Study on immobilized glucoamylase on bacterial cellulose
碩士 === 輔英科技大學 === 生物技術系碩士班 === 95 === Abstract Glucoamylase was immobilized onto bacterial cellulose bead activated with five different methods. The immobilized glucoamylase presented better performance than free enzyme when submitted to heat treatment, showing a 10 ◦C decrease on the optimal...
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ndltd-TW-095FY0051080052015-10-13T14:13:12Z http://ndltd.ncl.edu.tw/handle/30273159906412678169 Study on immobilized glucoamylase on bacterial cellulose 澱粉葡萄糖化酵素固定在細菌纖維素之研究 Ying-ke Lia 賴盈課 碩士 輔英科技大學 生物技術系碩士班 95 Abstract Glucoamylase was immobilized onto bacterial cellulose bead activated with five different methods. The immobilized glucoamylase presented better performance than free enzyme when submitted to heat treatment, showing a 10 ◦C decrease on the optimal assay temperature. The optimum condition such as reaction pH is 4.5and free enzyme is pH 5. The immobilization enhanced the enzyme stability against changes of pH value and temperature. The activity of immobilized enzyme was also improved 15% by optimal 1,4-butanediyl diglycidyl ether concentaration. The Km value of free enzyme for starch (3.025 g/L) was higher than that of the immobilized enzyme (2.667 g/L)﹒ Finally﹐the enzyme was also immobilized on bacterial cellulose by periodate oxidation mothod and the optimal conditions was searched. In the optimum temperature, the method performed equally with that of the preceding method. Moreover﹐the activity of immobilized enzyme retained more than 95% of relative activity when the immobilization was performed during pH3-5. Sheng-chi Wu 吳聲祺 2007 學位論文 ; thesis 84 zh-TW |
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碩士 === 輔英科技大學 === 生物技術系碩士班 === 95 === Abstract
Glucoamylase was immobilized onto bacterial cellulose bead activated with five different methods. The immobilized glucoamylase presented better performance than free enzyme when submitted to heat treatment, showing a 10 ◦C decrease on the optimal assay temperature. The optimum condition such as reaction pH is 4.5and free enzyme is pH 5. The immobilization enhanced the enzyme stability against changes of pH value and temperature. The activity of immobilized enzyme was also improved 15% by optimal 1,4-butanediyl diglycidyl ether concentaration. The Km value of free enzyme for starch (3.025 g/L) was higher than that of the immobilized enzyme (2.667 g/L)﹒
Finally﹐the enzyme was also immobilized on bacterial cellulose by periodate oxidation mothod and the optimal conditions was searched. In the optimum temperature, the method performed equally with that of the preceding method. Moreover﹐the activity of immobilized enzyme retained more than 95% of relative activity when the immobilization was performed during pH3-5.
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author2 |
Sheng-chi Wu |
author_facet |
Sheng-chi Wu Ying-ke Lia 賴盈課 |
author |
Ying-ke Lia 賴盈課 |
spellingShingle |
Ying-ke Lia 賴盈課 Study on immobilized glucoamylase on bacterial cellulose |
author_sort |
Ying-ke Lia |
title |
Study on immobilized glucoamylase on bacterial cellulose |
title_short |
Study on immobilized glucoamylase on bacterial cellulose |
title_full |
Study on immobilized glucoamylase on bacterial cellulose |
title_fullStr |
Study on immobilized glucoamylase on bacterial cellulose |
title_full_unstemmed |
Study on immobilized glucoamylase on bacterial cellulose |
title_sort |
study on immobilized glucoamylase on bacterial cellulose |
publishDate |
2007 |
url |
http://ndltd.ncl.edu.tw/handle/30273159906412678169 |
work_keys_str_mv |
AT yingkelia studyonimmobilizedglucoamylaseonbacterialcellulose AT làiyíngkè studyonimmobilizedglucoamylaseonbacterialcellulose AT yingkelia diànfěnpútáotánghuàjiàosùgùdìngzàixìjūnxiānwéisùzhīyánjiū AT làiyíngkè diànfěnpútáotánghuàjiàosùgùdìngzàixìjūnxiānwéisùzhīyánjiū |
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