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OGAN, AYŞE

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OGAN

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AYŞE

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2006 - 200912010 - 20141
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End date: 2019 × Subject: alpha-amylase ×

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    Soybean oil based resin: A new tool for improved immobilization of alpha-amylase
    (WILEY, 2006) OGAN, AYŞE; Kahraman, MV; Kayaman-Apohan, N; Ogan, A; Gungor, A
    Acrylated epoxidized soybean resin has been utilized to immobilize the alpha-amylase via UV-curing technique. Among the numerous methods that exist for enzyme immobilization, entrapment and covalent binding are the focus of this study. The properties of immobilized enzyme were investigated and compared with those of the free enzyme. Upon immobilization by the two methods, the catalytic properties of the enzyme were not considerably changed as compared with that of nonimmobilized form; enzyme. The free enzyme lost its activity completely in 20 days, where as storage and repeated usage capability experiments demonstrated higher stability for the immobilized form. Immobilized enzyme prepared by attachment method possesses relatively higher activity compared with the activity of those obtained by entrapment method. (c) 2006 Wiley Periodicals, Inc.
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    A Maltooligosaccharides Producing alpha-Amylase from Bacillus subtilis SDP1 Isolated from Rhizosphere of Acacia cyanophylla Lindley
    (TAYLOR & FRANCIS INC, 2014) OGAN, AYŞE; Ozturk, Hasan Umit; Denizci, Aziz Akin; Ogan, Ayse; Kazan, Dilek
    Maltooligosaccharides producing amylases are required in the food industry, especially in breadmaking. The Bacillus subtilis strain SDP1 amylase hydrolyses starch to produce maltotriose and maltotetraose along with maltose after prolonged reactions of 5 h. Bacillus subtilis strain SDP1 was isolated from the rhizosphere of Acacia cyanophylla Lindley from the cukurova region of Turkey. The highest enzyme production was achieved with soluble starch as the carbon and yeast extract as the nitrogen source and at pH 7.0 and 37 degrees C. Under optimized culture conditions, 68.49 U/mL activity was obtained. SDP1 alpha-amylase had molecular weight of 61 kD. The optimum pH of the enzyme was 7.0 and was highly active at pH ranging from 5.0 to 9.0. The optimum temperature of the crude enzyme was 60 degrees C, and it retained 83% and 74% of its initial activity after 1 h and 2 h incubation periods, respectively, at 50 degrees C. While, Mn+2 has a stimulatory effect on the activity, Ca+2, Mg+2, Na+ did not effect the enzyme activity. Fe+3, Ni+2, Cu+2 and Co+2 had an inhibitory effect on SDP1 amylase activity.