Institutional Repository of Key Laboratory of Coastal Zone Environmental Processes, Yantai Institute of Coastal Zone Research, Chinese Academy of Sciences (KLCEP)
| Cellulase immobilization properties and their catalytic effect on cellulose hydrolysis in ionic liquid | |
| Su, Zhongliang1,2; Yang, Xingyu1; Luli1; Shao, Hongbo1,2; Yu, Shitao1 | |
| 发表期刊 | AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH
 |
| ISSN | 1996-0808 |
| 2012-01-09 | |
| 卷号 | 6期号:1页码:64-70 |
| 关键词 | Renewable Energy Cellulose Immobilization Chitosan Cellulose Ionic Liquids |
| 产权排序 | [Su, Zhongliang; Yang, Xingyu; Luli; Shao, Hongbo; Yu, Shitao] QUST, Inst Life Sci, Coll Chem Engn, Qingdao 266042, Peoples R China; [Su, Zhongliang; Shao, Hongbo] Chinese Acad Sci, Yantai Inst Coastal Zone Res, CAS Shandong Prov Key Lab Coastal Environm Proc, Yantai 264003, Peoples R China |
| 通讯作者 | Shao, HB (reprint author), QUST, Inst Life Sci, Coll Chem Engn, Qingdao 266042, Peoples R China.,shaohongbochu@126.com |
| 作者部门 | 中科院海岸带环境过程与生态修复重点实验室 |
| 英文摘要 | Cellulase was immobilized on chitosan by the method of covalent binding. The optimum immobilized conditions were as follow: the pH value was 5.0, the glutaraldehyde concentration was 0.015 (w/v) and the formaldehyde concentration was 0.15 (w/v). Both the free and immobilized cellulase were characterized by determining the pH, temperature, thermal stability and storage stability. The optimum pH of both the free and immobilized cellulase was found as 4. The immobilized cellulase had optimum temperature of 50 degrees C as compared to 40 degrees C in case of free enzyme. The immobilized enzyme showed higher thermal stability than the free cellulase, after 120 min, the activity of immobilized cellulose and the free enzyme retained 86.5 and 61% respectively. After 11 cycles, the activity of the immobilize enzyme conserved 80.27%. The immobilized enzyme exhibited slightly better storage stability than the free enzyme. The Km and Vm values for the immobilized and free cellulase were 8.1 and 1.84 mg/L and 0.01 and 0.0036 mg/ml/min respectively. Cellulose hydrolysis by immobilized cellulase in the presence of a 88 ionic liquid (IL), 1,3-dimethylimidazolium dimethylphosphate (MMIM-DMP), was investgated. The result showed that the addition of 20% (v/v) MMIM-DMP gave the highest initial rate, which was 1.3 and 13.9 times higher than the hydrolysis rate in citric acid - sodium hydrogen phosphate buffer and in IL, respectively.; Cellulase was immobilized on chitosan by the method of covalent binding. The optimum immobilized conditions were as follow: the pH value was 5.0, the glutaraldehyde concentration was 0.015 (w/v) and the formaldehyde concentration was 0.15 (w/v). Both the free and immobilized cellulase were characterized by determining the pH, temperature, thermal stability and storage stability. The optimum pH of both the free and immobilized cellulase was found as 4. The immobilized cellulase had optimum temperature of 50 degrees C as compared to 40 degrees C in case of free enzyme. The immobilized enzyme showed higher thermal stability than the free cellulase, after 120 min, the activity of immobilized cellulose and the free enzyme retained 86.5 and 61% respectively. After 11 cycles, the activity of the immobilize enzyme conserved 80.27%. The immobilized enzyme exhibited slightly better storage stability than the free enzyme. The Km and Vm values for the immobilized and free cellulase were 8.1 and 1.84 mg/L and 0.01 and 0.0036 mg/ml/min respectively. Cellulose hydrolysis by immobilized cellulase in the presence of a 88 ionic liquid (IL), 1,3-dimethylimidazolium dimethylphosphate (MMIM-DMP), was investgated. The result showed that the addition of 20% (v/v) MMIM-DMP gave the highest initial rate, which was 1.3 and 13.9 times higher than the hydrolysis rate in citric acid - sodium hydrogen phosphate buffer and in IL, respectively. |
| 文章类型 | Article |
| 资助机构 | National Natural Science Foundation of China[31070520, 30900126]; Universities Technology Plan of Shandong[J09LG16]; One Hundred-Talent Plan of Chinese Academy of Sciences (CAS); CAS/SAFEA International Partnership Program for Creative Research Teams-Typical Environmental Processes |
| 收录类别 | SCI |
| 语种 | 英语 |
| 关键词[WOS] | ENZYME IMMOBILIZATION ; HORSERADISH-PEROXIDASE ; STABILITY ; CHITOSAN ; ENTRAPMENT ; SUPPORT ; MEDIA |
| 研究领域[WOS] | Microbiology |
| WOS记录号 | WOS:000306316000011 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.yic.ac.cn/handle/133337/5970 |
| 专题 | 中国科学院海岸带环境过程与生态修复重点实验室 |
| 作者单位 | 1.QUST, Inst Life Sci, Coll Chem Engn, Qingdao 266042, Peoples R China 2.Chinese Acad Sci, Yantai Inst Coastal Zone Res, CAS Shandong Prov Key Lab Coastal Environm Proc, Yantai 264003, Peoples R China |
| 推荐引用方式 GB/T 7714 | Su, Zhongliang,Yang, Xingyu,Luli,et al. Cellulase immobilization properties and their catalytic effect on cellulose hydrolysis in ionic liquid[J]. AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH,2012,6(1):64-70. |
| APA | Su, Zhongliang,Yang, Xingyu,Luli,Shao, Hongbo,&Yu, Shitao.(2012).Cellulase immobilization properties and their catalytic effect on cellulose hydrolysis in ionic liquid.AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH,6(1),64-70. |
| MLA | Su, Zhongliang,et al."Cellulase immobilization properties and their catalytic effect on cellulose hydrolysis in ionic liquid".AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH 6.1(2012):64-70. |
| 条目包含的文件 | 下载所有文件 | |||||
| 文件名称/大小 | 文献类型 | 版本类型 | 开放类型 | 使用许可 | ||
| Cellulase immobiliza（82KB） | 开放获取 | -- | 浏览 下载 | |||
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。
修改评论