细菌纤维素微球固定化α-淀粉酶的研究  

Immobilization ofα-amylase on bacterial cellulose pellets

作　　者：赵昆[1] 张良[2] 沈才洪[2] 胡承[1] 

机构地区：[1]四川大学生命科学学院生物资源与生态环境教育部重点实验室,成都610064 [2]泸州老窖股份有限公司,泸州646000

出　　处：《四川大学学报（自然科学版）》2011年第1期213-218,共6页Journal of Sichuan University(Natural Science Edition)

基　　金：科技部其它项目(2005DKA21208-7)

摘　　要：由本实验室分离保存的葡糖醋杆菌(Gluconacetobacter intermedius)G-29摇瓶培养产生的细菌纤维素微球作为载体,采用戊二醛交联法固定化α-淀粉酶.通过正交实验确定了固定化的最佳条件:pH 6.4,3%戊二醛浓度,给酶量12.5 mL(1 mg/mL),固定化时间12 h.研究了固定化酶的性质,与游离酶相比,α-淀粉酶经细菌纤维素微球固定化后,抗酸碱和温度变化的能力提高,最适pH向酸性区偏移0.4个单位(从6.0降到5.6),最适温度升高10℃(从60℃升高到70℃),并在较宽的pH和温度范围内也能保持较高的活性,保藏性和重复使用性较稳定,说明细菌纤维素微球在工业上作为酶载体支持物有较大潜力.Bacterial cellulose pellets were produced in shaking flasks by Gluconacetobacter interrnedius G- 29 which was isolated and preserved by our laboratory. Activated bacterial cellulose pellets by the method of glutaraldehyde cross-linking were used as the support of a-amylase for its immobilization. The optimal conditions for immobilization were determined by orthogonal experiment, the result was as following. pH 6.4, 3% of glutaraldehyde concentration, 12.5 mL（1 mg/mL） of enzyme amount, 12 h. The properties of free and immobilized a-amylase were also investigated and compared, the optimal pH of im- mobilized a-amylase was descended by 0.4 to the acid region （from 6.0 to 5.6） arid the optimal temperature was 70 ℃, 10 ℃ higher than that of free α-amylase, immobilized a-amylase could maintain high activity in a wider range of pH and temperature; the operational and storage stability of immobilized α-am- ylase were improved significantly. We can infer that the bacterial cellulose pellets have the potential to be used as a new support for enzyme immobilization in industry.

关 键 词：细菌纤维素微球 Α-淀粉酶 固定化 戊二醛 

分 类 号：Q93[生物学—微生物学]