壳聚糖对漆酶的固定化研究
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摘要
为了掌握固定化漆酶对不同种类苹果酚类化合物生物催化的特异性,本文以白腐菌漆酶为试材,采用分光光度法等手段,对白腐菌漆酶的特性进行了研究,并首次应用于苹果果胶液多酚的去除脱色,试验结果如下:
(1)游离漆酶催化儿茶素、绿原酸的转化,产物的最大吸收波长分别为442、379nm;反应最适温度均为55℃;最适pH对儿茶素在pH6.0,pH6.5两个点,对绿原酸为pH5.5,pH6.0两个值;儿茶素浓度0.5mol L-1时,最适酶浓度为0.05U mL-1。2种底物的漆酶催化反应均符合米氏方程规律,在标准条件(25℃温度)下测得儿茶素和绿原酸两种底物的Km值分别为0.1489,0.3390mol L-1;Vmax分别为212.77,28.01δA U-1 min-1。
(2)用壳聚糖固定化漆酶,单因素试验表明戊二醛(交联剂)的最适浓度5%,交联时间8h,最适的pH为5.5,最适酶浓度1U/ml,固定化酶的最适温度为55℃;用JMP7.0软件对单因素中影响较为显著的戊二醛浓度,酶浓度,pH3因素进行了相应曲面法的试验设计和处理后,得最适的戊二醛浓度,酶浓度,pH分别4.9694%, 1.0096U/ml,和5.4942。最适反应条件固定化漆酶的重复使用次数试验表明,经壳聚糖固定化的漆酶重复使用6次,相对酶活仍能保持70%以上。
(3)通过固定化漆酶对苹果果胶液除酚试验,结果表明,固定化酶对果胶中多酚的去除效率均高于游离酶对果胶中多酚的去除率,以40℃时酶的稳定性和对果胶的去除率最佳;固定化酶对酶的相对酶活力也均高于游离酶的相对酶活力;反应2h时,酶的相对活力较为稳定,尤其时40℃时明显高于游离酶的相对酶活力,具有在果胶工业化脱色中应用的潜力。
In order to learn the specific of bio-transformation of different apple phenolic compounds catalyzed by immobilized Laccase (Trametes versicolor). In this paper, white-rot fungus laccase characteristics were studied by spectrophotometry and other means, and applied to the apple pectin for removal of polyphenol decolorization for the first time, The trial results showed as follows:
1. The maximum absorption wavelength of laccase-catalyzed end-product for catechin and chlorogenic acid were 442,379 nm, respectively; optimum reaction temperatures were both 55℃; optimum pH were pH6.0 and pH6.5 for catechin,pH5.5 and pH6.0 for chlorogenic acid; enzyme concentration of 0.05U mL-1 was the most efficient for 0.5 mol·L-1 catechin. And laccase catalyzed bio-transformation for both substrates fitted the Michaelis-Menten equation. Under the standand reaction (25℃), km values for catechin and chlorogenic acid were 0.1489,0.3390mol L-1, respectively; Vmax values were 212.77,28.01δA*(U*min)-1, respectively.
2. Chitosan immobilized laccase with glutaraldehyde. The results indicated that the optimized conditions of immobilization of laccase could be specified as: pH 5.5, 0.2g Chitosan microspheres was activated by 5% glutaraldehyde for 8h,then added 1U/ml laccase to immobilize for 8h in the temperature of 50℃.By the analysis method of Response surface methodology(RSM),the resultd indicated that activity,concentration of glutaraldehyde, amount of enzyme, and pH were 4.9694%, 1.0096U/ml, and 5.4942 ,respectively.
3. The application of chitosan immobilized laccases in the removal of polyphenol of apple pectin was studied in this article. Experiments showed that the polyphenol of apple pectin dealed with chitosan immobilized laccase in the optimized temperature 40'C for 2h decreased15%,while enzyme activity did not vary which indicated immobilized lactase was more stable than free enzyme. Therefore chitosan immobilized laccase had potential application in industrialized production of apple pectin.
(1)游离漆酶催化儿茶素、绿原酸的转化,产物的最大吸收波长分别为442、379nm;反应最适温度均为55℃;最适pH对儿茶素在pH6.0,pH6.5两个点,对绿原酸为pH5.5,pH6.0两个值;儿茶素浓度0.5mol L-1时,最适酶浓度为0.05U mL-1。2种底物的漆酶催化反应均符合米氏方程规律,在标准条件(25℃温度)下测得儿茶素和绿原酸两种底物的Km值分别为0.1489,0.3390mol L-1;Vmax分别为212.77,28.01δA U-1 min-1。
(2)用壳聚糖固定化漆酶,单因素试验表明戊二醛(交联剂)的最适浓度5%,交联时间8h,最适的pH为5.5,最适酶浓度1U/ml,固定化酶的最适温度为55℃;用JMP7.0软件对单因素中影响较为显著的戊二醛浓度,酶浓度,pH3因素进行了相应曲面法的试验设计和处理后,得最适的戊二醛浓度,酶浓度,pH分别4.9694%, 1.0096U/ml,和5.4942。最适反应条件固定化漆酶的重复使用次数试验表明,经壳聚糖固定化的漆酶重复使用6次,相对酶活仍能保持70%以上。
(3)通过固定化漆酶对苹果果胶液除酚试验,结果表明,固定化酶对果胶中多酚的去除效率均高于游离酶对果胶中多酚的去除率,以40℃时酶的稳定性和对果胶的去除率最佳;固定化酶对酶的相对酶活力也均高于游离酶的相对酶活力;反应2h时,酶的相对活力较为稳定,尤其时40℃时明显高于游离酶的相对酶活力,具有在果胶工业化脱色中应用的潜力。
In order to learn the specific of bio-transformation of different apple phenolic compounds catalyzed by immobilized Laccase (Trametes versicolor). In this paper, white-rot fungus laccase characteristics were studied by spectrophotometry and other means, and applied to the apple pectin for removal of polyphenol decolorization for the first time, The trial results showed as follows:
1. The maximum absorption wavelength of laccase-catalyzed end-product for catechin and chlorogenic acid were 442,379 nm, respectively; optimum reaction temperatures were both 55℃; optimum pH were pH6.0 and pH6.5 for catechin,pH5.5 and pH6.0 for chlorogenic acid; enzyme concentration of 0.05U mL-1 was the most efficient for 0.5 mol·L-1 catechin. And laccase catalyzed bio-transformation for both substrates fitted the Michaelis-Menten equation. Under the standand reaction (25℃), km values for catechin and chlorogenic acid were 0.1489,0.3390mol L-1, respectively; Vmax values were 212.77,28.01δA*(U*min)-1, respectively.
2. Chitosan immobilized laccase with glutaraldehyde. The results indicated that the optimized conditions of immobilization of laccase could be specified as: pH 5.5, 0.2g Chitosan microspheres was activated by 5% glutaraldehyde for 8h,then added 1U/ml laccase to immobilize for 8h in the temperature of 50℃.By the analysis method of Response surface methodology(RSM),the resultd indicated that activity,concentration of glutaraldehyde, amount of enzyme, and pH were 4.9694%, 1.0096U/ml, and 5.4942 ,respectively.
3. The application of chitosan immobilized laccases in the removal of polyphenol of apple pectin was studied in this article. Experiments showed that the polyphenol of apple pectin dealed with chitosan immobilized laccase in the optimized temperature 40'C for 2h decreased15%,while enzyme activity did not vary which indicated immobilized lactase was more stable than free enzyme. Therefore chitosan immobilized laccase had potential application in industrialized production of apple pectin.
引文
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