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Title: | 黑黴菌細胞內α-澱粉水解酵素的純化及特性鑑定 The purification and characterization of Intracelluar α-amylase from Aspergillus niger |
Authors: | Pu-Cheng Chen 陳浦城 |
Publication Year : | 1988 |
Degree: | 碩士 |
Abstract: | 由黑黴菌(Aspergillus niger)自體消化的溶液中可純化出兩種細胞內α-澱粉水解酵素(E.C. 3.2.1.1.)所使用的純化步驟如下: (l)培養黑黴菌。(2)從細胞自體消化液抽取粗酵素。(3) 以DEAE-cellulose初步分離。(4) Sephadex G-75柱體分離。經上述步驟可得到6.5%的回收率。 經純化的酵素依其對基質的特異性和分子量的測定,鑑定出有兩個α-澱粉水解酵素,其中一個分子量為六萬五,在pH2時仍具有活性,在此稱之為抗酸性α-澱粉水解酵素。因抗酸性α-澱粉水解酵素純化時無法避免葡萄糖澱粉水解酵素(glucoamylases, E.C. 3.2.1.3)的汙染,所以抗酸性α-澱粉水解酵素的特性只能做到部分純化。 另一個α-澱粉水解酵素分子量為五萬三,在pH<4時易失去活性,在此稱之為酸敏感α-澱粉水解酵素,其最佳反應的pH範圍為pH 4.5-5.5,而穩定性則在 pH 5-9。 Two intracellular α-amylases from Aspergillus niger were purifiei. The processes involve: (a) Cellular autolysis. (b) DEAE-cellulose fractionation, (c) Sephadex G-75 filtration and (d) DEAE-cellulose fractionation. α-amylases have molecular weight of 53,000 and 65,000 as measured by poly-acrylamide gel electrophoresis in the present of sodium dodecyl sulfate. The smaller one is a single homogenous polypeptide and acid sensitive. The larger one is acid-stable and contains gluco-amylase. Both α-amylases catalyze hydrolysis of starch into oligosaccharides. |
URI: | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75663 |
Fulltext Rights: | 未授權 |
Appears in Collections: | 生化科學研究所 |
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