjan Kumar Sana,Habibur Rahman,Sang Gyu Park,Dong Sun Lee,So Mi Kim Cho 한국응용생명화학회 2010 Journal of Applied Biological Chemistry (J. Appl. Vol.53 No.1
Purification, Characterization, and Biochemical Properties of $\alpha$-Amylase from Potato
Sarker, Goutam Kumar,Hasan, Sohel,Nikkon, Farjana,Mosaddik, Ashik,Sana, Niranjan Kumar,Rahman, Habibur,Park, Sang-Gyu,Lee, Dong-Sun,Cho, So-Mi Kim The Korean Society for Applied Biological Chemistr 2010 Applied Biological Chemistry (Appl Biol Chem) Vol.53 No.1
Purification, characterization and biochemical properties of $\alpha$-amylase from post harvest Bangladeshi Potato (Solanum tuberosum L.) were investigated. The $\alpha$-amylase was purified by successive chromatography on DEAE and CM-cellulose columns with a yield of 24.24%. SDSPAGE showed a molecular weight of 44 kDa for the enzyme that contain 2.8% sugar. The enzyme lost total activity in the presence of the chelating agent EDTA, confirming it was an $\alpha$-type amylase. The enzyme displayed optimum activity at pH 7.2 and $37^{\circ}C$, with an apparent Km value of 0.26% using starch as its substrate. The enzyme was strongly inhibited by $Cu^{2+},\;Fe^{2+}$ and $Zn^{2+}$; moderately by $Li^+,\;Hg^+$ and $Cd^{2+}$; and slightly by $Ag^+,\;K^+,\;Mn^{2+}$ and $Mg^{2+}$. Conversely, $Fe%{3+}$ and $Na^+$ appreciably enhanced activity, while adding calcium ion nearly doubled enzyme activity. In addition, the activity of $\alpha$-amylase gradually decreased with increasing concentrations of urea. Thus, potato $\alpha$-amylase is an attractive target for study to better understand the structure-function relationships of $\alpha$-amylases.