球形交联壳聚糖固定化风味蛋白酶的制备及特性研究.doc

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球形交联壳聚糖固定化风味蛋白酶的制备及特性研究,摘要:研究了球形交联壳聚糖固定化风味蛋白酶的制备及其特性,以壳聚糖为载体,戊二醛为交联剂制备固定化风味蛋白酶,测定了不同戊二醛浓度、交联时间、给酶量、固定化时间、固定化温度及固定化ph对固定化风味蛋白酶酶活性的影响。结果表明:固定化反应的最佳条件为戊二醛浓度0.5%,交联时...
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球形交联壳聚糖固定化风味蛋白酶的制备及特性研究

摘要:研究了球形交联壳聚糖固定化风味蛋白酶的制备及其特性,以壳聚糖为载体,戊二醛为交联剂制备固定化风味蛋白酶,测定了不同戊二醛浓度、交联时间、给酶量、固定化时间、固定化温度及固定化pH对固定化风味蛋白酶酶活性的影响。结果表明:固定化反应的最佳条件为戊二醛浓度0.5%,交联时间6h,给酶量40mg/g载体 ,固定化时间10h,固定化pH5.5,固定化温度35℃。在此条件下制备的固定化风味蛋白酶机械强度最大,酶活回收率最高,固定化酶的pH稳定性与温度稳定性均得到提高,连续使用11次后固定化酶活力还剩余56.7%。
关键词:风味蛋白酶,固定化,球形交联壳聚糖,特性

Study on Preparation and Properties of Immobilized FlavourzymeonGlobular Cross-linked Chitosan
Abstract:The preparation and properties of immobilized flavourzymeon globular cross-linked chitosanwere investigated.Flavourzyme has been immobilized on chitosan with glutaraldehyde as crosslinking agent. The effects on the activity of immobilized flavourzyme, such as crosslinking time, concentration of glutaraldehyde,flavourzyme dosage, reaction time, reaction temperature and reaction pH were studied. The results showed that the optimal conditions of immobilization: the optimal concentration of glutaraldehyde was 0.5%, the optimal flavourzyme dosage was 40mg/g carrier, the optimal reaction time, temperature and pH were 6h, 35℃ and 5.5 respectively. Under the optimal conditions, the immobilized flavourzyme have the best mechanical strength and the highest enzyme recovery, the pH and temperature stability were considerably improved. The recovery activity of immobilized flavourzyme was more than 66.1% after being repeated eleven times.

Key words:flavourzyme; immobilization; globular cross-linked chitosan; properties

目录
中文摘要.............................................................................................................................1中文关键词.........................................................................................................................1英文摘要............................................................................................................................ 1英文关键词.........................................................................................................................1 1前言..................................................................................................................................2
1.1壳聚糖的应用………………………………………………………………………...2
1.2固定化酶的主要方法……………………………………………………………...…2
1.3风味蛋白酶………………………………………………………………………...…4
2 材料与方法.....................................................................................................................5
2.1材料...............................................................................................................................5
2.2仪器...............................................................................................................................5
2.3方法...............................................................................................................................5
3结果与分析......................................................................................................................5
3.1.壳聚糖固定化风味酶的最佳条件选则.......................................................................5
3.1.1NaOH浓度和壳聚糖浓度的影响.............................................................................6
3.1.2戊二醛浓度和交联时间的影响................................................................................6
3.1.3给酶量对固定化酶活性的影响................................................................................7
3.1.4 固定化反应时间的影响...........................................................................................8
3.1.5 固定化体系温度和ph的影响.................................................................................9
3.2 球形交联壳蛋白固定化风味酶的特性....................................................................10
3.2.1固定化酶的最佳反应ph.........................................................................................11
3.2.2固定化酶的最佳反应温度......................................................................................11
3.2.3固定化酶的储存稳定性..........................................................................................12
3.2.4固定化酶的操作稳定性..........................................................................................12
4结论................................................................................................................................14
参考文献...........................................................................................................................15
致 谢......................................................................................