碩士 / 國立海洋大學 / 食品科學系 / 91 / Abstract
An amylase was purified from the viscera of Ruditapes variegates by ammonium sulfate fractionation, Sepharose CL-6B and DEAE-Sephadex A-50 columns. By these steps, the purification of this enzyme increased to 197 fold and the recovery of this enzyme activity was 4%. According to Disc-PAGE (native), the purified amylase appeared a single protein band. The molecular weight was 24 kDa of this amylase by Sephadex G150 column. This amylase could digest amylopectin and glycogen to product glucose, maltose, maltotriose and maltotetraose. The optimal temperature of this enzyme was 37.5oC. The optimal pH of this amylase for digesting the soluble starch, under the optimal temperature, was found to be 7.0. This amylase was activated by Ba2+, Mg2+, Ca2+ ions, but completely inhibited by Al3+, Fe3+, Ni2+, Cu2+, Cd2+, Hg2+, Zn2+ ions. The inhibitors, EDTA and DTNB were also found to have partially inhibited ability on this enzyme.
| Identifer | oai:union.ndltd.org:TW/091NTOU0253029 |
| Date | January 2003 |
| Creators | P0-Yang Hsu, 許博揚 |
| Contributors | Ching-Yu Tsao, 曹欽玉 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 80 |
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